메뉴 건너뛰기




Volumn 1821, Issue 12, 2012, Pages 1508-1517

Novel insights into cyclooxygenases, linoleate diol synthases, and lipoxygenases from deuterium kinetic isotope effects and oxidation of substrate analogs

Author keywords

Animal heme peroxidase; Chiral phase HPLC; Fatty acid oxygenation; Kinetic isotope effect; Mass spectrometry; Oxygenation mechanism

Indexed keywords

CARBON; DEUTERIUM; ENZYME; FATTY ACID; HYDROGEN; ISOTOPE; LINOLEATE DIOL SYNTHASE; LIPOXYGENASE; PROSTAGLANDIN SYNTHASE; UNCLASSIFIED DRUG;

EID: 84866530943     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2012.09.001     Document Type: Article
Times cited : (13)

References (45)
  • 1
    • 34248596797 scopus 로고    scopus 로고
    • Control of oxygenation in lipoxygenase and cyclooxygenase catalysis
    • C. Schneider, D.A. Pratt, N.A. Porter, and A.R. Brash Control of oxygenation in lipoxygenase and cyclooxygenase catalysis Chem. Biol. 14 2007 473 488
    • (2007) Chem. Biol. , vol.14 , pp. 473-488
    • Schneider, C.1    Pratt, D.A.2    Porter, N.A.3    Brash, A.R.4
  • 2
    • 70350489461 scopus 로고    scopus 로고
    • Lipoxygenases - Structure and reaction mechanism
    • A. Andreou, and I. Feussner Lipoxygenases - structure and reaction mechanism Phytochemistry 70 2009 1504 1510
    • (2009) Phytochemistry , vol.70 , pp. 1504-1510
    • Andreou, A.1    Feussner, I.2
  • 3
    • 80054052917 scopus 로고    scopus 로고
    • Lipoxygenase and leukotriene pathways: Biochemistry, biology, and roles in disease
    • J.Z. Haeggström, and C.D. Funk Lipoxygenase and leukotriene pathways: biochemistry, biology, and roles in disease Chem. Rev. 111 2011 5866 5898
    • (2011) Chem. Rev. , vol.111 , pp. 5866-5898
    • Haeggström, J.Z.1    Funk, C.D.2
  • 4
    • 80054072295 scopus 로고    scopus 로고
    • Enzymes of the cyclooxygenase pathways of prostanoid biosynthesis
    • W.L. Smith, Y. Urade, and P.J. Jakobsson Enzymes of the cyclooxygenase pathways of prostanoid biosynthesis Chem. Rev. 111 2011 5821 5865
    • (2011) Chem. Rev. , vol.111 , pp. 5821-5865
    • Smith, W.L.1    Urade, Y.2    Jakobsson, P.J.3
  • 5
    • 36849034824 scopus 로고    scopus 로고
    • Identification of dioxygenases required for Aspergillus development. studies of products, stereochemistry, and the reaction mechanism
    • U. Garscha, F. Jernerén, D. Chung, N.P. Keller, M. Hamberg, and E.H. Oliw Identification of dioxygenases required for Aspergillus development. studies of products, stereochemistry, and the reaction mechanism J. Biol. Chem. 282 2007 34707 34718
    • (2007) J. Biol. Chem. , vol.282 , pp. 34707-34718
    • Garscha, U.1    Jernerén, F.2    Chung, D.3    Keller, N.P.4    Hamberg, M.5    Oliw, E.H.6
  • 6
    • 79952833264 scopus 로고    scopus 로고
    • Oxylipins in fungi
    • F. Brodhun, and I. Feussner Oxylipins in fungi FEBS J. 278 2011 1047 1063
    • (2011) FEBS J. , vol.278 , pp. 1047-1063
    • Brodhun, F.1    Feussner, I.2
  • 7
    • 84866410538 scopus 로고    scopus 로고
    • Role of 9-lipoxygenase and alpha-dioxygenase oxylipin pathways as modulators of local and systemic defense
