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Volumn 68-69, Issue , 2002, Pages 313-323

Plant and fungal lipoxygenases

Author keywords

Electron paramagnetic resonance; Hydroperoxide; Lipoxygenation

Indexed keywords

APOENZYME; HYDROXIDE; IRON; LIGAND; LINOLEIC ACID; LIPOXYGENASE; MANGANESE;

EID: 0036669668     PISSN: 00906980     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0090-6980(02)00037-0     Document Type: Article
Times cited : (81)

References (61)
  • 1
    • 0033588022 scopus 로고    scopus 로고
    • Lipoxygenases: Occurrence, functions, catalysis, and acquisition of substrate
    • Brash A.R. Lipoxygenases: occurrence, functions, catalysis, and acquisition of substrate. J. Biol. Chem. 274:1999;23679.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23679
    • Brash, A.R.1
  • 2
    • 0000023568 scopus 로고
    • Biological roles and biochemistry of the lipoxygenase pathway
    • Gardner H.W. Biological roles and biochemistry of the lipoxygenase pathway. HortScience. 30:1995;197.
    • (1995) HortScience , vol.30 , pp. 197
    • Gardner, H.W.1
  • 5
    • 0030930205 scopus 로고    scopus 로고
    • Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme
    • Skrzypczak-Jankun E., Amzel L.M., Kroa B.A., Funk M.O. Jr. Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme. Proteins. 29:1997;15.
    • (1997) Proteins , vol.29 , pp. 15
    • Skrzypczak-Jankun, E.1    Amzel, L.M.2    Kroa, B.A.3    Funk M.O., Jr.4
  • 6
    • 0030736867 scopus 로고    scopus 로고
    • The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity
    • Gillmor S.A., Villaseñor 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. 4:1997;1003.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 1003
    • Gillmor, S.A.1    Villaseñor, A.2    Fletterick, R.3    Sigal, E.4    Browner, M.F.5
  • 7
    • 0035081930 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of a lipoxygenase in almond (Prunus dulcis) seed
    • Mita G., Gallo A., Greco V., Zasiura C., Casey R., Zacheo G.et al. Molecular cloning and biochemical characterization of a lipoxygenase in almond (Prunus dulcis) seed. Eur. J. Biochem. 268:2001;1500.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1500
    • Mita, G.1    Gallo, A.2    Greco, V.3    Zasiura, C.4    Casey, R.5    Zacheo, G.6
  • 8
    • 0029809331 scopus 로고    scopus 로고
    • Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns
    • Royo J., Vancanneyt G., Pérez A.G., Sanz C., Störmann K., Rosahl S.et al. Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns. J. Biol. Chem. 271:1996;21012.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21012
    • Royo, J.1    Vancanneyt, G.2    Pérez, A.G.3    Sanz, C.4    Störmann, K.5    Rosahl, S.6
  • 9
    • 0032126176 scopus 로고    scopus 로고
    • Characterization of authentic recombinant pea-seed lipoxygenases with distinct properties and reaction mechanisms
    • Hughes R.K., Wu Z., Robinson D.S., Hardy D., West S.I., Fairhurst S.A.et al. Characterization of authentic recombinant pea-seed lipoxygenases with distinct properties and reaction mechanisms. Biochem. J. 333:1998;33.
    • (1998) Biochem. J. , vol.333 , pp. 33
    • Hughes, R.K.1    Wu, Z.2    Robinson, D.S.3    Hardy, D.4    West, S.I.5    Fairhurst, S.A.6
  • 13
    • 0035864373 scopus 로고    scopus 로고
    • Site-directed mutagenesis studies on a putative fifth iron ligand of mouse 8S-lipoxygenase: Retention of catalytic activity on mutation of serine-558 to asparagine, histidine, or alanine
    • Jisaka M., Boeglin W.E., Kim R.B., Brash A.R. Site-directed mutagenesis studies on a putative fifth iron ligand of mouse 8S-lipoxygenase: retention of catalytic activity on mutation of serine-558 to asparagine, histidine, or alanine. Arch. Biochem. Biophys. 386:2001;136.
    • (2001) Arch. Biochem. Biophys. , vol.386 , pp. 136
    • Jisaka, M.1    Boeglin, W.E.2    Kim, R.B.3    Brash, A.R.4
  • 14
    • 0029864977 scopus 로고    scopus 로고
    • Structure conservation in lipoxygenases: Structural analysis of soybean lipoxygenase-1 and modeling of human lipoxygenases
    • Prigge S.T., Boyington J.C., Gaffney B.J., Amzel L.M. Structure conservation in lipoxygenases: structural analysis of soybean lipoxygenase-1 and modeling of human lipoxygenases. Proteins. 24:1996;275.
