<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE article PUBLIC "-//NLM//DTD JATS (Z39.96) Journal Publishing DTD v1.3 20210610//EN" "JATS-journalpublishing1-3.dtd">
<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">chemicallytech</journal-id><journal-title-group><journal-title xml:lang="en">Fine Chemical Technologies</journal-title><trans-title-group xml:lang="ru"><trans-title>Тонкие химические технологии</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2410-6593</issn><issn pub-type="epub">2686-7575</issn><publisher><publisher-name>MIREA – Russian Technological University (RTU MIREA).</publisher-name></publisher></journal-meta><article-meta><article-id custom-type="elpub" pub-id-type="custom">chemicallytech-448</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>CHEMISTRY AND TECHNOLOGY OF MEDICINAL COMPOUNDS AND BIOLOGICALLY ACTIVE SUBSTANCES</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>ХИМИЯ И ТЕХНОЛОГИЯ ЛЕКАРСТВЕННЫХ ПРЕПАРАТОВ И БИОЛОГИЧЕСКИ АКТИВНЫХ СОЕДИНЕНИЙ</subject></subj-group></article-categories><title-group><article-title>Structural biology of lipoxygenases: current knowledge and further development</article-title><trans-title-group xml:lang="ru"><trans-title>Структурная биология липоксигеназ: настоящее и перспективы развития</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Иванов</surname><given-names>И. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Ivanov</surname><given-names>I. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>кафедра Химии и технологии биологически активных соединений им. Н.А. Преображенского, научный сотрудник</p></bio><email xlink:type="simple">igor_ivanov@gmx.de</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Гроза</surname><given-names>Н. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Groza</surname><given-names>N. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>кафедра Химии и технологии биологически активных соединений им. Н.А. Преображенского, ассистент</p></bio><email xlink:type="simple">noemail@neicon.ru</email><xref ref-type="aff" rid="aff-2"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Мягкова</surname><given-names>Г. И.</given-names></name><name name-style="western" xml:lang="en"><surname>Myagkova</surname><given-names>G. I.</given-names></name></name-alternatives><bio xml:lang="ru"><p>кафедра Химии и технологии биологически активных соединений им. Н.А. Преображенского, ведущий научный сотрудник</p></bio><email xlink:type="simple">noemail@neicon.ru</email><xref ref-type="aff" rid="aff-2"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Кюн</surname><given-names>Х. .</given-names></name><name name-style="western" xml:lang="en"><surname>Kühn</surname><given-names>H.</given-names></name></name-alternatives><bio xml:lang="ru"><p>профессор</p></bio><email xlink:type="simple">noemail@neicon.ru</email><xref ref-type="aff" rid="aff-3"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Институт токсикологии и фармакологии, Медицинский университет г. Ростока,&#13;
Росток, D-18057 Германия; МИТХТ им. М.В. Ломоносова, 119571, Москва, пр-т Вернадского, д. 86</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Institute of Biochemistry, Medicine University Berlin-Charité, D-10117 Berlin, Germany; M.V. Lomonosov Moscow State University of Fine Chemical Technologies, 86, Vernadskogo pr., Moscow 119571</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-2"><aff xml:lang="ru"><institution>МИТХТ им. М.В. Ломоносова, 119571, Москва, пр-т Вернадского, д. 86</institution><country>Россия</country></aff><aff xml:lang="en"><institution>M.V. Lomonosov Moscow State University of Fine Chemical Technologies, 86, Vernadskogo pr., Moscow 119571</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-3"><aff xml:lang="ru"><institution>Институт биохимии, Медицинский университет Шарите,&#13;
Берлин, D-10115</institution><country>Германия</country></aff><aff xml:lang="en"><institution>Institute of Pharmacology and Toxycology, Medicine University of Rostock, D-18057 Rostock</institution><country>Germany</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2014</year></pub-date><pub-date pub-type="epub"><day>28</day><month>08</month><year>2014</year></pub-date><volume>9</volume><issue>4</issue><fpage>3</fpage><lpage>26</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Ivanov I.V., Groza N.V., Myagkova G.I., Kühn H..., 2014</copyright-statement><copyright-year>2014</copyright-year><copyright-holder xml:lang="ru">Иванов И.В., Гроза Н.В., Мягкова Г.И., Кюн Х...</copyright-holder><copyright-holder xml:lang="en">Ivanov I.V., Groza N.V., Myagkova G.I., Kühn H.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://www.finechem-mirea.ru/jour/article/view/448">https://www.finechem-mirea.ru/jour/article/view/448</self-uri><abstract><p>Lipoxygenases (LOX) form a heterogeneous family of lipid peroxidizing enzymes, which have been implicated in the synthesis of inflammatory mediators. The involvement of LOX isoenzymes in regulation of physiological homeostasis and pathogenesis of various diseases with major health and political relevance made them potential targets for pharmacological intervention. Although the first plant lipoxygenase (soybean LOX1) was discovered more than 60 years ago, the structural aspects of these enzymes were not studied until the mid 1990s. For the time being the crystal structures of various lipoxygenase-isoforms have been reported, and X-ray coordinates for numerous enzyme-ligand complexes are also available. This review focuses on recent developments in molecular enzymology of LOX and summarizes our current knowledge on the structural basis of LOX catalysis. Hypotheses explaining the reaction specificity of different isoforms as well as evolutionary aspects are reviewed and discussed. As the review is mainly intended to cover thematic priorities, which have not been reviewed in the past, a detailed discussion of the biological function of LOX goes beyond the scope of this review.</p></abstract><trans-abstract xml:lang="ru"><p>Липоксигеназы (LOX) - ферменты перекисного окисления липидов - вовлечены в патогенез воспалительных и гиперпролиферативных реакций организма. Несмотря на то, что первая липоксигеназа растительного происхождения (LOX1 сои) была обнаружена более 60 лет назад, структурная биология этой группы ферментов не изучалась вплоть до середины 1990-ых годов. Данный обзор посвящен новейшим аспектам в области изучения молекулярной энзимологии липоксигеназ и обобщает существующие в настоящее время представления о структурных основах катализа с их участием. В обзоре рассмотрены различные гипотезы, объясняющие реакционную специфичность LOX, а также подведен промежуточный итог в области знания об эволюционном развитии этого класса ферментов в различных организмах. Несмотря на то, что биологическая роль LOX в низших организмах далеко не ясна, наличие в их ДНК последовательности LOX позволяет предположить, что семейство этих ферментов могло возникнуть сразу после появления атмосферного кислорода на Земле.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>липоксигеназа</kwd><kwd>структура</kwd><kwd>катализ</kwd><kwd>полиненасыщенные жирные кислоты</kwd><kwd>окисление</kwd></kwd-group><kwd-group xml:lang="en"><kwd>lipoxygenase</kwd><kwd>structure</kwd><kwd>catalysis</kwd><kwd>polyunsaturated fatty acids</kwd><kwd>oxygenation.</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Brash A.R. Lipoxygenases: Occurrence, functions, catalysis, and acquisition of substrate // J. Biol. Chem. 1999. V. 274. P. 23679-23682.</mixed-citation><mixed-citation xml:lang="en">Brash A.R. Lipoxygenases: Occurrence, functions, catalysis, and acquisition of substrate // J. Biol. Chem. 1999. V. 274. P. 23679-23682.</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Kuhn H., Saam J., Eibach S., Holzhutter H.G., Ivanov I., Walther M. Structural biology of mammalian lipoxygenases: Enzymatic consequences of targeted alterations of the protein structure // Biochem. Biophys. Res. Commun. 2005. V. 338. P. 93-101.</mixed-citation><mixed-citation xml:lang="en">Kuhn H., Saam J., Eibach S., Holzhutter H.G., Ivanov I., Walther M. Structural biology of mammalian lipoxygenases: Enzymatic consequences of targeted alterations of the protein structure // Biochem. Biophys. Res. Commun. 2005. V. 338. P. 93-101.</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Schneider C., Pratt D.A., Porter N.A., Brash A.R. Control of oxygenation in lipoxygenase and cyclooxygenase catalysis // Chem. Biol. 2007. V. 14. P. 473-488.</mixed-citation><mixed-citation xml:lang="en">Schneider C., Pratt D.A., Porter N.A., Brash A.R. Control of oxygenation in lipoxygenase and cyclooxygenase catalysis // Chem. Biol. 2007. V. 14. P. 473-488.</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Glickman M.H., Klinman J.P. Nature of rate-limiting steps in the soybean lipoxygenase-1 reaction // Biochemistry. 1995. V. 34. P. 14077-14092.</mixed-citation><mixed-citation xml:lang="en">Glickman M.H., Klinman J.P. Nature of rate-limiting steps in the soybean lipoxygenase-1 reaction // Biochemistry. 1995. V. 34. P. 14077-14092.</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Rickert K.W., Klinman J.P. Nature of hydrogen transfer in soybean lipoxygenase 1: Separation of primary and secondary isotope effects // Biochemistry. 1999. V. 38. P. 12218-12228.</mixed-citation><mixed-citation xml:lang="en">Rickert K.W., Klinman J.P. Nature of hydrogen transfer in soybean lipoxygenase 1: Separation of primary and secondary isotope effects // Biochemistry. 1999. V. 38. P. 12218-12228.</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Lehnert N., Solomon E.I. Density-functional investigation on the mechanism of H-atom abstraction by lipoxygenase // J. Biol. Inorg. Chem. 2003. V. 8. P. 294-305.</mixed-citation><mixed-citation xml:lang="en">Lehnert N., Solomon E.I. Density-functional investigation on the mechanism of H-atom abstraction by lipoxygenase // J. Biol. Inorg. Chem. 2003. V. 8. P. 294-305.</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Hatcher E., Soudackov A.V., Hammes-Schiffer S. Proton-coupled electron transfer in soybean lipoxygenase // J. Am. Chem. Soc. 2004. V. 126. P. 5763-5775.</mixed-citation><mixed-citation xml:lang="en">Hatcher E., Soudackov A.V., Hammes-Schiffer S. Proton-coupled electron transfer in soybean lipoxygenase // J. Am. Chem. Soc. 2004. V. 126. P. 5763-5775.</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Upston J.M., Neuzil J., Witting P.K., Alleva R., Stocker R. Oxidation of free fatty acids in low density lipoprotein by 15-lipoxygenase stimulates nonenzymic, alpha-tocopherol-mediated peroxidation of cholesteryl esters // J. Biol. Chem. 1997. V. 272. P. 30067-30074.</mixed-citation><mixed-citation xml:lang="en">Upston J.M., Neuzil J., Witting P.K., Alleva R., Stocker R. Oxidation of free fatty acids in low density lipoprotein by 15-lipoxygenase stimulates nonenzymic, alpha-tocopherol-mediated peroxidation of cholesteryl esters // J. Biol. Chem. 1997. V. 272. P. 30067-30074.</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Takahashi Y., Glasgow W.C., Suzuki H., Taketani Y., Yamamoto S., Anton M., Kuhn H., Brash A.R. Investigation of the oxygenation of phospholipids by the porcine leukocyte and human platelet arachidonate 12-lipoxygenases // Eur. J. Biochem. 