    • J. Vicente, T. Cascon, B. Vicedo, P. Garcia-Agustin, M. Hamberg, and C. Castresana Role of 9-lipoxygenase and alpha-dioxygenase oxylipin pathways as modulators of local and systemic defense Mol. Plant 5 2012 914 928
    • (2012) Mol. Plant , vol.5 , pp. 914-928
    • Vicente, J.1    Cascon, T.2    Vicedo, B.3    Garcia-Agustin, P.4    Hamberg, M.5    Castresana, C.6
  • 10
    • 0032557426 scopus 로고    scopus 로고
    • Manganese lipoxygenase. Purification and characterization
    • C. Su, and E.H. Oliw Manganese lipoxygenase. Purification and characterization J. Biol. Chem. 273 1998 13072 13079
    • (1998) J. Biol. Chem. , vol.273 , pp. 13072-13079
    • Su, C.1    Oliw, E.H.2
  • 11
    • 84866356189 scopus 로고    scopus 로고
    • Catalytic convergence of Mn- and iron lipoxygenases by replacement of a single amino acid
    • A. Wennman, F. Jernerén, M. Hamberg, and E.H. Oliw Catalytic convergence of Mn- and iron lipoxygenases by replacement of a single amino acid J. Biol. Chem. 287 2012 31757 31765
    • (2012) J. Biol. Chem. , vol.287 , pp. 31757-31765
    • Wennman, A.1    Jernerén, F.2    Hamberg, M.3    Oliw, E.H.4
  • 12
    • 0036301901 scopus 로고    scopus 로고
    • Environmentally coupled hydrogen tunneling. Linking catalysis to dynamics
    • M.J. Knapp, and J.P. Klinman Environmentally coupled hydrogen tunneling. Linking catalysis to dynamics Eur. J. Biochem. 269 2002 3113 3121
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3113-3121
    • Knapp, M.J.1    Klinman, J.P.2
  • 13
    • 0012297369 scopus 로고
    • The magnitude of the primary kinetic isotope effect for compounds of hydrogen and deuterium
    • F.H. Westheimer The magnitude of the primary kinetic isotope effect for compounds of hydrogen and deuterium Chem. Rev. 61 1961 265 273
    • (1961) Chem. Rev. , vol.61 , pp. 265-273
    • Westheimer, F.H.1
  • 14
    • 39549094013 scopus 로고    scopus 로고
    • Enzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1
    • M.P. Meyer, D.R. Tomchick, and J.P. Klinman Enzyme structure and dynamics affect hydrogen tunneling: the impact of a remote side chain (I553) in soybean lipoxygenase-1 Proc. Natl. Acad. Sci. U. S. A. 105 2008 1146 1151
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 1146-1151
    • Meyer, M.P.1    Tomchick, D.R.2    Klinman, J.P.3
  • 15
    • 0032516915 scopus 로고    scopus 로고
    • A protein radical and ferryl intermediates are generated by linoleate diol synthase, a ferric hemeprotein with dioxygenase and hydroperoxide isomerase activities
    • C. Su, M. Sahlin, and E.H. Oliw A protein radical and ferryl intermediates are generated by linoleate diol synthase, a ferric hemeprotein with dioxygenase and hydroperoxide isomerase activities J. Biol. Chem. 273 1998 20744 20751
    • (1998) J. Biol. Chem. , vol.273 , pp. 20744-20751
    • Su, C.1    Sahlin, M.2    Oliw, E.H.3
  • 16
    • 79952991780 scopus 로고    scopus 로고
    • Cyclooxygenase reaction mechanism of prostaglandin H synthase from deuterium kinetic isotope effects
    • G. Wu, J.M. Lu, W.A. van der Donk, R.J. Kulmacz, and A.L. Tsai Cyclooxygenase reaction mechanism of prostaglandin H synthase from deuterium kinetic isotope effects J. Inorg. Biochem. 105 2011 382 390
    • (2011) J. Inorg. Biochem. , vol.105 , pp. 382-390