    • (1996) Proteins , vol.24 , pp. 275
    • Prigge, S.T.1    Boyington, J.C.2    Gaffney, B.J.3    Amzel, L.M.4
  • 15
    • 0031392653 scopus 로고    scopus 로고
    • A model of arachidonic acid binding for 15-lipoxygenase
    • Gan Q.F., Sigal E., Browner M.F. A model of arachidonic acid binding for 15-lipoxygenase. Adv. Exp. Med. Biol. 433:1997;435.
    • (1997) Adv. Exp. Med. Biol. , vol.433 , pp. 435
    • Gan, Q.F.1    Sigal, E.2    Browner, M.F.3
  • 16
    • 0033837450 scopus 로고    scopus 로고
    • Structural basis for the positional specificity of lipoxygenases
    • Kuhn H. Structural basis for the positional specificity of lipoxygenases. Prostaglandins Other Lipid Mediat. 62:2000;255.
    • (2000) Prostaglandins Other Lipid Mediat. , vol.62 , pp. 255
    • Kuhn, H.1
  • 17
    • 0033616797 scopus 로고    scopus 로고
    • Conversion of cucumber linoleate 13-lipoxygenase to a 9-lipoxygenating species by site-directed mutagenesis
    • Hornung E., Walther M., Kühn H., Feussner I. Conversion of cucumber linoleate 13-lipoxygenase to a 9-lipoxygenating species by site-directed mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 96:1999;4192.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4192
    • Hornung, E.1    Walther, M.2    Kühn, H.3    Feussner, I.4
  • 18
    • 0035964334 scopus 로고    scopus 로고
    • Soybean lipoxygenase-1 oxygenates synthetic polyenoic fatty acids with an altered positional specificity. Evidence for inverse substrate alignment
    • Ivanov I., Rathmann J., Myagkova G., Kuhn H. Soybean lipoxygenase-1 oxygenates synthetic polyenoic fatty acids with an altered positional specificity. Evidence for inverse substrate alignment. Biochemistry. 40:2001;10223.
    • (2001) Biochemistry , vol.40 , pp. 10223
    • Ivanov, I.1    Rathmann, J.2    Myagkova, G.3    Kuhn, H.4
  • 19
    • 0035808468 scopus 로고    scopus 로고
    • Structural basis for lipoxygenase specificity. Conversion of the human leukocyte 5-lipoxygenase to a 15-lipoxygenating enzyme species by site-directed mutagenesis
    • 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. 276:2001;773.
    • (2001) J. Biol. Chem. , vol.276 , pp. 773
    • Schwarz, K.1    Walther, M.2    Anton, M.3    Gerth, C.4    Feussner, I.5    Kuhn, H.6
  • 20
    • 0035863234 scopus 로고    scopus 로고
    • Probing a novel potato lipoxygenase with dual positional specificity reveals primary determinants of substrate binding and requirements for a surface hydrophobic loop and has implications for the role of lipoxygenases in tubers
    • Hughes R.K., West S.I., Hornostaj A.R., Lawson D.M., Fairhurst S.A., Sanchez R.O.et al. Probing a novel potato lipoxygenase with dual positional specificity reveals primary determinants of substrate binding and requirements for a surface hydrophobic loop and has implications for the role of lipoxygenases in tubers. Biochem. J. 353:2001;345.
    • (2001) Biochem. J. , vol.353 , pp. 345
    • Hughes, R.K.1    West, S.I.2    Hornostaj, A.R.3    Lawson, D.M.4    Fairhurst, S.A.5    Sanchez, R.O.6
  • 21
    • 0035095841 scopus 로고    scopus 로고
    • Enzymes of the biosynthesis of octadecanoid-derived signalling molecules
    • Schaller F. Enzymes of the biosynthesis of octadecanoid-derived signalling molecules. J. Exp. Bot. 52:2001;11.
    • (2001) J. Exp. Bot. , vol.52 , pp. 11
    • Schaller, F.1
  • 22
    • 0031574232 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad - An emerging structural motif in mononuclear non-heme iron(II) enzymes
    • Hegg E.L., Que L. Jr. The 2-His-1-carboxylate facial triad - an emerging structural motif in mononuclear non-heme iron(II) enzymes. Eur. J. Biochem. 250:1997;625.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 625
    • Hegg, E.L.1    Que L., Jr.2
  • 23
    • 0035954384 scopus 로고    scopus 로고
    • Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1
    • 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. 40:2001;7509.