1993. V. 218. P. 165-171.</mixed-citation><mixed-citation xml:lang="en">Takahashi Y., Glasgow W.C., Suzuki H., Taketani Y., Yamamoto S., Anton M., Kuhn H., Brash A.R. Investigation of the oxygenation of phospholipids by the porcine leukocyte and human platelet arachidonate 12-lipoxygenases // Eur. J. Biochem. 1993. V. 218. P. 165-171.</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Schewe T., Halangk W., Hiebsch C., Rapoport S.M. A lipoxygenase in rabbit reticulocytes which attacks phospholipids and intact mitochondria // FEBS Lett. 1975. V. 60. P. 149-152.</mixed-citation><mixed-citation xml:lang="en">Schewe T., Halangk W., Hiebsch C., Rapoport S.M. A lipoxygenase in rabbit reticulocytes which attacks phospholipids and intact mitochondria // FEBS Lett. 1975. V. 60. P. 149-152.</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Andreou A., Feussner I. Lipoxygenases - Structure and reaction mechanism // Phytochemistry. 2009. V. 70. P. 1504-1510.</mixed-citation><mixed-citation xml:lang="en">Andreou A., Feussner I. Lipoxygenases - Structure and reaction mechanism // Phytochemistry. 2009. V. 70. P. 1504-1510.</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Bhattacharya S., Mathew G., Jayne D.G., Pelengaris S., Khan M. 15-Lipoxygenase-1 in colorectal cancer: a review // Tumour Biol. 2009. V. 30. P. 185-199.</mixed-citation><mixed-citation xml:lang="en">Bhattacharya S., Mathew G., Jayne D.G., Pelengaris S., Khan M. 15-Lipoxygenase-1 in colorectal cancer: a review // Tumour Biol. 2009. V. 30. P. 185-199.</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Pidgeon G.P., Lysaght J., Krishnamoorthy S., Reynolds J.V., O’Byrne K., Nie D., Honn K.V. Lipoxygenase metabolism: Roles in tumor progression and survival // Cancer Metastasis Rev. 2007. V. 26. P. 503-524.</mixed-citation><mixed-citation xml:lang="en">Pidgeon G.P., Lysaght J., Krishnamoorthy S., Reynolds J.V., O’Byrne K., Nie D., Honn K.V. Lipoxygenase metabolism: Roles in tumor progression and survival // Cancer Metastasis Rev. 2007. V. 26. P. 503-524.</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Chawengsub Y., Gauthier K.M., Campbell W.B. Role of arachidonic acid lipoxygenase metabolites in the regulation of vascular tone // Am. J. Physiol. Heart Circ. Physiol. 2009. V. 297. P. 495-507.</mixed-citation><mixed-citation xml:lang="en">Chawengsub Y., Gauthier K.M., Campbell W.B. Role of arachidonic acid lipoxygenase metabolites in the regulation of vascular tone // Am. J. Physiol. Heart Circ. Physiol. 2009. V. 297. P. 495-507.</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Mochizuki N., Kwon Y.G. 15-Lipoxygenase-1 in the vasculature: Expanding roles in angiogenesis // Circ. Res. 2008. V. 102. P. 143-145.</mixed-citation><mixed-citation xml:lang="en">Mochizuki N., Kwon Y.G. 15-Lipoxygenase-1 in the vasculature: Expanding roles in angiogenesis // Circ. Res. 2008. V. 102. P. 143-145.</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Duroudier N.P., Tulah A.S., Sayers I. Leukotriene pathway genetics and pharmacogenetics in allergy // Allergy. 2009. V. 64. P. 823-839.</mixed-citation><mixed-citation xml:lang="en">Duroudier N.P., Tulah A.S., Sayers I. Leukotriene pathway genetics and pharmacogenetics in allergy // Allergy. 2009. V. 64. P. 823-839.</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Hersberger M. Potential role of the lipoxygenase derived lipid mediators in atherosclerosis: Leukotrienes, lipoxins and resolvins. // Clin. Chem. Lab. Med. 2010. V. 12. P. 1063-1073.</mixed-citation><mixed-citation xml:lang="en">Hersberger M. Potential role of the lipoxygenase derived lipid mediators in atherosclerosis: Leukotrienes, lipoxins and resolvins. // Clin. Chem. Lab. Med. 2010. V. 12. P. 1063-1073.</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Meyer M.P., Tomchick D.R., Klinman J.P. Enzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1 // Proc. Natl. Acad. Sci. USA. 2008. V. 105. P. 1146-1151.</mixed-citation><mixed-citation xml:lang="en">Meyer M.P., Tomchick D.R., Klinman J.P. Enzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1 // Proc. Natl. Acad. Sci. USA. 2008. V. 105. P. 1146-1151.</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Tomchick D.R., Phan P., Cymborowski M., Minor W., Holman T.R. Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1 // Biochemistry. 2001. V. 40. P. 7509-7517.</mixed-citation><mixed-citation xml:lang="en">Tomchick D.R., Phan P., Cymborowski M., Minor W., Holman T.R. Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1 // Biochemistry. 2001. V. 40. P. 7509-7517.</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Minor W., Solomon E.I., Holman T.R. Kinetic, spectroscopic, and structural investigations of the soybean lipoxygenase-1 first-coordination sphere mutant, Asn694Gly // Biochemistry. 2006. V. 45. P. 10233-10242.</mixed-citation><mixed-citation xml:lang="en">Minor W., Solomon E.I., Holman T.R. Kinetic, spectroscopic, and structural investigations of the soybean lipoxygenase-1 first-coordination sphere mutant, Asn694Gly // Biochemistry. 2006. V. 45. P. 10233-10242.</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Boyington J.C., Gaffney B.J., Amzel L.M. Structure of soybean lipoxygenase-I // Biochem. Soc. Trans. 1993. V. 21. P. 744-748.</mixed-citation><mixed-citation xml:lang="en">Boyington J.C., Gaffney B.J., Amzel L.M. Structure of soybean lipoxygenase-I // Biochem. Soc. Trans. 1993. V. 21. P. 744-748.</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Minor W., Steczko J., Stec B., Otwinowski Z., Bolin J.T., Walter R., Axelrod B. Crystal structure of soybean lipoxygenase L-1 at 1.4 Å resolution // Biochemistry. 1996. V. 35. P. 10687-10701.</mixed-citation><mixed-citation xml:lang="en">Minor W., Steczko J., Stec B., Otwinowski Z., Bolin J.T., Walter R., Axelrod B. Crystal structure of soybean lipoxygenase L-1 at 1.4 Å resolution // Biochemistry. 1996. V. 35. P. 10687-10701.</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Skrzypczak-Jankun E., Amzel L.M., Kroa B.A., Funk Jr. M.O. Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme // Proteins. 1997. V. 29. P. 15-31.</mixed-citation><mixed-citation xml:lang="en">Skrzypczak-Jankun E., Amzel L.M., Kroa B.A., Funk Jr. M.O. Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme // Proteins. 1997. V. 29. P. 15-31.</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Skrzypczak-Jankun E., Borbulevych O.Y., Zavodszky M.I., Baranski M.R., Padmanabhan K., Petricek V., Jankun J. Effect of crystal freezing and small-molecule binding on internal cavity size in a large protein: X-ray and docking studies of lipoxygenase at ambient and low temperature at 2.0 Å resolution // Acta Crystallogr. Sect. D. Biol. Crystallogr. 2006. V. 62. P. 766-775.</mixed-citation><mixed-citation xml:lang="en">Skrzypczak-Jankun E., Borbulevych O.Y., Zavodszky M.I., Baranski M.R., Padmanabhan K., Petricek V., Jankun J. Effect of crystal freezing and small-molecule binding on internal cavity size in a large protein: X-ray and docking studies of lipoxygenase at ambient and low temperature at 2.0 Å resolution // Acta Crystallogr. Sect. D. Biol. Crystallogr. 2006. V. 62. P. 766-775.</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Youn B., Sellhorn G.E., Mirchel R.J., Gaffney B.J., Grimes H.D., Kang C. Crystal structures of vegetative soybean lipoxygenase VLX-B and VLX-D, and comparisons with seed isoforms LOX-1 and LOX-3 // Proteins. 2006. V. 65. P. 1008-1020.</mixed-citation><mixed-citation xml:lang="en">Youn B., Sellhorn G.E., Mirchel R.J., Gaffney B.J., Grimes H.D., Kang C. Crystal structures of vegetative soybean lipoxygenase VLX-B and VLX-D, and comparisons with seed isoforms LOX-1 and LOX-3 // Proteins. 2006. V. 65. P. 1008-1020.</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Skrzypczak-Jankun E., Zhou K., McCabe N.P., Selman S.H., Jankun J. Structure of curcumin in complex with lipoxygenase and its significance in cancer // Int. J. Mol. Med. 2003. V. 12. P. 17-24.</mixed-citation><mixed-citation xml:lang="en">Skrzypczak-Jankun E., Zhou K., McCabe N.P., Selman S.H., Jankun J. Structure of curcumin in complex with lipoxygenase and its significance in cancer // Int. J. Mol. Med. 2003. V. 12. P. 17-24.</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Skrzypczak-Jankun E., Bross R.A., Carroll R.T., Dunham W.R., Funk Jr. M.O. Three dimensional structure of a purple lipoxygenase // J. Am. Chem. Soc. 2001. V. 123. P. 10814-10820.</mixed-citation><mixed-citation xml:lang="en">Skrzypczak-Jankun E., Bross R.A., Carroll R.T., Dunham W.R., Funk Jr. M.O. Three dimensional structure of a purple lipoxygenase // J. Am. Chem. Soc. 2001. V. 123. P. 10814-10820.</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Borbulevych O.Y., Jankun J., Selman S.H., Skrzypczak-Jankun E. Lipoxygenase interactions with natural flavonoid, quercetin, reveal a complex with protocatechuic acid in its X-ray structure at 2.1 Å resolution // Proteins. 2004. V. 54. P. 13-19.</mixed-citation><mixed-citation xml:lang="en">Borbulevych O.Y., Jankun J., Selman S.H., Skrzypczak-Jankun E. Lipoxygenase interactions with natural flavonoid, quercetin, reveal a complex with protocatechuic acid in its X-ray structure at 2.1 Å resolution // Proteins. 2004. V. 54. P. 13-19.</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Skrzypczak-Jankun E., Zhou K., Jankun J. Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 Å reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead // Int. J. Mol. Med. 2003. V. 12. P. 415-420.</mixed-citation><mixed-citation xml:lang="en">Skrzypczak-Jankun E., Zhou K., Jankun J. Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 Å reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead // Int. J. Mol. Med. 2003. V. 12. P. 415-420.</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Skrzypczak-Jankun E., Borbulevych O.Y., Jankun J. Soybean lipoxygenase-3 in complex with 4-nitrocatechol // Acta Crystallogr. Sect. D Biol. Crystallogr. 2004. V. 60. P. 613-615.</mixed-citation><mixed-citation xml:lang="en">Skrzypczak-Jankun E., Borbulevych O.Y., Jankun J. Soybean lipoxygenase-3 in complex with 4-nitrocatechol // Acta Crystallogr. Sect. D Biol. Crystallogr. 2004. V. 60. P. 613-615.</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Pham C., Jankun J., Skrzypczak-Jankun E., Flowers 2nd R.A., Funk Jr. M.O. Structural and thermo-chemical characterization of lipoxygenase catechol complexes // Biochemistry. 1998. V. 37. P. 17952-17957.</mixed-citation><mixed-citation xml:lang="en">Pham C., Jankun J., Skrzypczak-Jankun E., Flowers 2nd R.A., Funk Jr. M.O. Structural and thermo-chemical characterization of lipoxygenase catechol complexes // Biochemistry. 1998. V. 37. P. 17952-17957.</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Gillmor S.A., Villasenor A., Fletterick R., Sigal E., Browner M.F. The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity // Nat. Struct. Biol. 1997. V. 4. P. 1003-1009.</mixed-citation><mixed-citation xml:lang="en">Gillmor S.A., Villasenor A., Fletterick R., Sigal E., Browner M.F. The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity // Nat. Struct. Biol. 1997. V. 4. P. 1003-1009.</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Choi J., Chon J.K., Kim S., Shin W. Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data // Proteins. 2008. V. 70. P. 1023-1032.</mixed-citation><mixed-citation xml:lang="en">Choi J., Chon J.K., Kim S., Shin W. Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data // Proteins. 2008. V. 70. P. 1023-1032.</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Kobe M.J., Neau D.B, Mitchell C.E., Bartlett S.G., Newcomer M.E. The structure of human 15-lipoxygenase-2 with a substrate mimic // J. Biol. Chem. 2014. [Epub ahead of print].</mixed-citation><mixed-citation xml:lang="en">Kobe M.J., Neau D.B, Mitchell C.E., Bartlett S.G., Newcomer M.E. The structure of human 15-lipoxygenase-2 with a substrate mimic // J. Biol. Chem. 2014. [Epub ahead of print].</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Oldham M.L., Brash A.R., Newcomer M.E. Insights from the X-ray crystal structure of coral 8R-lipoxygenase: Calcium activation via a C2-like domain and a structural basis of product chirality // J. Biol. Chem. 2005. V. 280. P. 39545-39552.</mixed-citation><mixed-citation xml:lang="en">Oldham M.L., Brash A.R., Newcomer M.E. Insights from the X-ray crystal structure of coral 8R-lipoxygenase: Calcium activation via a C2-like domain and a structural basis of product chirality // J. Biol. Chem. 2005. V. 280. P. 39545-39552.</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">Neau D.B., Gilbert N.C., Bartlett S.G., Boeglin W., Brash A.R., Newcomer M.E. The 1.85 Å structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity // Biochemistry. 2009. V. 48. P. 7906-7915.</mixed-citation><mixed-citation xml:lang="en">Neau D.B., Gilbert N.C., Bartlett S.G., Boeglin W., Brash A.R., Newcomer M.E. The 1.85 Å structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity // Biochemistry. 2009. V. 48. P. 7906-7915.</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Gilbert N.C., Niebuhr M., Tsuruta H., Bordelon T., Ridderbusch O., Dassey A., Brash A.R., Bartlett S.G., Newcomer M.E. A covalent linker allows for membrane targeting of an oxylipin biosynthetic complex // Biochemistry. 2008. V. 47. P. 10665-10676.</mixed-citation><mixed-citation xml:lang="en">Gilbert N.C., Niebuhr M., Tsuruta H., Bordelon T., Ridderbusch O., Dassey A., Brash A.R., Bartlett S.G., Newcomer M.E. A covalent linker allows for membrane targeting of an oxylipin biosynthetic complex // Biochemistry. 2008. V. 47. P. 10665-10676.</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Tresaugues L., Moshe M., Arrowsmith C.H. [et al.] Crystal structure of the lipoxygenase domain of human arachidonate 12-lipoxygenase, 12s-type /PDB Deposition Date: 2008/5/12 (unpublished data).</mixed-citation><mixed-citation xml:lang="en">Tresaugues L., Moshe M., Arrowsmith C.H. [et al.] Crystal structure of the lipoxygenase domain of human arachidonate 12-lipoxygenase, 12s-type /PDB Deposition Date: 2008/5/12 (unpublished data).</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Gilbert N.C., Bartlett S.G., Waight M.T., Neau D.B., Boeglin W.E., Brash A.R., Newcomer M.E. The structure of human 5-lipoxygenase // Science. 2011. V. 331. P. 217-219.</mixed-citation><mixed-citation xml:lang="en">Gilbert N.C., Bartlett S.G., Waight M.T., Neau D.B., Boeglin W.E., Brash A.R., Newcomer M.E. The structure of human 5-lipoxygenase // Science. 2011. V. 331. P. 217-219.</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Eek P., Järving R., Järving I., Gilbert N.C., Newcomer M.E., Samel N. Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca2+ regulation // J. Biol. Chem. 2012. V. 287. P. 22377-22386.</mixed-citation><mixed-citation xml:lang="en">Eek P., Järving R., Järving I., Gilbert N.C., Newcomer M.E., Samel N. Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca2+ regulation // J. Biol. Chem. 2012. V. 287. P. 22377-22386.</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Xu S., Mueser T.C., Marnett L.J., Funk Jr. M.O. Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis // Structure. 2012. V. 20. P. 1490-1497.</mixed-citation><mixed-citation xml:lang="en">Xu S., Mueser T.C., Marnett L.J., Funk Jr. M.O. Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis // Structure. 2012. V. 20. P. 1490-1497.</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Koljak R., Boutaud O., Shieh B.H., Samel N., Brash A.R. Identification of a naturally occurring peroxidase-lipoxygenase fusion protein // Science. 1997. V. 277. P. 1994-1996.</mixed-citation><mixed-citation xml:lang="en">Koljak R., Boutaud O., Shieh B.H., Samel N., Brash A.R. Identification of a naturally occurring peroxidase-lipoxygenase fusion protein // Science. 1997. V. 277. P. 1994-1996.</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Boutaud O., Brash A.R. Purification and catalytic activities of the two domains of the allene oxide synthase-lipoxygenase fusion protein of the coral Plexaura homomalla // J. Biol. Chem. 1999. V. 274. P. 33764-33770.</mixed-citation><mixed-citation xml:lang="en">Boutaud O., Brash A.R. Purification and catalytic activities of the two domains of the allene oxide synthase-lipoxygenase fusion protein of the coral Plexaura homomalla // J. Biol. Chem. 1999. V. 274. P. 33764-33770.</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Abraham B.D., Sono M., Boutaud O., Shriner A., Dawson J.H., Brash A.R., Gaffney B.J. Characterization of the coral allene oxide synthase active site with UV-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopy: Еvidence for tyrosinate ligation to the ferric enzyme heme iron // Biochemistry. 2001. V. 40. P. 2251-2259.</mixed-citation><mixed-citation xml:lang="en">Abraham B.D., Sono M., Boutaud O., Shriner A., Dawson J.H., Brash A.R., Gaffney B.J. Characterization of the coral allene oxide synthase active site with UV-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance spectroscopy: Еvidence for tyrosinate ligation to the ferric enzyme heme iron // Biochemistry. 2001. V. 40. P. 2251-2259.</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Oldham M.L., Brash A.R., Newcomer M.E. The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide // Proc. Natl. Acad. Sci. USA. 2005. V. 102. P. 297-302.</mixed-citation><mixed-citation xml:lang="en">Oldham M.L., Brash A.R., Newcomer M.E. The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide // Proc. Natl. Acad. Sci. USA. 2005. V. 102. P. 297-302.</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Lohelaid H., Jarving R., Valmsen K., Varvas K., Kreen M., Jarving I., Samel N. Identification of a functional allene oxide synthase-lipoxygenase fusion protein in the soft coral Gersemia fruticosa suggests the generality of this pathway in octocorals // Biochim. Biophys. Acta. 2008. V. 1780. P. 315-321.</mixed-citation><mixed-citation xml:lang="en">Lohelaid H., Jarving R., Valmsen K., Varvas K., Kreen M., Jarving I., Samel N. Identification of a functional allene oxide synthase-lipoxygenase fusion protein in the soft coral Gersemia fruticosa suggests the generality of this pathway in octocorals // Biochim. Biophys. Acta. 2008. V. 1780. P. 315-321.</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Zheng Y., Boeglin W.E., Schneider C., Brash A.R. A 49 KD mini-lipoxygenase from Anabaena sp. PCC 7120 retains catalytically complete functionality // J. Biol. Chem. 2008. V. 283. P. 5138-5147.</mixed-citation><mixed-citation xml:lang="en">Zheng Y., Boeglin W.E., Schneider C., Brash A.R. A 49 KD mini-lipoxygenase from Anabaena sp. PCC 7120 retains catalytically complete functionality // J. Biol. Chem. 2008. V. 283. P. 5138-5147.</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Schneider C., Niisuke K., Boeglin W.E., Voehler M., Stec D.F., Porter N.A., Brash A.R. Enzymatic synthesis of a bicyclobutane fatty acid by a hemoprotein-lipoxygenase fusion protein from the cyanobacterium Anabaena PCC 7120 // Proc. Natl. Acad. Sci. USA. 2007. V. 104. P. 18941-18945.</mixed-citation><mixed-citation xml:lang="en">Schneider C., Niisuke K., Boeglin W.E., Voehler M., Stec D.F., Porter N.A., Brash A.R. Enzymatic synthesis of a bicyclobutane fatty acid by a hemoprotein-lipoxygenase fusion protein from the cyanobacterium Anabaena PCC 7120 // Proc. Natl. Acad. Sci. USA. 2007. V. 104. P. 18941-18945.</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Gao B., Boeglin W.E., Zheng Y., Schneider C., Brash A.R. Evidence for an ionic intermediate in the transformation of fatty acid hydroperoxide by a catalase-related allene oxide synthase from the cyanobacterium Acaryochloris marina // J. Biol. Chem. 2009. V. 284. P. 22087-22098.</mixed-citation><mixed-citation xml:lang="en">Gao B., Boeglin W.E., Zheng Y., Schneider C., Brash A.R. Evidence for an ionic intermediate in the transformation of fatty acid hydroperoxide by a catalase-related allene oxide synthase from the cyanobacterium Acaryochloris marina // J. Biol. Chem. 2009. V. 284. P. 22087-22098.</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Chahinian H., Sias B., Carriere F. The C-terminal domain of pancreatic lipase: Functional and structural analogies with C2 domains // Curr. Protein Pept. Sci. 2000. V. 1. P. 91-103.</mixed-citation><mixed-citation xml:lang="en">Chahinian H., Sias B., Carriere F. The C-terminal domain of pancreatic lipase: Functional and structural analogies with C2 domains // Curr. Protein Pept. Sci. 2000. V. 1. P. 91-103.</mixed-citation></citation-alternatives></ref><ref id="cit51"><label>51</label><citation-alternatives><mixed-citation xml:lang="ru">Maccarrone M., Salucci M.L. Tryptic digestion of soybean lipoxygenase-1 generates a 60 kDa fragment with improved activity and membrane binding ability // Biochemistry. 2001. V. 40. P. 6819-6827.</mixed-citation><mixed-citation xml:lang="en">Maccarrone M., Salucci M.L. Tryptic digestion of soybean lipoxygenase-1 generates a 60 kDa fragment with improved activity and membrane binding ability // Biochemistry. 2001. V. 40. P. 6819-6827.</mixed-citation></citation-alternatives></ref><ref id="cit52"><label>52</label><citation-alternatives><mixed-citation xml:lang="ru">Dainese E., Angelucci C.B., Sabatucci A., De Filippis V., Mei G., Maccarrone M. A novel role for iron in modulating the activity and membrane-binding ability of a trimmed soybean lipoxygenase-1 // FASEB J. 2010. V. 24. P. 1725-1736.</mixed-citation><mixed-citation xml:lang="en">Dainese E., Angelucci C.B., Sabatucci A., De Filippis V., Mei G., Maccarrone M. A novel role for iron in modulating the activity and membrane-binding ability of a trimmed soybean lipoxygenase-1 // FASEB J. 2010. V. 24. P. 1725-1736.</mixed-citation></citation-alternatives></ref><ref id="cit53"><label>53</label><citation-alternatives><mixed-citation xml:lang="ru">Walther M., Anton M., Wiedmann M., Fletterick R., Kuhn H. The N-terminal domain of the reticulocyte-type 15-lipoxygenase is not essential for enzymatic activity but contains determinants for membrane binding // J. Biol. Chem. 2002. V. 277. P. 27360-27366.</mixed-citation><mixed-citation xml:lang="en">Walther M., Anton M., Wiedmann M., Fletterick R., Kuhn H. The N-terminal domain of the reticulocyte-type 15-lipoxygenase is not essential for enzymatic activity but contains determinants for membrane binding // J. Biol. Chem. 2002. V. 277. P. 27360-27366.