    • Wu, G.1    Lu, J.M.2    Van Der Donk, W.A.3    Kulmacz, R.J.4    Tsai, A.L.5
  • 17
    • 50249166700 scopus 로고    scopus 로고
    • Evidence for protein radical-mediated nuclear tunneling in fatty acid alpha-oxygenase
    • A. Gupta, A. Mukherjee, K. Matsui, and J.P. Roth Evidence for protein radical-mediated nuclear tunneling in fatty acid alpha-oxygenase J. Am. Chem. Soc. 130 2008 11274 11275
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11274-11275
    • Gupta, A.1    Mukherjee, A.2    Matsui, K.3    Roth, J.P.4
  • 18
    • 80053465271 scopus 로고    scopus 로고
    • Hydrogen tunneling steps in cyclooxygenase-2 catalysis
    • H.H. Danish, I.S. Doncheva, and J.P. Roth Hydrogen tunneling steps in cyclooxygenase-2 catalysis J. Am. Chem. Soc. 133 2011 15846 15849
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15846-15849
    • Danish, H.H.1    Doncheva, I.S.2    Roth, J.P.3
  • 19
    • 66449133395 scopus 로고    scopus 로고
    • Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450
    • F. Brodhun, C. Göbel, E. Hornung, and I. Feussner Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450 J. Biol. Chem. 284 2009 11792 11805
    • (2009) J. Biol. Chem. , vol.284 , pp. 11792-11805
    • Brodhun, F.1    Göbel, C.2    Hornung, E.3    Feussner, I.4
  • 20
    • 79151469191 scopus 로고    scopus 로고
    • Expression of 5,8-LDS of Aspergillus fumigatus and its dioxygenase domain. A comparison with 7,8-LDS, 10-dioxygenase, and cyclooxygenase
    • I. Hoffmann, F. Jernerén, U. Garscha, and E.H. Oliw Expression of 5,8-LDS of Aspergillus fumigatus and its dioxygenase domain. A comparison with 7,8-LDS, 10-dioxygenase, and cyclooxygenase Arch. Biochem. Biophys. 506 2011 216 222
    • (2011) Arch. Biochem. Biophys. , vol.506 , pp. 216-222
    • Hoffmann, I.1    Jernerén, F.2    Garscha, U.3    Oliw, E.H.4
  • 21
    • 0028260498 scopus 로고
    • Sequential oxygenation of linoleic acid in the fungus Gaeumannomyces graminis: Stereochemistry of dioxygenase and hydroperoxide isomerase reactions
    • M. Hamberg, L.Y. Zhang, I.D. Brodowsky, and E.H. Oliw Sequential oxygenation of linoleic acid in the fungus Gaeumannomyces graminis: stereochemistry of dioxygenase and hydroperoxide isomerase reactions Arch. Biochem. Biophys. 309 1994 77 80
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 77-80
    • Hamberg, M.1    Zhang, L.Y.2    Brodowsky, I.D.3    Oliw, E.H.4
  • 22
    • 79952677027 scopus 로고    scopus 로고
    • Influence of substrate dideuteration on the reaction of the bifunctional heme enzyme psi factor producing oxygenase A (PpoA)
    • A. Nadler, C. Koch, F. Brodhun, J.D. Wehland, K. Tittmann, I. Feussner, and U. Diederichsen Influence of substrate dideuteration on the reaction of the bifunctional heme enzyme psi factor producing oxygenase A (PpoA) Chembiochem 12 2011 728 737
    • (2011) Chembiochem , vol.12 , pp. 728-737
    • Nadler, A.1    Koch, C.2    Brodhun, F.3    Wehland, J.D.4    Tittmann, K.5    Feussner, I.6    Diederichsen, U.7
  • 23
    • 0037620493 scopus 로고    scopus 로고
    • Theoretical calculations of carbon-oxygen bond dissociation enthalpies of peroxyl radicals formed in the autoxidation of lipids