    • (2001) Biochemistry , vol.40 , pp. 7509
    • Tomchick, D.R.1    Phan, P.2    Cymborowski, M.3    Minor, W.4    Holman, T.R.5
  • 24
    • 0028639234 scopus 로고
    • X-ray spectroscopy of the iron site in soybean lipoxygenase-1: Changes in coordination upon oxidation or addition of methanol
    • Scarrow R.C., Trimitsis M.G., Buck C.P., Grove G.N., Cowling R.A., Nelson M.J. X-ray spectroscopy of the iron site in soybean lipoxygenase-1: changes in coordination upon oxidation or addition of methanol. Biochemistry. 33:1994;15023.
    • (1994) Biochemistry , vol.33 , pp. 15023
    • Scarrow, R.C.1    Trimitsis, M.G.2    Buck, C.P.3    Grove, G.N.4    Cowling, R.A.5    Nelson, M.J.6
  • 25
    • 0029843150 scopus 로고    scopus 로고
    • Lipoxygenase reaction mechanism: Demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover
    • Glickman M.H., Klinman J.P. Lipoxygenase reaction mechanism: demonstration that hydrogen abstraction from substrate precedes dioxygen binding during catalytic turnover. Biochemistry. 35:1996;12882.
    • (1996) Biochemistry , vol.35 , pp. 12882
    • Glickman, M.H.1    Klinman, J.P.2
  • 26
    • 0033592315 scopus 로고    scopus 로고
    • Nature of hydrogen transfer in soybean lipoxygenase 1: Separation of primary and secondary isotope effects
    • Rickert K.W., Klinman J.P. Nature of hydrogen transfer in soybean lipoxygenase 1: separation of primary and secondary isotope effects. Biochemistry. 38:1999;12218.
    • (1999) Biochemistry , vol.38 , pp. 12218
    • Rickert, K.W.1    Klinman, J.P.2
  • 27
    • 0030920947 scopus 로고    scopus 로고
    • Reduction of ferric iron could drive hydrogen tunneling in lipoxygenase catalysis: Implications for enzymatic and chemical mechanisms
    • Moiseyev N., Rucker J., Glickman M.H. Reduction of ferric iron could drive hydrogen tunneling in lipoxygenase catalysis: implications for enzymatic and chemical mechanisms. J. Am. Chem. Soc. 119:1997;3853.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3853
    • Moiseyev, N.1    Rucker, J.2    Glickman, M.H.3
  • 28
    • 0033576983 scopus 로고    scopus 로고
    • Large competitive kinetic isotope effects in human 15-lipoxygenase catalysis measured by a novel HPLC method
    • Lewis R.E., Johansen E., Holman T.R. Large competitive kinetic isotope effects in human 15-lipoxygenase catalysis measured by a novel HPLC method. J. Am. Chem. Soc. 121:1999;1395.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1395
    • Lewis, R.E.1    Johansen, E.2    Holman, T.R.3
  • 30
    • 0034646193 scopus 로고    scopus 로고
    • The action of soybean lipoxygenase-1 on 12-iodo-cis-9-octadecenoic acid: The importance of C11-H bond breaking
    • Clapp C.H., McKown J., Xu H., Grandizio A.M., Yang G., Fayer J. The action of soybean lipoxygenase-1 on 12-iodo-cis-9-octadecenoic acid: the importance of C11-H bond breaking. Biochemistry. 39:2000;2603.
    • (2000) Biochemistry , vol.39 , pp. 2603
    • Clapp, C.H.1    McKown, J.2    Xu, H.3    Grandizio, A.M.4    Yang, G.5    Fayer, J.6
  • 31
    • 0034811728 scopus 로고    scopus 로고
    • Steric control of oxygenation regiochemistry in soybean lipoxygenase-1
    • Knapp M.J., Seebeck F.P., Klinman J.P. Steric control of oxygenation regiochemistry in soybean lipoxygenase-1. J. Am. Chem. Soc. 123:2001;2931.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2931
    • Knapp, M.J.1    Seebeck, F.P.2    Klinman, J.P.3
  • 32
    • 0028306325 scopus 로고
    • Structural characterization of alkyl and peroxyl radicals in solutions of purple lipoxygenase
    • Nelson M.J., Cowling R.A., Seitz S.P. Structural characterization of alkyl and peroxyl radicals in solutions of purple lipoxygenase. Biochemistry. 33:1994;4966.