</mixed-citation></citation-alternatives></ref><ref id="cit54"><label>54</label><citation-alternatives><mixed-citation xml:lang="ru">Romanov S., Wiesner R., Myagkova G., Kuhn H., Ivanov I. Affinity labeling of the rabbit 12/15-lipoxygenase using azido derivatives of arachidonic acid // Biochemistry. 2006. V. 45. P. 3554-3562.</mixed-citation><mixed-citation xml:lang="en">Romanov S., Wiesner R., Myagkova G., Kuhn H., Ivanov I. Affinity labeling of the rabbit 12/15-lipoxygenase using azido derivatives of arachidonic acid // Biochemistry. 2006. V. 45. P. 3554-3562.</mixed-citation></citation-alternatives></ref><ref id="cit55"><label>55</label><citation-alternatives><mixed-citation xml:lang="ru">Winkler F.K., D’Arcy A., Hunziker W. Structure of human pancreatic lipase // Nature. 1990. V. 343. P. 771-774.</mixed-citation><mixed-citation xml:lang="en">Winkler F.K., D’Arcy A., Hunziker W. Structure of human pancreatic lipase // Nature. 1990. V. 343. P. 771-774.</mixed-citation></citation-alternatives></ref><ref id="cit56"><label>56</label><citation-alternatives><mixed-citation xml:lang="ru">May C., Hohne M., Gnau P., Schwennesen K., Kindl H. The N-terminal β-barrel structure of lipid body lipoxygenase mediates its binding to liposomes and lipid bodies // Eur. J. Biochem. 2000. V. 267. P. 1100-1109.</mixed-citation><mixed-citation xml:lang="en">May C., Hohne M., Gnau P., Schwennesen K., Kindl H. The N-terminal β-barrel structure of lipid body lipoxygenase mediates its binding to liposomes and lipid bodies // Eur. J. Biochem. 2000. V. 267. P. 1100-1109.</mixed-citation></citation-alternatives></ref><ref id="cit57"><label>57</label><citation-alternatives><mixed-citation xml:lang="ru">Tatulian S.A., Steczko J., Minor W. Uncovering a calcium-regulated membrane-binding mechanism for soybean lipoxygenase-1 // Biochemistry. 1998. V. 37. P. 15481-15490.</mixed-citation><mixed-citation xml:lang="en">Tatulian S.A., Steczko J., Minor W. Uncovering a calcium-regulated membrane-binding mechanism for soybean lipoxygenase-1 // Biochemistry. 1998. V. 37. P. 15481-15490.</mixed-citation></citation-alternatives></ref><ref id="cit58"><label>58</label><citation-alternatives><mixed-citation xml:lang="ru">Kulkarni S., Das S., Funk C.D., Murray D., Cho W. Molecular basis of the specific subcellular localization of the C2-like domain of 5-lipoxygenase // J. Biol. Chem. 2002. V. 277. P. 13167-13174.</mixed-citation><mixed-citation xml:lang="en">Kulkarni S., Das S., Funk C.D., Murray D., Cho W. Molecular basis of the specific subcellular localization of the C2-like domain of 5-lipoxygenase // J. Biol. Chem. 2002. V. 277. P. 13167-13174.</mixed-citation></citation-alternatives></ref><ref id="cit59"><label>59</label><citation-alternatives><mixed-citation xml:lang="ru">Walther M., Wiesner R., Kuhn H. Investigations into calcium-dependent membrane association of 15-lipoxygenase-1. Mechanistic roles of surface-exposed hydrophobic amino acids and calcium // J. Biol. Chem. 2004. V. 279. P. 3717-3725.</mixed-citation><mixed-citation xml:lang="en">Walther M., Wiesner R., Kuhn H. Investigations into calcium-dependent membrane association of 15-lipoxygenase-1. Mechanistic roles of surface-exposed hydrophobic amino acids and calcium // J. Biol. Chem. 2004. V. 279. P. 3717-3725.</mixed-citation></citation-alternatives></ref><ref id="cit60"><label>60</label><citation-alternatives><mixed-citation xml:lang="ru">Hammarberg T., Provost P., Persson B., Radmark O. The N-terminal domain of 5-lipoxygenase binds calcium and mediates calcium stimulation of enzyme activity // J. Biol. Chem. 2000. V. 275. P. 38787-38793.</mixed-citation><mixed-citation xml:lang="en">Hammarberg T., Provost P., Persson B., Radmark O. The N-terminal domain of 5-lipoxygenase binds calcium and mediates calcium stimulation of enzyme activity // J. Biol. Chem. 2000. V. 275. P. 38787-38793.</mixed-citation></citation-alternatives></ref><ref id="cit61"><label>61</label><citation-alternatives><mixed-citation xml:lang="ru">Chen X.S., Funk C.D. The N-terminal “β-barrel” domain of 5-lipoxygenase is essential for nuclear membrane translocation // J. Biol. Chem. 2001. V. 276. P. 811-818.</mixed-citation><mixed-citation xml:lang="en">Chen X.S., Funk C.D. The N-terminal “β-barrel” domain of 5-lipoxygenase is essential for nuclear membrane translocation // J. Biol. Chem. 2001. V. 276. P. 811-818.</mixed-citation></citation-alternatives></ref><ref id="cit62"><label>62</label><citation-alternatives><mixed-citation xml:lang="ru">Brinckmann R., Schnurr K., Heydeck D., Rosenbach T., Kolde G., Kuhn H. Membrane translocation of 15-lipoxygenase in hematopoietic cells is calcium-dependent and activates the oxygenase activity of the enzyme // Blood. 1998. V. 91. P. 64-74.</mixed-citation><mixed-citation xml:lang="en">Brinckmann R., Schnurr K., Heydeck D., Rosenbach T., Kolde G., Kuhn H. Membrane translocation of 15-lipoxygenase in hematopoietic cells is calcium-dependent and activates the oxygenase activity of the enzyme // Blood. 1998. V. 91. P. 64-74.</mixed-citation></citation-alternatives></ref><ref id="cit63"><label>63</label><citation-alternatives><mixed-citation xml:lang="ru">Schenk G., Neidig M.L., Zhou J., Holman T.R., Solomon E.I. Spectroscopic characterization of soybean lipoxygenase-1 mutants: The role of second coordination sphere residues in the regulation of enzyme activity // Biochemistry. 2003. V. 42. P. 7294-7302.</mixed-citation><mixed-citation xml:lang="en">Schenk G., Neidig M.L., Zhou J., Holman T.R., Solomon E.I. Spectroscopic characterization of soybean lipoxygenase-1 mutants: The role of second coordination sphere residues in the regulation of enzyme activity // Biochemistry. 2003. V. 42. P. 7294-7302.</mixed-citation></citation-alternatives></ref><ref id="cit64"><label>64</label><citation-alternatives><mixed-citation xml:lang="ru">Kuban R.J., Wiesner R., Rathman J., Veldink G., Nolting H., Sole V.A., Kuhn H. The iron ligand sphere geometry of mammalian 15-lipoxygenases // Biochem. J. 1998. V. 332 (Pt 1). P. 237-242.</mixed-citation><mixed-citation xml:lang="en">Kuban R.J., Wiesner R., Rathman J., Veldink G., Nolting H., Sole V.A., Kuhn H. The iron ligand sphere geometry of mammalian 15-lipoxygenases // Biochem. J. 1998. V. 332 (Pt 1). P. 237-242.</mixed-citation></citation-alternatives></ref><ref id="cit65"><label>65</label><citation-alternatives><mixed-citation xml:lang="ru">Dainese E., Sabatucci A., van Zadelhoff G., Angelucci C.B., Vachette P., Veldink G.A., Agrò A.F., Maccarrone M. Structural stability of soybean lipoxygenase-1 in solution as probed by small angle X-ray scattering // J. Mol. Biol. 2005. V. 349. P. 143-152.</mixed-citation><mixed-citation xml:lang="en">Dainese E., Sabatucci A., van Zadelhoff G., Angelucci C.B., Vachette P., Veldink G.A., Agrò A.F., Maccarrone M. Structural stability of soybean lipoxygenase-1 in solution as probed by small angle X-ray scattering // J. Mol. Biol. 2005. V. 349. P. 143-152.</mixed-citation></citation-alternatives></ref><ref id="cit66"><label>66</label><citation-alternatives><mixed-citation xml:lang="ru">Mei G., Di Venere A., Nicolai E., Angelucci C.B., Ivanov I., Sabatucci A., Dainese E., Kuhn H., Maccarrone M. Structural properties of plant and mammalian lipoxygenases. Temperature-dependent conformational alterations and membrane binding ability // Biochemistry. 2008. V. 47. P. 9234-9242.</mixed-citation><mixed-citation xml:lang="en">Mei G., Di Venere A., Nicolai E., Angelucci C.B., Ivanov I., Sabatucci A., Dainese E., Kuhn H., Maccarrone M. Structural properties of plant and mammalian lipoxygenases. Temperature-dependent conformational alterations and membrane binding ability // Biochemistry. 2008. V. 47. P. 9234-9242.</mixed-citation></citation-alternatives></ref><ref id="cit67"><label>67</label><citation-alternatives><mixed-citation xml:lang="ru">Hammel M., Walther M., Prassl R., Kuhn H. Structural flexibility of the N-terminal beta-barrel domain of 15-lipoxygenase-1 probed by small angle X-ray scattering. Functional consequences for activity regulation and membrane binding // J. Mol. Biol. 2004. V. 343. P. 917-929.</mixed-citation><mixed-citation xml:lang="en">Hammel M., Walther M., Prassl R., Kuhn H. Structural flexibility of the N-terminal beta-barrel domain of 15-lipoxygenase-1 probed by small angle X-ray scattering. Functional consequences for activity regulation and membrane binding // J. Mol. Biol. 2004. V. 343. P. 917-929.</mixed-citation></citation-alternatives></ref><ref id="cit68"><label>68</label><citation-alternatives><mixed-citation xml:lang="ru">Borngraber S., Browner M., Gillmor S., Gerth C., Anton M., Fletterick R., Kuhn H. Shape and specificity in mammalian 15-lipoxygenase active site. The functional interplay of sequence determinants for the reaction specificity // J. Biol. Chem. 1999. V. 274. P. 37345-37350.</mixed-citation><mixed-citation xml:lang="en">Borngraber S., Browner M., Gillmor S., Gerth C., Anton M., Fletterick R., Kuhn H. Shape and specificity in mammalian 15-lipoxygenase active site. The functional interplay of sequence determinants for the reaction specificity // J. Biol. Chem. 1999. V. 274. P. 37345-37350.</mixed-citation></citation-alternatives></ref><ref id="cit69"><label>69</label><citation-alternatives><mixed-citation xml:lang="ru">Borngraber S., Kuban R.J., Anton M., Kuhn H. Phenylalanine 353 is a primary determinant for the positional specificity of mammalian 15-lipoxygenases // J. Mol. Biol. 1996. V. 264. P. 1145-1153.</mixed-citation><mixed-citation xml:lang="en">Borngraber S., Kuban R.J., Anton M., Kuhn H. Phenylalanine 353 is a primary determinant for the positional specificity of mammalian 15-lipoxygenases // J. Mol. Biol. 1996. V. 264. P. 1145-1153.</mixed-citation></citation-alternatives></ref><ref id="cit70"><label>70</label><citation-alternatives><mixed-citation xml:lang="ru">Knapp M.J., Klinman J.P. Kinetic studies of oxygen reactivity in soybean lipoxygenase-1 // Biochemistry. 2003. V. 42. P. 11466-11475.</mixed-citation><mixed-citation xml:lang="en">Knapp M.J., Klinman J.P. Kinetic studies of oxygen reactivity in soybean lipoxygenase-1 // Biochemistry. 2003. V. 42. P. 11466-11475.</mixed-citation></citation-alternatives></ref><ref id="cit71"><label>71</label><citation-alternatives><mixed-citation xml:lang="ru">Chu K., Vojtchovsky J., McMahon B.H., Sweet R.M., Berendzen J., Schlichting I. Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin // Nature. 2000. V. 403. P. 921-923.</mixed-citation><mixed-citation xml:lang="en">Chu K., Vojtchovsky J., McMahon B.H., Sweet R.M., Berendzen J., Schlichting I. Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin // Nature. 2000. V. 403. P. 921-923.</mixed-citation></citation-alternatives></ref><ref id="cit72"><label>72</label><citation-alternatives><mixed-citation xml:lang="ru">Ostermann A., Waschipky R., Parak F.G., Nienhaus G.U. Ligand binding and conformational motions in myoglobin // Nature. 2000. V. 404. P. 205-208.</mixed-citation><mixed-citation xml:lang="en">Ostermann A., Waschipky R., Parak F.G., Nienhaus G.U. Ligand binding and conformational motions in myoglobin // Nature. 2000. V. 404. P. 205-208.</mixed-citation></citation-alternatives></ref><ref id="cit73"><label>73</label><citation-alternatives><mixed-citation xml:lang="ru">Scott E.E., Gibson Q.H. Ligand migration in sperm whale myoglobin // Biochemistry. 