    • D.A. Pratt, J.H. Mills, and N.A. Porter Theoretical calculations of carbon-oxygen bond dissociation enthalpies of peroxyl radicals formed in the autoxidation of lipids J. Am. Chem. Soc. 125 2003 5801 5810
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5801-5810
    • Pratt, D.A.1    Mills, J.H.2    Porter, N.A.3
  • 24
    • 78651229995 scopus 로고    scopus 로고
    • Manganese lipoxygenase oxidizes bis-allylic hydroperoxides and octadecenoic acids by different mechanisms
    • E.H. Oliw, F. Jernerén, I. Hoffmann, M. Sahlin, and U. Garscha Manganese lipoxygenase oxidizes bis-allylic hydroperoxides and octadecenoic acids by different mechanisms Biochim. Biophys. Acta 1811 2011 138 147
    • (2011) Biochim. Biophys. Acta , vol.1811 , pp. 138-147
    • Oliw, E.H.1    Jernerén, F.2    Hoffmann, I.3    Sahlin, M.4    Garscha, U.5
  • 25
    • 80054112003 scopus 로고    scopus 로고
    • Stereoselective oxidation of regioisomeric octadecenoic acids by fatty acid dioxygenases
    • E.H. Oliw, A. Wennman, I. Hoffmann, U. Garscha, M. Hamberg, and F. Jernerén Stereoselective oxidation of regioisomeric octadecenoic acids by fatty acid dioxygenases J. Lipid Res. 52 2011 1995 2004
    • (2011) J. Lipid Res. , vol.52 , pp. 1995-2004
    • Oliw, E.H.1    Wennman, A.2    Hoffmann, I.3    Garscha, U.4    Hamberg, M.5    Jernerén, F.6
  • 26
    • 79952311370 scopus 로고    scopus 로고
    • Stereochemistry of hydrogen removal during oxygenation of linoleic acid by singlet oxygen and synthesis of 11(S)-deuterium-labeled linoleic acid
    • M. Hamberg Stereochemistry of hydrogen removal during oxygenation of linoleic acid by singlet oxygen and synthesis of 11(S)-deuterium-labeled linoleic acid Lipids 46 2011 201 206
    • (2011) Lipids , vol.46 , pp. 201-206
    • Hamberg, M.1
  • 27
    • 0039619742 scopus 로고    scopus 로고
    • Oxygenation of 5,8,11-eicosatrienoic acid by prostaglandin H synthase-2 of ovine placental cotyledons: Isolation of 13-hydroxy-5,8,11- eicosatrienoic and 11-hydroxy-5,8,12-eicosatrienoic acids
    • E.H. Oliw, L. Hörnsten, and H. Sprecher Oxygenation of 5,8,11-eicosatrienoic acid by prostaglandin H synthase-2 of ovine placental cotyledons: isolation of 13-hydroxy-5,8,11- eicosatrienoic and 11-hydroxy-5,8,12-eicosatrienoic acids J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 690 1997 332 337
    • (1997) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.690 , pp. 332-337
    • Oliw, E.H.1    Hörnsten, L.2    Sprecher, H.3
  • 28
    • 0042334839 scopus 로고    scopus 로고
    • 3 promoted coupling reactions for the preparation of skipped diynes
    • 3 promoted coupling reactions for the preparation of skipped diynes Tetrahedron 59 2003 7787 7790
    • (2003) Tetrahedron , vol.59 , pp. 7787-7790
    • Caruso, T.1    Spinella, A.2
  • 29
    • 33947086247 scopus 로고
    • Catalytic-hydrogenation. 6. Reaction of sodium-borohydride with nickel salts in ethanol solution - P-2 nickel, a highly convenient, new, selective hydrogenation catalyst with great sensitivity to substrate structure
    • C.A. Brown, and V.K. Ahuja Catalytic-hydrogenation. 6. Reaction of sodium-borohydride with nickel salts in ethanol solution - P-2 nickel, a highly convenient, new, selective hydrogenation catalyst with great sensitivity to substrate structure J. Org. Chem. 38 1973 2226 2230