    • (1994) Biochemistry , vol.33 , pp. 4966
    • Nelson, M.J.1    Cowling, R.A.2    Seitz, S.P.3
  • 33
    • 0034805399 scopus 로고    scopus 로고
    • Iron extraction from soybean lipoxygenase 3 and reconstitution of catalytic activity from the apoenzyme
    • Kariapper M.S., Dunham W.R., Funk M.O. Jr. Iron extraction from soybean lipoxygenase 3 and reconstitution of catalytic activity from the apoenzyme. Biochem. Biophys. Res. Commun. 284:2001;563.
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 563
    • Kariapper, M.S.1    Dunham, W.R.2    Funk M.O., Jr.3
  • 34
    • 0026801413 scopus 로고
    • Limited proteolysis and active-site labeling studies of soybean lipoxygenase L
    • Ramachandran S., Carroll R.T., Dunham W.R., Funk M.O. Jr. Limited proteolysis and active-site labeling studies of soybean lipoxygenase L. Biochemistry. 31:1992;7700.
    • (1992) Biochemistry , vol.31 , pp. 7700
    • Ramachandran, S.1    Carroll, R.T.2    Dunham, W.R.3    Funk M.O., Jr.4
  • 35
    • 0035849587 scopus 로고    scopus 로고
    • Tryptic digestion of soybean lipoxygenase-1 generates a 60 kDa fragment with improved activity and membrane binding ability
    • Maccarrone M., Salucci M.L., van Zadelhoff G., Malatesta F., Veldink G., Vliegenthart J.F.G.et al. Tryptic digestion of soybean lipoxygenase-1 generates a 60 kDa fragment with improved activity and membrane binding ability. Biochemistry. 40:2001;6819.
    • (2001) Biochemistry , vol.40 , pp. 6819
    • Maccarrone, M.1    Salucci, M.L.2    Van Zadelhoff, G.3    Malatesta, F.4    Veldink, G.5    Vliegenthart, J.F.G.6
  • 36
    • 48549111085 scopus 로고
    • Origin of the oxygen in the products of the enzymatic cleavage reaction of linoleic acid to 1-octen-3-ol and 10-oxo-trans-8-decenoic acid in mushrooms (Psalliota bispora)
    • Wurzenberger M., Grosch W. Origin of the oxygen in the products of the enzymatic cleavage reaction of linoleic acid to 1-octen-3-ol and 10-oxo-trans-8-decenoic acid in mushrooms (Psalliota bispora). Biochim. Biophys. Acta. 794:1984;18.
    • (1984) Biochim. Biophys. Acta , vol.794 , pp. 18
    • Wurzenberger, M.1    Grosch, W.2
  • 37
    • 48749134865 scopus 로고
    • The formation of 1-octen-3-ol from the 10-hydroperoxide isomer of linoleic acid by a hydroperoxide lyase in mushrooms (Psalliota bispora)
    • Wurzenberger M., Grosch W. The formation of 1-octen-3-ol from the 10-hydroperoxide isomer of linoleic acid by a hydroperoxide lyase in mushrooms (Psalliota bispora). Biochim. Biophys. Acta. 794:1984;25.
    • (1984) Biochim. Biophys. Acta , vol.794 , pp. 25
    • Wurzenberger, M.1    Grosch, W.2
  • 38
    • 0028049915 scopus 로고
    • A novel lipoxygenase from rice. Primary structure and specific expression upon incompatible infection with rice blast fungus
    • Peng Y.L., Shirano Y., Ohta H., Hibino T., Tanaka K., Shibata D. A novel lipoxygenase from rice. Primary structure and specific expression upon incompatible infection with rice blast fungus. J. Biol. Chem. 269:1994;3755.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3755
    • Peng, Y.L.1    Shirano, Y.2    Ohta, H.3    Hibino, T.4    Tanaka, K.5    Shibata, D.6
  • 39
    • 0029838864 scopus 로고    scopus 로고
    • Specificity of two lipoxygenases from rice: Unusual regiospecificity of a lipoxygenase isoenzyme
    • Zhang L.Y., Hamberg M. Specificity of two lipoxygenases from rice: unusual regiospecificity of a lipoxygenase isoenzyme. Lipids. 31:1996;803.