1997. V. 36. P. 11909-11917.</mixed-citation><mixed-citation xml:lang="en">Scott E.E., Gibson Q.H. Ligand migration in sperm whale myoglobin // Biochemistry. 1997. V. 36. P. 11909-11917.</mixed-citation></citation-alternatives></ref><ref id="cit74"><label>74</label><citation-alternatives><mixed-citation xml:lang="ru">Knapp M.J., Seebeck F.P., Klinman J.P. Steric control of oxygenation regiochemistry in soybean lipoxygenase-1 // J. Am. Chem. Soc. 2001. V. 123. P. 2931-2932.</mixed-citation><mixed-citation xml:lang="en">Knapp M.J., Seebeck F.P., Klinman J.P. Steric control of oxygenation regiochemistry in soybean lipoxygenase-1 // J. Am. Chem. Soc. 2001. V. 123. P. 2931-2932.</mixed-citation></citation-alternatives></ref><ref id="cit75"><label>75</label><citation-alternatives><mixed-citation xml:lang="ru">Saam J., Ivanov I., Walther M., Holzhutter H.G., Kuhn H. Molecular dioxygen enters the active site of 12/15-lipoxygenase via dynamic oxygen access channels // Proc. Natl. Acad. Sci. USA. 2007. V. 104. P. 13319-13324.</mixed-citation><mixed-citation xml:lang="en">Saam J., Ivanov I., Walther M., Holzhutter H.G., Kuhn H. Molecular dioxygen enters the active site of 12/15-lipoxygenase via dynamic oxygen access channels // Proc. Natl. Acad. Sci. USA. 2007. V. 104. P. 13319-13324.</mixed-citation></citation-alternatives></ref><ref id="cit76"><label>76</label><citation-alternatives><mixed-citation xml:lang="ru">Hamberg M., Samuelsson B. On the specificity of the oxygenation of unsaturated fatty acids catalyzed by soybean lipoxidase // J. Biol. Chem. 1967. V. 242. P. 5329-5335.</mixed-citation><mixed-citation xml:lang="en">Hamberg M., Samuelsson B. On the specificity of the oxygenation of unsaturated fatty acids catalyzed by soybean lipoxidase // J. Biol. Chem. 1967. V. 242. P. 5329-5335.</mixed-citation></citation-alternatives></ref><ref id="cit77"><label>77</label><citation-alternatives><mixed-citation xml:lang="ru">Kuhn H., Sprecher H., Brash A.R. On singular or dual positional specificity of lipoxygenases // J. Biol. Chem. 1990. V. 265. P. 16300-16305.</mixed-citation><mixed-citation xml:lang="en">Kuhn H., Sprecher H., Brash A.R. On singular or dual positional specificity of lipoxygenases // J. Biol. Chem. 1990. V. 265. P. 16300-16305.</mixed-citation></citation-alternatives></ref><ref id="cit78"><label>78</label><citation-alternatives><mixed-citation xml:lang="ru">Kuhn H., Schewe T., Rapoport S.M. The stereochemistry of the reactions of lipoxygenases and their metabolites. Proposed nomenclature of lipoxygenases and related enzymes // Adv. Enzymol. Relat. Areas Mol. Biol. 1986. V. 58. P. 273-311.</mixed-citation><mixed-citation xml:lang="en">Kuhn H., Schewe T., Rapoport S.M. The stereochemistry of the reactions of lipoxygenases and their metabolites. Proposed nomenclature of lipoxygenases and related enzymes // Adv. Enzymol. Relat. Areas Mol. Biol. 1986. V. 58. P. 273-311.</mixed-citation></citation-alternatives></ref><ref id="cit79"><label>79</label><citation-alternatives><mixed-citation xml:lang="ru">Browner M., Gillmor S.A., Fletterick R. Burying a charge // Nat. Struct. Biol. 1998. V. 5. P. 179.</mixed-citation><mixed-citation xml:lang="en">Browner M., Gillmor S.A., Fletterick R. Burying a charge // Nat. Struct. Biol. 1998. V. 5. P. 179.</mixed-citation></citation-alternatives></ref><ref id="cit80"><label>80</label><citation-alternatives><mixed-citation xml:lang="ru">Prigge S.T., Gaffney B.J., Amzel L.M. Relation between positional specificity and chirality in mammalian lipoxygenases // Nat. Struct. Biol. 1998. V. 5. P. 178-179.</mixed-citation><mixed-citation xml:lang="en">Prigge S.T., Gaffney B.J., Amzel L.M. Relation between positional specificity and chirality in mammalian lipoxygenases // Nat. Struct. Biol. 1998. V. 5. P. 178-179.</mixed-citation></citation-alternatives></ref><ref id="cit81"><label>81</label><citation-alternatives><mixed-citation xml:lang="ru">Hornung E., Walther M., Kuhn H., Feussner I. Conversion of cucumber linoleate 13-lipoxygenase to a 9-lipoxygenating species by site-directed mutagenesis // Proc. Natl. Acad. Sci. USA. 1999. V. 96. P. 4192-4197.</mixed-citation><mixed-citation xml:lang="en">Hornung E., Walther M., Kuhn H., Feussner I. Conversion of cucumber linoleate 13-lipoxygenase to a 9-lipoxygenating species by site-directed mutagenesis // Proc. Natl. Acad. Sci. USA. 1999. V. 96. P. 4192-4197.</mixed-citation></citation-alternatives></ref><ref id="cit82"><label>82</label><citation-alternatives><mixed-citation xml:lang="ru">Gardner H.W. Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-hydroperoxides from linoleic acid by a pH-dependent mechanism // Biochim. Biophys. Acta. 1989. V. 1001. P. 274-281.</mixed-citation><mixed-citation xml:lang="en">Gardner H.W. Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-hydroperoxides from linoleic acid by a pH-dependent mechanism // Biochim. Biophys. Acta. 1989. V. 1001. P. 274-281.</mixed-citation></citation-alternatives></ref><ref id="cit83"><label>83</label><citation-alternatives><mixed-citation xml:lang="ru">Walther M., Roffeis J., Jansen C., Anton M., Ivanov I., Kuhn H. Structural basis for pH-dependent alterations of reaction specificity of vertebrate lipoxygenase isoforms // Biochim. Biophys. Acta. 2009. V. 1791. P. 827-835.</mixed-citation><mixed-citation xml:lang="en">Walther M., Roffeis J., Jansen C., Anton M., Ivanov I., Kuhn H. Structural basis for pH-dependent alterations of reaction specificity of vertebrate lipoxygenase isoforms // Biochim. Biophys. Acta. 2009. V. 1791. P. 827-835.</mixed-citation></citation-alternatives></ref><ref id="cit84"><label>84</label><citation-alternatives><mixed-citation xml:lang="ru">Walther M., Ivanov I., Myagkova G., Kuhn H. Alterations of lipoxygenase specificity by targeted substrate modification and site-directed mutagenesis // Chem. Biol. 2001. V. 8. P. 779-790.</mixed-citation><mixed-citation xml:lang="en">Walther M., Ivanov I., Myagkova G., Kuhn H. Alterations of lipoxygenase specificity by targeted substrate modification and site-directed mutagenesis // Chem. Biol. 2001. V. 8. P. 779-790.</mixed-citation></citation-alternatives></ref><ref id="cit85"><label>85</label><citation-alternatives><mixed-citation xml:lang="ru">Meruvu S., Walther M., Ivanov I., Hammarstrom S., Furstenberger G., Krieg P., Reddanna P., Kuhn H. Sequence determinants for the reaction specificity of murine (12R)-lipoxygenase: Targeted substrate modification and site-directed mutagenesis // J. Biol. Chem. 2005. V. 280. P. 36633-36641.</mixed-citation><mixed-citation xml:lang="en">Meruvu S., Walther M., Ivanov I., Hammarstrom S., Furstenberger G., Krieg P., Reddanna P., Kuhn H. Sequence determinants for the reaction specificity of murine (12R)-lipoxygenase: Targeted substrate modification and site-directed mutagenesis // J. Biol. Chem. 2005. V. 280. P. 36633-36641.</mixed-citation></citation-alternatives></ref><ref id="cit86"><label>86</label><citation-alternatives><mixed-citation xml:lang="ru">Coffa G., Brash A.R. A single active site residue directs oxygenation stereospecificity in lipoxy-genases: Stereocontrol is linked to the position of oxygenation // Proc. Natl. Acad. Sci. USA. 2004. V. 101. P. 15579-15584.</mixed-citation><mixed-citation xml:lang="en">Coffa G., Brash A.R. A single active site residue directs oxygenation stereospecificity in lipoxy-genases: Stereocontrol is linked to the position of oxygenation // Proc. Natl. Acad. Sci. USA. 2004. V. 101. P. 15579-15584.</mixed-citation></citation-alternatives></ref><ref id="cit87"><label>87</label><citation-alternatives><mixed-citation xml:lang="ru">Coffa G., Schneider C., Brash A.R. A comprehensive model of positional and stereo control in lipoxy-genases // Biochem. Biophys. Res. Commun. 2005. V. 338. P. 87-92.</mixed-citation><mixed-citation xml:lang="en">Coffa G., Schneider C., Brash A.R. A comprehensive model of positional and stereo control in lipoxy-genases // Biochem. Biophys. Res. Commun. 2005. V. 338. P. 87-92.</mixed-citation></citation-alternatives></ref><ref id="cit88"><label>88</label><citation-alternatives><mixed-citation xml:lang="ru">Coffa G., Imber A.N., Maguire B.C., Laxmikanthan G., Schneider C., Gaffney B.J., Brash A.R. On the relationships of substrate orientation, hydrogen abstraction, and product stereochemistry in single and double dioxygenations by soybean lipoxygenase-1 and its Ala542Gly mutant // J. Biol. Chem. 2005. V. 280. P. 38756-38766.</mixed-citation><mixed-citation xml:lang="en">Coffa G., Imber A.N., Maguire B.C., Laxmikanthan G., Schneider C., Gaffney B.J., Brash A.R. On the relationships of substrate orientation, hydrogen abstraction, and product stereochemistry in single and double dioxygenations by soybean lipoxygenase-1 and its Ala542Gly mutant // J. Biol. Chem. 2005. V. 280. P. 38756-38766.</mixed-citation></citation-alternatives></ref><ref id="cit89"><label>89</label><citation-alternatives><mixed-citation xml:lang="ru">Boeglin W.E., Itoh A., Zheng Y., Coffa G., Howe G.A., Brash A.R. Investigation of substrate binding and product stereochemistry issues in two linoleate 9-lipoxygenases // Lipids. 2008. V. 43. P. 979-987.</mixed-citation><mixed-citation xml:lang="en">Boeglin W.E., Itoh A., Zheng Y., Coffa G., Howe G.A., Brash A.R. Investigation of substrate binding and product stereochemistry issues in two linoleate 9-lipoxygenases // Lipids. 2008. V. 43. P. 979-987.</mixed-citation></citation-alternatives></ref><ref id="cit90"><label>90</label><citation-alternatives><mixed-citation xml:lang="ru">Sloane D.L., Leung R., Barnett J., Craik C.S., Sigal E. Conversion of human 15-lipoxygenase to an efficient 12-lipoxygenase: The side-chain geometry of amino acids 417 and 418 determine positional specificity // Protein Eng. 1995. V. 8. P. 275-282.</mixed-citation><mixed-citation xml:lang="en">Sloane D.L., Leung R., Barnett J., Craik C.S., Sigal E. Conversion of human 15-lipoxygenase to an efficient 12-lipoxygenase: The side-chain geometry of amino acids 417 and 418 determine positional specificity // Protein Eng. 1995. V. 8. P. 275-282.</mixed-citation></citation-alternatives></ref><ref id="cit91"><label>91</label><citation-alternatives><mixed-citation xml:lang="ru">Sloane D.L., Leung R., Craik C.S., Sigal E. A primary determinant for lipoxygenase positional specificity // Nature. 1991. V. 354. P. 149-152.</mixed-citation><mixed-citation xml:lang="en">Sloane D.L., Leung R., Craik C.S., Sigal E. A primary determinant for lipoxygenase positional specificity // Nature. 1991. V. 354. P. 149-152.</mixed-citation></citation-alternatives></ref><ref id="cit92"><label>92</label><citation-alternatives><mixed-citation xml:lang="ru">Vogel R., Jansen C., Roffeis J., Reddanna P., Forsell P., Claesson H.E., Kuhn H., Walther M. Applicability of the triad concept for the positional specificity of mammalian lipoxygenases // J. Biol. Chem. 2010. V. 285. P. 5369-5376.</mixed-citation><mixed-citation xml:lang="en">Vogel R., Jansen C., Roffeis J., Reddanna P., Forsell P., Claesson H.E., Kuhn H., Walther M. Applicability of the triad concept for the positional specificity of mammalian lipoxygenases // J. Biol. Chem. 2010. V. 285. P. 5369-5376.