    • (1973) J. Org. Chem. , vol.38 , pp. 2226-2230
    • Brown, C.A.1    Ahuja, V.K.2
  • 30
    • 2042524507 scopus 로고
    • Useful procedures for the oxidation of alcohols involving pyridinium dichromate in aprotic media
    • E.J. Corey, and G. Schmidt Useful procedures for the oxidation of alcohols involving pyridinium dichromate in aprotic media Tetrahedron Lett. 1979 399 402
    • (1979) Tetrahedron Lett. , pp. 399-402
    • Corey, E.J.1    Schmidt, G.2
  • 31
    • 0032518173 scopus 로고    scopus 로고
    • Stereochemistry of oxygenation of linoleic acid catalyzed by prostaglandin-endoperoxide H synthase-2
    • M. Hamberg Stereochemistry of oxygenation of linoleic acid catalyzed by prostaglandin-endoperoxide H synthase-2 Arch. Biochem. Biophys. 349 1998 376 380
    • (1998) Arch. Biochem. Biophys. , vol.349 , pp. 376-380
    • Hamberg, M.1
  • 32
    • 0015135670 scopus 로고
    • Steric analysis of hydroperoxides formed by lipoxygenase oxygenation of linoleic acid
    • M. Hamberg Steric analysis of hydroperoxides formed by lipoxygenase oxygenation of linoleic acid Anal. Biochem. 43 1971 515 526
    • (1971) Anal. Biochem. , vol.43 , pp. 515-526
    • Hamberg, M.1
  • 33
    • 0035813182 scopus 로고    scopus 로고
    • Structure of eicosapentaenoic and linoleic acids in the cyclooxygenase site of prostaglandin endoperoxide H synthase-1
    • M.G. Malkowski, E.D. Thuresson, K.M. Lakkides, C.J. Rieke, R. Micielli, W.L. Smith, and R.M. Garavito Structure of eicosapentaenoic and linoleic acids in the cyclooxygenase site of prostaglandin endoperoxide H synthase-1 J. Biol. Chem. 276 2001 37547 37555
    • (2001) J. Biol. Chem. , vol.276 , pp. 37547-37555
    • Malkowski, M.G.1    Thuresson, E.D.2    Lakkides, K.M.3    Rieke, C.J.4    Micielli, R.5    Smith, W.L.6    Garavito, R.M.7
  • 34
    • 0019330094 scopus 로고
    • Stereochemistry in the formation of 9-hydroxy-10,12-octadecadienoic acid and 13-hydroxy-9,11-octadecadienoic acid from linoleic acid by fatty acid cyclooxygenase
    • M. Hamberg, and B. Samuelsson Stereochemistry in the formation of 9-hydroxy-10,12-octadecadienoic acid and 13-hydroxy-9,11-octadecadienoic acid from linoleic acid by fatty acid cyclooxygenase Biochim. Biophys. Acta 617 1980 545 547
    • (1980) Biochim. Biophys. Acta , vol.617 , pp. 545-547
    • Hamberg, M.1    Samuelsson, B.2
  • 36
    • 0023661062 scopus 로고
    • Oxygenation of trans polyunsaturated fatty acids by lipoxygenase reveals steric features of the catalytic mechanism
    • M.O. Funk Jr., J.C. Andre, and T. Otsuki Oxygenation of trans polyunsaturated fatty acids by lipoxygenase reveals steric features of the catalytic mechanism Biochemistry 26 1987 6880 6884
    • (1987) Biochemistry , vol.26 , pp. 6880-6884
    • Funk Jr., M.O.1    Andre, J.C.2    Otsuki, T.3
  • 37
    • 35148843206 scopus 로고    scopus 로고
    • Free radical functionalization of organic compounds catalyzed by N-hydroxyphthalimide
    • F. Recupero, and C. Punta Free radical functionalization of organic compounds catalyzed by N-hydroxyphthalimide Chem. Rev. 107 2007 3800 3842