</mixed-citation></citation-alternatives></ref><ref id="cit93"><label>93</label><citation-alternatives><mixed-citation xml:lang="ru">Burger F., Krieg P., Marks F., Furstenberger G. Enzymic characterization of epidermis-derived 12-lipoxygenase isoenzymes // Biochem. J. 2000. V. 348 (Pt 2). P. 329-335.</mixed-citation><mixed-citation xml:lang="en">Burger F., Krieg P., Marks F., Furstenberger G. Enzymic characterization of epidermis-derived 12-lipoxygenase isoenzymes // Biochem. J. 2000. V. 348 (Pt 2). P. 329-335.</mixed-citation></citation-alternatives></ref><ref id="cit94"><label>94</label><citation-alternatives><mixed-citation xml:lang="ru">Watanabe T., Haeggstrom J.Z. Rat 12-lipoxygenase: Mutations of amino acids implicated in the positional specificity of 15- and 12-lipoxygenases // Biochem. Biophys. Res. Commun. 1993. V. 192. P. 1023-1029.</mixed-citation><mixed-citation xml:lang="en">Watanabe T., Haeggstrom J.Z. Rat 12-lipoxygenase: Mutations of amino acids implicated in the positional specificity of 15- and 12-lipoxygenases // Biochem. Biophys. Res. Commun. 1993. V. 192. P. 1023-1029.</mixed-citation></citation-alternatives></ref><ref id="cit95"><label>95</label><citation-alternatives><mixed-citation xml:lang="ru">Suzuki H., Kishimoto K., Yoshimoto T., Yamamoto S., Kanai F., Ebina Y., Miyatake A., Tanabe T. Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase // Biochim. Biophys. Acta. 1994. V. 1210. P. 308-316.</mixed-citation><mixed-citation xml:lang="en">Suzuki H., Kishimoto K., Yoshimoto T., Yamamoto S., Kanai F., Ebina Y., Miyatake A., Tanabe T. Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase // Biochim. Biophys. Acta. 1994. V. 1210. P. 308-316.</mixed-citation></citation-alternatives></ref><ref id="cit96"><label>96</label><citation-alternatives><mixed-citation xml:lang="ru">Schwarz K., Walther M., Anton M., Gerth C., Feussner I., Kuhn H. Structural basis for lipoxygenase specificity. Conversion of the human leukocyte 5-lipoxygenase to a 15-lipoxygenating enzyme species by site-directed mutagenesis // J. Biol. Chem. 2001. V. 276. P. 773-779.</mixed-citation><mixed-citation xml:lang="en">Schwarz K., Walther M., Anton M., Gerth C., Feussner I., Kuhn H. Structural basis for lipoxygenase specificity. Conversion of the human leukocyte 5-lipoxygenase to a 15-lipoxygenating enzyme species by site-directed mutagenesis // J. Biol. Chem. 2001. V. 276. P. 773-779.</mixed-citation></citation-alternatives></ref><ref id="cit97"><label>97</label><citation-alternatives><mixed-citation xml:lang="ru">Hornung E., Rosahl S., Kuhn H., Feussner I. Creating lipoxygenases with new positional specificities by site-directed mutagenesis // Biochem. Soc. Trans. 2000. V. 28. P. 825-826.</mixed-citation><mixed-citation xml:lang="en">Hornung E., Rosahl S., Kuhn H., Feussner I. Creating lipoxygenases with new positional specificities by site-directed mutagenesis // Biochem. Soc. Trans. 2000. V. 28. P. 825-826.</mixed-citation></citation-alternatives></ref><ref id="cit98"><label>98</label><citation-alternatives><mixed-citation xml:lang="ru">Toledo L., Masgrau L., Marechal J.D., Lluch J.M., Gonzalez-Lafont A. nsights into the mechanism of binding of arachidonic acid to mammalian 15-lipoxygenases // J. Phys. Chem. B. 2010. V. 114. P. 7037-7046.</mixed-citation><mixed-citation xml:lang="en">Toledo L., Masgrau L., Marechal J.D., Lluch J.M., Gonzalez-Lafont A. nsights into the mechanism of binding of arachidonic acid to mammalian 15-lipoxygenases // J. Phys. Chem. B. 2010. V. 114. P. 7037-7046.</mixed-citation></citation-alternatives></ref><ref id="cit99"><label>99</label><citation-alternatives><mixed-citation xml:lang="ru">Toledo L., Masgrau L., Lluch J.M., Gonzalez-Lafont A. Substrate binding to mammalian 15-lipoxygenase // J. Comput. Aided Mol. Des. 2011. V. 25. P. 825-835.</mixed-citation><mixed-citation xml:lang="en">Toledo L., Masgrau L., Lluch J.M., Gonzalez-Lafont A. Substrate binding to mammalian 15-lipoxygenase // J. Comput. Aided Mol. Des. 2011. V. 25. P. 825-835.</mixed-citation></citation-alternatives></ref><ref id="cit100"><label>100</label><citation-alternatives><mixed-citation xml:lang="ru">Jisaka M., Kim R.B., Boeglin W.E., Brash A.R. Identification of amino acid determinants of the positional specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2 // J. Biol. Chem. 2000. V. 275. P. 1287-1293.</mixed-citation><mixed-citation xml:lang="en">Jisaka M., Kim R.B., Boeglin W.E., Brash A.R. Identification of amino acid determinants of the positional specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2 // J. Biol. Chem. 2000. V. 275. P. 1287-1293.</mixed-citation></citation-alternatives></ref><ref id="cit101"><label>101</label><citation-alternatives><mixed-citation xml:lang="ru">Veldink G.A., Garssen G.J., Vliegenthart J.F., Boldingh J. Positional specificity of corn germ lipoxygenase as a function of pH // Biochem. Biophys. Res. Commun. 1972. V. 47. P. 22-26.</mixed-citation><mixed-citation xml:lang="en">Veldink G.A., Garssen G.J., Vliegenthart J.F., Boldingh J. Positional specificity of corn germ lipoxygenase as a function of pH // Biochem. Biophys. Res. Commun. 1972. V. 47. P. 22-26.</mixed-citation></citation-alternatives></ref><ref id="cit102"><label>102</label><citation-alternatives><mixed-citation xml:lang="ru">Hornung E., Kunze S., Liavonchanka A., Zimmermann G., Kuhn D., Fritsche K., Renz A., Kuhn H., Feussner I. Identification of an amino acid determinant of pH regiospecificity in a seed lipoxygenase from Momordica charantia // Phytochemistry. 2008. V. 69. P. 2774-2780.</mixed-citation><mixed-citation xml:lang="en">Hornung E., Kunze S., Liavonchanka A., Zimmermann G., Kuhn D., Fritsche K., Renz A., Kuhn H., Feussner I. Identification of an amino acid determinant of pH regiospecificity in a seed lipoxygenase from Momordica charantia // Phytochemistry. 2008. V. 69. P. 2774-2780.</mixed-citation></citation-alternatives></ref><ref id="cit103"><label>103</label><citation-alternatives><mixed-citation xml:lang="ru">Falgueyret J.P., Denis D., Macdonald D., Hutchinson J.H., Riendeau D. Characterization of the arachidonate and ATP binding sites of human 5-lipoxygenase using photoaffinity labeling and enzyme immobilization // Biochemistry. 1995. V. 34. P. 13603-13611.</mixed-citation><mixed-citation xml:lang="en">Falgueyret J.P., Denis D., Macdonald D., Hutchinson J.H., Riendeau D. Characterization of the arachidonate and ATP binding sites of human 5-lipoxygenase using photoaffinity labeling and enzyme immobilization // Biochemistry. 1995. V. 34. P. 13603-13611.</mixed-citation></citation-alternatives></ref><ref id="cit104"><label>104</label><citation-alternatives><mixed-citation xml:lang="ru">Mogul R., Johansen E., Holman T.R. Oleyl sulfate reveals allosteric inhibition of soybean lipoxygenase-1 and human 15-lipoxygenase // Biochemistry. 2000. V. 39. P. 4801-4807.</mixed-citation><mixed-citation xml:lang="en">Mogul R., Johansen E., Holman T.R. Oleyl sulfate reveals allosteric inhibition of soybean lipoxygenase-1 and human 15-lipoxygenase // Biochemistry. 2000. V. 39. P. 4801-4807.</mixed-citation></citation-alternatives></ref><ref id="cit105"><label>105</label><citation-alternatives><mixed-citation xml:lang="ru">Wecksler A.T., Jacquot C., van der Donk W.A., Holman T. Mechanistic investigations of human reticulocyte 15- and platelet 12-lipoxygenases with arachidonic acid // Biochemistry. 2009. V. 48. P. 6259-6267.</mixed-citation><mixed-citation xml:lang="en">Wecksler A.T., Jacquot C., van der Donk W.A., Holman T. Mechanistic investigations of human reticulocyte 15- and platelet 12-lipoxygenases with arachidonic acid // Biochemistry. 2009. V. 48. P. 6259-6267.</mixed-citation></citation-alternatives></ref><ref id="cit106"><label>106</label><citation-alternatives><mixed-citation xml:lang="ru">Wecksler A.T., Kenyon V., Deschamps J.D., Holman T.R. Substrate specificity changes for human reticulocyte and epithelial 15-lipoxygenases reveal allosteric product regulation // Biochemistry. 2008. V. 47. P. 7364-7375.</mixed-citation><mixed-citation xml:lang="en">Wecksler A.T., Kenyon V., Deschamps J.D., Holman T.R. Substrate specificity changes for human reticulocyte and epithelial 15-lipoxygenases reveal allosteric product regulation // Biochemistry. 2008. V. 47. P. 7364-7375.</mixed-citation></citation-alternatives></ref><ref id="cit107"><label>107</label><citation-alternatives><mixed-citation xml:lang="ru">Wecksler A.T., Garcia N.K., Holman T.R. Substrate specificity effects of lipoxygenase products and inhibitors on soybean lipoxygenase-1 // Bioorg. Med. Chem. 2009. V. 17. P. 6534-6539.</mixed-citation><mixed-citation xml:lang="en">Wecksler A.T., Garcia N.K., Holman T.R. Substrate specificity effects of lipoxygenase products and inhibitors on soybean lipoxygenase-1 // Bioorg. Med. Chem. 2009. V. 17. P. 6534-6539.</mixed-citation></citation-alternatives></ref><ref id="cit108"><label>108</label><citation-alternatives><mixed-citation xml:lang="ru">Ivanov I., Shang W., Toledo L., Masgrau L., Svergun D.I., Stehling S., Gomez H., Di Venere A., Mei G., Lluch J.M., Skrzypczak-Jankun E., Gonzalez-Lafont A., Kuhn H. Ligand-induced formation of transient dimers of mammalian 12/15-lipoxygenase: A key to allosteric behavior of this class of enzymes? // Proteins. 2012. V. 80. P. 703-712.</mixed-citation><mixed-citation xml:lang="en">Ivanov I., Shang W., Toledo L., Masgrau L., Svergun D.I., Stehling S., Gomez H., Di Venere A., Mei G., Lluch J.M., Skrzypczak-Jankun E., Gonzalez-Lafont A., Kuhn H. Ligand-induced formation of transient dimers of mammalian 12/15-lipoxygenase: A key to allosteric behavior of this class of enzymes? // Proteins. 2012. V. 80. P. 703-712.</mixed-citation></citation-alternatives></ref><ref id="cit109"><label>109</label><citation-alternatives><mixed-citation xml:lang="ru">Aleem A.M., Jankun J., Dignam J.D., Walther M., Kuhn H., Svergun D.I., Skrzypczak-Jankun E. Human platelet 12-lipoxygenase, new findings about its activity, membrane binding and low-resolution structure // J. Mol. Biol. 2008. V. 376. P. 193-209.</mixed-citation><mixed-citation xml:lang="en">Aleem A.M., Jankun J., Dignam J.D., Walther M., Kuhn H., Svergun D.I., Skrzypczak-Jankun E. Human platelet 12-lipoxygenase, new findings about its activity, membrane binding and low-resolution structure // J. Mol. Biol. 2008. V. 376. P. 193-209.</mixed-citation></citation-alternatives></ref><ref id="cit110"><label>110</label><citation-alternatives><mixed-citation xml:lang="ru">Häfner A.K., Cernescu M., Hofmann B., Ermisch M., Hörnig M., Metzner J., Schneider G., Brutschy B., Steinhilber D. Dimerization of human 5-lypoxygenase // Biol. Chem. 2011. V. 392. P. 1097-1111.</mixed-citation><mixed-citation xml:lang="en">Häfner A.K., Cernescu M., Hofmann B., Ermisch M., Hörnig M., Metzner J., Schneider G., Brutschy B., Steinhilber D. Dimerization of human 5-lypoxygenase // Biol. Chem. 2011. V. 392. P. 1097-1111.</mixed-citation></citation-alternatives></ref><ref id="cit111"><label>111</label><citation-alternatives><mixed-citation xml:lang="ru">Oliw E.H. Plant and fungal lipoxygenases // Prostaglandins Other Lipid Mediators. 2002. V. 68-69. P. 313-323.</mixed-citation><mixed-citation xml:lang="en">Oliw E.H. Plant and fungal lipoxygenases // Prostaglandins Other Lipid Mediators. 2002. V. 68-69. P. 313-323.</mixed-citation></citation-alternatives></ref><ref id="cit112"><label>112</label><citation-alternatives><mixed-citation xml:lang="ru">De Petrocellis L., Di Marzo V. Aquatic invertebrates open up new perspectives in eicosanoid research: Biosynthesis and bioactivity // Prostaglandins Leukotrienes Essent. Fatty Acids 1994. V. 51. P. 215-229.</mixed-citation><mixed-citation xml:lang="en">De Petrocellis L., Di Marzo V. Aquatic invertebrates open up new perspectives in eicosanoid research: Biosynthesis and bioactivity // Prostaglandins Leukotrienes Essent. Fatty Acids 1994. V. 51. P. 215-229.</mixed-citation></citation-alternatives></ref><ref id="cit113"><label>113</label><citation-alternatives><mixed-citation xml:lang="ru">Hawkins D.J., Brash A.R. Eggs of the sea urchin, Strongylocentrotus purpuratus, contain a prominent (11R) and (12R) lipoxygenase activity // J. Biol. Chem. 1987. V. 262. P. 7629-7634.</mixed-citation><mixed-citation xml:lang="en">Hawkins D.J., Brash A.R. Eggs of the sea urchin, Strongylocentrotus purpuratus, contain a prominent (11R) and (12R) lipoxygenase activity // J. Biol. Chem. 1987. V. 262. P. 7629-7634.</mixed-citation></citation-alternatives></ref><ref id="cit114"><label>114</label><citation-alternatives><mixed-citation xml:lang="ru">Porta H., Rocha-Sosa M. Lipoxygenases in bacteria: Horizontal transfer event? // Microbiology. 2001. V. 147. P. 3199-3200.</mixed-citation><mixed-citation xml:lang="en">Porta H., Rocha-Sosa M. Lipoxygenases in bacteria: Horizontal transfer event? // Microbiology. 2001. V. 147. P. 3199-3200.</mixed-citation></citation-alternatives></ref><ref id="cit115"><label>115</label><citation-alternatives><mixed-citation xml:lang="ru">Vance R.E., Hong S., Gronert K., Serhan C.N., Mekalanos J.J. The opportunistic pathogen Pseudomonas aeruginosa carries a secretable arachidonate 15-lipoxygenase // Proc. Natl. Acad. Sci. USA. 2004. V. 101. P. 2135-2139.</mixed-citation><mixed-citation xml:lang="en">Vance R.E., Hong S., Gronert K., Serhan C.N., Mekalanos J.J. The opportunistic pathogen Pseudomonas aeruginosa carries a secretable arachidonate 15-lipoxygenase // Proc. Natl. Acad. Sci. USA. 2004. V. 101. P. 2135-2139.</mixed-citation></citation-alternatives></ref><ref id="cit116"><label>116</label><citation-alternatives><mixed-citation xml:lang="ru">Koeduka T., Kajiwara T., Matsui K. Cloning of lipoxygenase genes from a cyanobacteria, Nostoc punctiforme, and its expression in Eschelichia coli // Curr. Microbiol. 2007. V. 54. P. 315-319.</mixed-citation><mixed-citation xml:lang="en">Koeduka T., Kajiwara T., Matsui K. Cloning of lipoxygenase genes from a cyanobacteria, Nostoc punctiforme, and its expression in Eschelichia coli // Curr. Microbiol. 2007. V. 54. P. 315-319.</mixed-citation></citation-alternatives></ref><ref id="cit117"><label>117</label><citation-alternatives><mixed-citation xml:lang="ru">Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U., Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L., Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J., Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L., Rokhsar D.S. The Trichoplax genome and the nature of placozoans // Nature. 2008. V. 454. P. 955-960.</mixed-citation><mixed-citation xml:lang="en">Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U., Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L., Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J., Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L., Rokhsar D.S. The Trichoplax genome and the nature of placozoans // Nature. 2008. V. 454. P. 955-960.</mixed-citation></citation-alternatives></ref><ref id="cit118"><label>118</label><citation-alternatives><mixed-citation xml:lang="ru">Bannenberg G., Martinez M., Hamberg M., Castresana C. Diversity of the enzymatic activity in the lipoxygenase gene family of Arabidopsis thaliana // Lipids. 2009. V. 44. P. 85-95.</mixed-citation><mixed-citation xml:lang="en">Bannenberg G., Martinez M., Hamberg M., Castresana C. Diversity of the enzymatic activity in the lipoxygenase gene family of Arabidopsis thaliana // Lipids. 2009. V. 44. P. 85-95.</mixed-citation></citation-alternatives></ref><ref id="cit119"><label>119</label><citation-alternatives><mixed-citation xml:lang="ru">Toh H., Yokoyama C., Tanabe T., Yoshimoto T., Yamamoto S. Molecular evolution of cyclo-oxygenase and lipoxygenase // Prostaglandins. 1992. V. 44. P. 291-315.</mixed-citation><mixed-citation xml:lang="en">Toh H., Yokoyama C., Tanabe T., Yoshimoto T., Yamamoto S. Molecular evolution of cyclo-oxygenase and lipoxygenase // Prostaglandins. 1992. V. 44. P. 291-315.</mixed-citation></citation-alternatives></ref><ref id="cit120"><label>120</label><citation-alternatives><mixed-citation xml:lang="ru">Shin J.H., Van K., Kim D.H., Kim K.D., Jang Y.E., Choi B.S., Kim M.Y., Lee S.H. The lipoxygenase gene family: A genomic fossil of shared polyploidy between Glycine max and Medicago truncatula // BMC Plant Biol. 2008. V. 8. P. 133.</mixed-citation><mixed-citation xml:lang="en">Shin J.H., Van K., Kim D.H., Kim K.D., Jang Y.E., Choi B.S., Kim M.Y., Lee S.H. The lipoxygenase gene family: A genomic fossil of shared polyploidy between Glycine max and Medicago truncatula // BMC Plant Biol. 2008. V. 8. P. 133.</mixed-citation></citation-alternatives></ref><ref id="cit121"><label>121</label><citation-alternatives><mixed-citation xml:lang="ru">Andreou A.Z., Vanko M., Bezakova L., Feussner I. Properties of a mini 9R-lipoxygenase from Nostoc sp. PCC 7120 and its mutant forms // Phytochemistry. 2008. V. 69. P. 1832-1837.</mixed-citation><mixed-citation xml:lang="en">Andreou A.Z., Vanko M., Bezakova L., Feussner I. Properties of a mini 9R-lipoxygenase from Nostoc sp. PCC 7120 and its mutant forms // Phytochemistry. 2008. V. 69. P. 1832-1837.</mixed-citation></citation-alternatives></ref><ref id="cit122"><label>122</label><citation-alternatives><mixed-citation xml:lang="ru">Lang I., Feussner I. Oxylipin formation in Nostoc punctiforme (PCC73102) // Phytochemistry. 2007. V. 68. P. 1120-1127.</mixed-citation><mixed-citation xml:lang="en">Lang I., Feussner I. Oxylipin formation in Nostoc punctiforme (PCC73102) // Phytochemistry. 2007. V. 68. P. 1120-1127.</mixed-citation></citation-alternatives></ref><ref id="cit123"><label>123</label><citation-alternatives><mixed-citation xml:lang="ru">Lang I., Gobel C., Porzel A., Heilmann I., Feussner I. A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120 // Biochem. J. 2008. V. 410. P. 347-357.</mixed-citation><mixed-citation xml:lang="en">Lang I., Gobel C., Porzel A., Heilmann I., Feussner I. A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120 // Biochem. J. 2008. V. 410. P. 347-357.</mixed-citation></citation-alternatives></ref><ref id="cit124"><label>124</label><citation-alternatives><mixed-citation xml:lang="ru">Andreou A., Gobel C., Hamberg M., Feussner I. A bisallylic mini-lipoxygenase from cyanobacterium Cyanothece sp. that has an iron as cofactor // J. Biol. Chem. 2010. V. 285. P. 14178-14186.</mixed-citation><mixed-citation xml:lang="en">Andreou A., Gobel C., Hamberg M., Feussner I. A bisallylic mini-lipoxygenase from cyanobacterium Cyanothece sp. that has an iron as cofactor // J. Biol. Chem. 2010. V. 285. P. 14178-14186.</mixed-citation></citation-alternatives></ref><ref id="cit125"><label>125</label><citation-alternatives><mixed-citation xml:lang="ru">Mereschkowski C. Über Natur und Ursprung der Chromatophoren im Pflanzenreiche // Biol. Centralbl. 1905. B. 25. S. 593-604.</mixed-citation><mixed-citation xml:lang="en">Mereschkowski C. Über Natur und Ursprung der Chromatophoren im Pflanzenreiche // Biol. Centralbl. 1905. B. 25. S. 593-604.</mixed-citation></citation-alternatives></ref><ref id="cit126"><label>126</label><citation-alternatives><mixed-citation xml:lang="ru">Sagan L. On the origin of mitosing cells // J. Theor. Biol. 1967. V. 14. P. 255-274.</mixed-citation><mixed-citation xml:lang="en">Sagan L. On the origin of mitosing cells // J. Theor. Biol. 1967. V. 14. P. 255-274.</mixed-citation></citation-alternatives></ref><ref id="cit127"><label>127</label><citation-alternatives><mixed-citation xml:lang="ru">Huang C.Y., Ayliffe M.A., Timmis J.N. Direct measurement of the transfer rate of chloroplast DNA into the nucleus // Nature. 2003. V. 422. P. 72-76.</mixed-citation><mixed-citation xml:lang="en">Huang C.Y., Ayliffe M.A., Timmis J.N. Direct measurement of the transfer rate of chloroplast DNA into the nucleus // Nature. 2003. V. 422. P. 72-76.</mixed-citation></citation-alternatives></ref><ref id="cit128"><label>128</label><citation-alternatives><mixed-citation xml:lang="ru">Maliga P. Plant biology: Mobile plastid genes // Nature. 2003. V. 422. P. 31-32.</mixed-citation><mixed-citation xml:lang="en">Maliga P. Plant biology: Mobile plastid genes // Nature. 2003. V. 422. P. 31-32.</mixed-citation></citation-alternatives></ref><ref id="cit129"><label>129</label><citation-alternatives><mixed-citation xml:lang="ru">Huang C.Y., Ayliffe M.A., Timmis J.N. Simple and complex nuclear loci created by newly transferred chloroplast DNA in tabacco // Proc. Natl. Acad. Sci. USA. 2004. V. 101. P. 9710-9715.</mixed-citation><mixed-citation xml:lang="en">Huang C.Y., Ayliffe M.A., Timmis J.N. Simple and complex nuclear loci created by newly transferred chloroplast DNA in tabacco // Proc. Natl. Acad. Sci. USA. 2004. V. 101. P. 9710-9715.</mixed-citation></citation-alternatives></ref><ref id="cit130"><label>130</label><citation-alternatives><mixed-citation xml:lang="ru">Timmis J.N., Ayliffe M.A., Huang C.Y., Martin W. Endosymbiotic gene transfer: Organelle genomes forge eukaryotic chromosomes // Nat. Rev. Genet. 2004. V. 5. P. 123-135.</mixed-citation><mixed-citation xml:lang="en">Timmis J.N., Ayliffe M.A., Huang C.Y., Martin W. Endosymbiotic gene transfer: Organelle genomes forge eukaryotic chromosomes // Nat. Rev. Genet. 2004. V. 5. P. 123-135.</mixed-citation></citation-alternatives></ref><ref id="cit131"><label>131</label><citation-alternatives><mixed-citation xml:lang="ru">Martin W., Stoebe B., Goremykin V., Hapsmann S., Hasegawa M., Kowallik K.V. Gene transfer to the nucleus and the evolution of chloroplasts // Nature. 1998. V. 393. P. 162-165.</mixed-citation><mixed-citation xml:lang="en">Martin W., Stoebe B., Goremykin V., Hapsmann S., Hasegawa M., Kowallik K.V. Gene transfer to the nucleus and the evolution of chloroplasts // Nature. 1998. V. 393. P. 162-165.</mixed-citation></citation-alternatives></ref><ref id="cit132"><label>132</label><citation-alternatives><mixed-citation xml:lang="ru">Barsan C., Sanchez-Bel P., Rombaldi C., Egea I., Rossignol M., Kuntz M., Zouine M., Latche A., Bouzayen M., Pech J.C. Characteristics of the tomato chromoplast revealed by proteomic analysis // J. Exp. Bot. 2010. V. 61. P. 2413-2431.</mixed-citation><mixed-citation xml:lang="en">Barsan C., Sanchez-Bel P., Rombaldi C., Egea I., Rossignol M., Kuntz M., Zouine M., Latche A., Bouzayen M., Pech J.C. Characteristics of the tomato chromoplast revealed by proteomic analysis // J. Exp. Bot. 2010. V. 61. P. 2413-2431.</mixed-citation></citation-alternatives></ref><ref id="cit133"><label>133</label><citation-alternatives><mixed-citation xml:lang="ru">Johannesson M., Backman L., Claesson H.E., Forsell P.K. Cloning, purification and characterization of non-human primate 12/15-lipoxygenases // Prostaglandins Leukotrienes Essent. Fatty Acids. 