    • (2007) Chem. Rev. , vol.107 , pp. 3800-3842
    • Recupero, F.1    Punta, C.2
  • 38
    • 33244490501 scopus 로고    scopus 로고
    • Additivity rule holds in the hydrogen transfer reactivity of unsaturated fatty acids with a peroxyl radical: Mechanistic insight into lipoxygenase
    • H. Kitaguchi, K. Ohkubo, S. Ogo, and S. Fukuzumi Additivity rule holds in the hydrogen transfer reactivity of unsaturated fatty acids with a peroxyl radical: mechanistic insight into lipoxygenase Chem. Commun. (Camb) 2006 979 981
    • (2006) Chem. Commun. (Camb) , pp. 979-981
    • Kitaguchi, H.1    Ohkubo, K.2    Ogo, S.3    Fukuzumi, S.4
  • 39
    • 0021947113 scopus 로고
    • Synthesis of dihomoprostaglandins from adrenic acid (7,10,13,16- docosatetraenoic acid) by human endothelial cells
    • W.B. Campbell, J.R. Falck, J.R. Okita, A.R. Johnson, and K.S. Callahan Synthesis of dihomoprostaglandins from adrenic acid (7,10,13,16-docosatetraenoic acid) by human endothelial cells Biochim. Biophys. Acta 837 1985 67 76
    • (1985) Biochim. Biophys. Acta , vol.837 , pp. 67-76
    • Campbell, W.B.1    Falck, J.R.2    Okita, J.R.3    Johnson, A.R.4    Callahan, K.S.5
  • 41
    • 0024562115 scopus 로고
    • Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-hydroperoxides from linoleic acid by a pH-dependent mechanism
    • H.W. Gardner Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-hydroperoxides from linoleic acid by a pH-dependent mechanism Biochim. Biophys. Acta 1001 1989 274 281
    • (1989) Biochim. Biophys. Acta , vol.1001 , pp. 274-281
    • Gardner, H.W.1
  • 42
    • 84857036013 scopus 로고    scopus 로고
    • Applications of stereospecifically-labeled fatty acids in oxygenase and desaturase biochemistry
    • A.R. Brash, C. Schneider, and M. Hamberg Applications of stereospecifically-labeled fatty acids in oxygenase and desaturase biochemistry Lipids 47 2012 101 116
    • (2012) Lipids , vol.47 , pp. 101-116
    • Brash, A.R.1    Schneider, C.2    Hamberg, M.3
  • 43
    • 0027962756 scopus 로고
    • Unusually large deuterium-isotope effect in soybean lipoxygenase is not caused by a magnetic isotope effect
    • C.C. Hwang, and C.B. Grissom Unusually large deuterium-isotope effect in soybean lipoxygenase is not caused by a magnetic isotope effect J. Am. Chem. Soc. 116 1994 795 796
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 795-796
    • Hwang, C.C.1    Grissom, C.B.2
  • 44
    • 0024384199 scopus 로고
    • Pulse radiolytic measurement of redox potentials - The tyrosine and tryptophan radicals
    • M.R. Defelippis, C.P. Murthy, M. Faraggi, and M.H. Klapper Pulse radiolytic measurement of redox potentials - the tyrosine and tryptophan radicals Biochemistry 28 1989 4847 4853
    • (1989) Biochemistry , vol.28 , pp. 4847-4853
    • Defelippis, M.R.1    Murthy, C.P.2    Faraggi, M.3    Klapper, M.H.4
  • 45
    • 0001185064 scopus 로고
    • Catecholate complexes of ferric soybean lipoxygenase 1
    • M.J. Nelson Catecholate complexes of ferric soybean lipoxygenase 1 Biochemistry 27 1988 4273 4278
    • (1988) Biochemistry , vol.27 , pp. 4273-4278
    • Nelson, M.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.