2010. V. 82. P. 121-129.</mixed-citation><mixed-citation xml:lang="en">Johannesson M., Backman L., Claesson H.E., Forsell P.K. Cloning, purification and characterization of non-human primate 12/15-lipoxygenases // Prostaglandins Leukotrienes Essent. Fatty Acids. 2010. V. 82. P. 121-129.</mixed-citation></citation-alternatives></ref><ref id="cit134"><label>134</label><citation-alternatives><mixed-citation xml:lang="ru">Yoshimoto T., Suzuki H., Yamamoto S., Takai T., Yokoyama C., Tanabe T. Cloning and sequence analysis of the cDNA for arachidonate 12-lipoxygenase of porcine leukocytes // Proc. Natl. Acad. Sci. USA. 1990. V. 87. P. 2142-2146.</mixed-citation><mixed-citation xml:lang="en">Yoshimoto T., Suzuki H., Yamamoto S., Takai T., Yokoyama C., Tanabe T. Cloning and sequence analysis of the cDNA for arachidonate 12-lipoxygenase of porcine leukocytes // Proc. Natl. Acad. Sci. USA. 1990. V. 87. P. 2142-2146.</mixed-citation></citation-alternatives></ref><ref id="cit135"><label>135</label><citation-alternatives><mixed-citation xml:lang="ru">Chen X.S., Kurre U., Jenkins N.A., Copeland N.G., Funk C.D. cDNA cloning, expression, mutagenesis of C-terminal isoleucine, genomic structure, and chromosomal localizations of murine 12-lipoxygenases // J. Biol. Chem. 1994. V. 269. P. 13979-13987.</mixed-citation><mixed-citation xml:lang="en">Chen X.S., Kurre U., Jenkins N.A., Copeland N.G., Funk C.D. cDNA cloning, expression, mutagenesis of C-terminal isoleucine, genomic structure, and chromosomal localizations of murine 12-lipoxygenases // J. Biol. Chem. 1994. V. 269. P. 13979-13987.</mixed-citation></citation-alternatives></ref><ref id="cit136"><label>136</label><citation-alternatives><mixed-citation xml:lang="ru">Watanabe T., Medina J.F., Haeggstrom J.Z., Radmark O., Samuelsson B. Molecular cloning of a 12-lipoxygenase cDNA from rat brain // Eur. J. Biochem. 1993. V. 212. P. 605-612.</mixed-citation><mixed-citation xml:lang="en">Watanabe T., Medina J.F., Haeggstrom J.Z., Radmark O., Samuelsson B. Molecular cloning of a 12-lipoxygenase cDNA from rat brain // Eur. J. Biochem. 1993. V. 212. P. 605-612.</mixed-citation></citation-alternatives></ref><ref id="cit137"><label>137</label><citation-alternatives><mixed-citation xml:lang="ru">Berger M., Schwarz K., Thiele H., Reimann I., Huth A., Borngraber S., Kuhn H., Thiele B.J. Simultaneous expression of leukocyte-type 12-lipoxygenase and reticulocyte-type 15-lipoxygenase in rabbits // J. Mol. Biol. 1998. V. 278. P. 935-948.</mixed-citation><mixed-citation xml:lang="en">Berger M., Schwarz K., Thiele H., Reimann I., Huth A., Borngraber S., Kuhn H., Thiele B.J. Simultaneous expression of leukocyte-type 12-lipoxygenase and reticulocyte-type 15-lipoxygenase in rabbits // J. Mol. Biol. 1998. V. 278. P. 935-948.</mixed-citation></citation-alternatives></ref><ref id="cit138"><label>138</label><citation-alternatives><mixed-citation xml:lang="ru">Sun D., Funk C.D. Disruption of 12/15-lipoxygenase expression in peritoneal macrophages. Enhanced utilization of the 5-lipoxygenase pathway and diminished oxidation of low density lipoprotein // J. Biol. Chem. 1996. V. 271. P. 24055-24062.</mixed-citation><mixed-citation xml:lang="en">Sun D., Funk C.D. Disruption of 12/15-lipoxygenase expression in peritoneal macrophages. Enhanced utilization of the 5-lipoxygenase pathway and diminished oxidation of low density lipoprotein // J. Biol. Chem. 1996. V. 271. P. 24055-24062.</mixed-citation></citation-alternatives></ref><ref id="cit139"><label>139</label><citation-alternatives><mixed-citation xml:lang="ru">Chen X.S., Sheller J.R., Johnson E.N., Funk C.D. Role of leukotrienes revealed by targeted disruption of the 5-lipoxygenase gene // Nature. 1994. V. 372. P. 179-182.</mixed-citation><mixed-citation xml:lang="en">Chen X.S., Sheller J.R., Johnson E.N., Funk C.D. Role of leukotrienes revealed by targeted disruption of the 5-lipoxygenase gene // Nature. 1994. V. 372. P. 179-182.</mixed-citation></citation-alternatives></ref><ref id="cit140"><label>140</label><citation-alternatives><mixed-citation xml:lang="ru">Johnson E.N., Brass L.F., Funk C.D. Increased platelet sensitivity to ADP in mice lacking platelet-type 12-lipoxygenase // Proc. Natl. Acad. Sci. USA. 1998. V. 95. P. 3100-3105.</mixed-citation><mixed-citation xml:lang="en">Johnson E.N., Brass L.F., Funk C.D. Increased platelet sensitivity to ADP in mice lacking platelet-type 12-lipoxygenase // Proc. Natl. Acad. Sci. USA. 1998. V. 95. P. 3100-3105.</mixed-citation></citation-alternatives></ref><ref id="cit141"><label>141</label><citation-alternatives><mixed-citation xml:lang="ru">Poeckel D., Zemski Berry K.A., Murphy R.C., Funk C.D. Dual 12/15- and 5-lipoxygenase deficiency in macrophages alters arachidonic acid metabolism and attenuates peritonitis and atherosclerosis in ApoE knock-out mice // J. Biol. Chem. 2009. V. 284. P. 21077-21089.</mixed-citation><mixed-citation xml:lang="en">Poeckel D., Zemski Berry K.A., Murphy R.C., Funk C.D. Dual 12/15- and 5-lipoxygenase deficiency in macrophages alters arachidonic acid metabolism and attenuates peritonitis and atherosclerosis in ApoE knock-out mice // J. Biol. Chem. 2009. V. 284. P. 21077-21089.</mixed-citation></citation-alternatives></ref><ref id="cit142"><label>142</label><citation-alternatives><mixed-citation xml:lang="ru">Porta H., Rocha-Sosa M. Plant lipoxygenases. Physiological and molecular features // Plant Physiol. 2002. V. 130. P. 15-21.</mixed-citation><mixed-citation xml:lang="en">Porta H., Rocha-Sosa M. Plant lipoxygenases. Physiological and molecular features // Plant Physiol. 2002. V. 130. P. 15-21.</mixed-citation></citation-alternatives></ref><ref id="cit143"><label>143</label><citation-alternatives><mixed-citation xml:lang="ru">Feussner I., Wasternack C., Kindl H., Kuhn H. Lipoxygenase-catalyzed oxygenation of storage lipids is implicated in lipid mobilization during germination // Proc. Natl. Acad. Sci. USA. 1995. V. 92. P. 11849-11853.</mixed-citation><mixed-citation xml:lang="en">Feussner I., Wasternack C., Kindl H., Kuhn H. Lipoxygenase-catalyzed oxygenation of storage lipids is implicated in lipid mobilization during germination // Proc. Natl. Acad. Sci. USA. 1995. V. 92. P. 11849-11853.</mixed-citation></citation-alternatives></ref><ref id="cit144"><label>144</label><citation-alternatives><mixed-citation xml:lang="ru">Bousquet J.F., Thimann K.V. Lipid peroxidation forms ethylene from 1-aminocyclopropane-1-carboxylic acid and may operate in leaf senescence // Proc. Natl. Acad. Sci. USA. 1984. V. 81. P. 1724-1727.</mixed-citation><mixed-citation xml:lang="en">Bousquet J.F., Thimann K.V. Lipid peroxidation forms ethylene from 1-aminocyclopropane-1-carboxylic acid and may operate in leaf senescence // Proc. Natl. Acad. Sci. USA. 1984. V. 81. P. 1724-1727.</mixed-citation></citation-alternatives></ref><ref id="cit145"><label>145</label><citation-alternatives><mixed-citation xml:lang="ru">He Y., Fukushige H., Hildebrand D.F., Gan S. Evidence supporting a role of jasmonic acid in arabidopsis leaf senescence // Plant Physiol. 2002. V. 128. P. 876-884.</mixed-citation><mixed-citation xml:lang="en">He Y., Fukushige H., Hildebrand D.F., Gan S. Evidence supporting a role of jasmonic acid in arabidopsis leaf senescence // Plant Physiol. 2002. V. 128. P. 876-884.</mixed-citation></citation-alternatives></ref><ref id="cit146"><label>146</label><citation-alternatives><mixed-citation xml:lang="ru">Chen G., Hackett R., Walker D., Taylor A., Lin Z., Grierson D. Identification of a specific isoform of tomato lipoxygenase (TomloxC) involved in the generation of fatty acid-derived flavor compounds // Plant Physiol. 2004. V. 136. P. 2641-2651.</mixed-citation><mixed-citation xml:lang="en">Chen G., Hackett R., Walker D., Taylor A., Lin Z., Grierson D. Identification of a specific isoform of tomato lipoxygenase (TomloxC) involved in the generation of fatty acid-derived flavor compounds // Plant Physiol. 2004. V. 136. P. 2641-2651.</mixed-citation></citation-alternatives></ref><ref id="cit147"><label>147</label><citation-alternatives><mixed-citation xml:lang="ru">Ridolfi M., Terenziani S., Patumi M., Fontanazza G. Characterization of the lipoxygenases in some olive cultivars and determination of their role in volatile compounds formation // J. Agric. Food Chem. 2002. V. 50. P. 835-839.</mixed-citation><mixed-citation xml:lang="en">Ridolfi M., Terenziani S., Patumi M., Fontanazza G. Characterization of the lipoxygenases in some olive cultivars and determination of their role in volatile compounds formation // J. Agric. Food Chem. 2002. V. 50. P. 835-839.</mixed-citation></citation-alternatives></ref><ref id="cit148"><label>148</label><citation-alternatives><mixed-citation xml:lang="ru">Song W.C., Brash A.R. Investigation of the allene oxide pathway in the coral Plexaura homomalla: Formation of novel ketols and isomers of prostaglandin A2 from 15-hydroxyeicosatetraenoic acid // Arch. Biochem. Biophys. 1991. V. 290. P. 427-435.</mixed-citation><mixed-citation xml:lang="en">Song W.C., Brash A.R. Investigation of the allene oxide pathway in the coral Plexaura homomalla: Formation of novel ketols and isomers of prostaglandin A2 from 15-hydroxyeicosatetraenoic acid // Arch. Biochem. Biophys. 1991. V. 290. P. 427-435.</mixed-citation></citation-alternatives></ref><ref id="cit149"><label>149</label><citation-alternatives><mixed-citation xml:lang="ru">Aparoy P., Reddy R.N., Guruprasad L., Reddy M.R., Reddanna P. Homology modeling of 5-lipoxygenase and hints for better inhibitor design // J. Comput. Aided Mol. Des. 2008. V. 22. P. 611-619.</mixed-citation><mixed-citation xml:lang="en">Aparoy P., Reddy R.N., Guruprasad L., Reddy M.R., Reddanna P. Homology modeling of 5-lipoxygenase and hints for better inhibitor design // J. Comput. Aided Mol. Des. 2008. V. 22. P. 611-619.</mixed-citation></citation-alternatives></ref><ref id="cit150"><label>150</label><citation-alternatives><mixed-citation xml:lang="ru">Di Venere A., Horn T., Stehling S., Mei G., Masgrau L., González-Lafont A., Kühn H., Ivanov I. Role of Arg403 for thermostability and catalytic activity of rabbit 12/15-lipoxygenase // Biochim. Biophys. Acta. 2013. V. 1831. P. 1079-1088.</mixed-citation><mixed-citation xml:lang="en">Di Venere A., Horn T., Stehling S., Mei G., Masgrau L., González-Lafont A., Kühn H., Ivanov I. Role of Arg403 for thermostability and catalytic activity of rabbit 12/15-lipoxygenase // Biochim. Biophys. Acta. 2013. V. 1831. P. 1079-1088.</mixed-citation></citation-alternatives></ref><ref id="cit151"><label>151</label><citation-alternatives><mixed-citation xml:lang="ru">Di Venere A., Nicolai E., Ivanov I., Dainese E., Adel S., Angelucci B.C., Kuhn H., Maccarrone M., Mei G. Probing conformational changes in lipoxygenases upon membrane binding: Fine-tuning by the active site inhibitor ETYA // Biochim. Biophys. Acta. 2014. V. 1841. P. 1-10.</mixed-citation><mixed-citation xml:lang="en">Di Venere A., Nicolai E., Ivanov I., Dainese E., Adel S., Angelucci B.C., Kuhn H., Maccarrone M., Mei G. Probing conformational changes in lipoxygenases upon membrane binding: Fine-tuning by the active site inhibitor ETYA // Biochim. Biophys. Acta. 2014. V. 1841. P. 1-10.</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