    • (1996) Lipids , vol.31 , pp. 803
    • Zhang, L.Y.1    Hamberg, M.2
  • 41
    • 0032568536 scopus 로고    scopus 로고
    • The incompatible interaction between Phytophthora parasitica var. nicotianae race 0 and tobacco is suppressed in transgenic plants expressing antisense lipoxygenase sequences
    • Rancé I.I., Fournier J., Esquerré-Tugayé M.T. The incompatible interaction between Phytophthora parasitica var. nicotianae race 0 and tobacco is suppressed in transgenic plants expressing antisense lipoxygenase sequences. Proc. Natl. Acad. Sci. U.S.A. 95:1998;6554.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6554
    • Rancé, I.I.1    Fournier, J.2    Esquerré-Tugayé, M.T.3
  • 42
    • 0033514476 scopus 로고    scopus 로고
    • Antisense-mediated depletion of a potato lipoxygenase reduces wound induction of proteinase inhibitors and increases weight gain of insect pests
    • Royo J., León J., Vancanneyt G., Albar J.P., Rosahl S., Ortego F.et al. Antisense-mediated depletion of a potato lipoxygenase reduces wound induction of proteinase inhibitors and increases weight gain of insect pests. Proc. Natl. Acad. Sci. U.S.A. 96:1999;1146.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1146
    • Royo, J.1    León, J.2    Vancanneyt, G.3    Albar, J.P.4    Rosahl, S.5    Ortego, F.6
  • 44
    • 0035794189 scopus 로고    scopus 로고
    • Oxylipin profiling reveals the preferential stimulation of the 9-lipoxygenase pathway in elicitor-treated potato cells
    • Göbel C., Feussner I., Schmidt A., Scheel D., Sanchez-Serrano J., Hamberg M.et al. Oxylipin profiling reveals the preferential stimulation of the 9-lipoxygenase pathway in elicitor-treated potato cells. J. Biol. Chem. 276:2001;6267.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6267
    • Göbel, C.1    Feussner, I.2    Schmidt, A.3    Scheel, D.4    Sanchez-Serrano, J.5    Hamberg, M.6
  • 45
    • 0039132786 scopus 로고    scopus 로고
    • Involvement of lipoxygenase-dependent production of fatty acid hydroperoxides in the development of the hypersensitive cell death induced by cryptogein on tobacco leaves
    • Rustérucci C., Montillet J.L., Agnel J.P., Battesti C., Alonso B., Knoll A.et al. Involvement of lipoxygenase-dependent production of fatty acid hydroperoxides in the development of the hypersensitive cell death induced by cryptogein on tobacco leaves. J. Biol. Chem. 274:1999;36446.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36446
    • Rustérucci, C.1    Montillet, J.L.2    Agnel, J.P.3    Battesti, C.4    Alonso, B.5    Knoll, A.6
  • 47
    • 0039850192 scopus 로고    scopus 로고
    • Cloning of linoleate diol synthase reveals homology with prostaglandin H synthases
    • Hörnsten L., Su C., Osbourn A.E., Garosi P., Hellman U., Wernstedt C.et al. Cloning of linoleate diol synthase reveals homology with prostaglandin H synthases. J. Biol. Chem. 274:1999;28219.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28219
    • Hörnsten, L.1    Su, C.2    Osbourn, A.E.3    Garosi, P.4    Hellman, U.5    Wernstedt, C.6
  • 48
    • 0002133585 scopus 로고    scopus 로고
    • Oxylipin production and action in fungi and related organisms
    • Rowley AF, Kühn K, Schwebe T, editors. London: Portland Press
    • Herman RP. Oxylipin production and action in fungi and related organisms. In: Rowley AF, Kühn K, Schwebe T, editors. Eicosanoids and Related Compounds in Plants and Animals. London: Portland Press, 1998. p. 117.
    • (1998) Eicosanoids and Related Compounds in Plants and Animals , pp. 117
    • Herman, R.P.1
  • 50
    • 0023371513 scopus 로고
    • Properties of the soluble arachidonic acid 15-lipoxygenase and 15-hydroperoxide isomerase from the oomycete Saprolegnia parasitica
    • Herman R.P., Hamberg M. Properties of the soluble arachidonic acid 15-lipoxygenase and 15-hydroperoxide isomerase from the oomycete Saprolegnia parasitica. Prostaglandins. 34:1987;129.
    • (1987) Prostaglandins , vol.34 , pp. 129
    • Herman, R.P.1    Hamberg, M.2
  • 52
    • 0030061401 scopus 로고    scopus 로고
    • Lipoperoxidase activity of Pityrosporum: Characterisation of by-products and possible role in pityriasis versicolor
    • De Luca C., Picardo M., Breathnach A., Passi S. Lipoperoxidase activity of Pityrosporum: characterisation of by-products and possible role in pityriasis versicolor. Exp. Dermatol. 5:1996;49.
    • (1996) Exp. Dermatol. , vol.5 , pp. 49
    • De Luca, C.1    Picardo, M.2    Breathnach, A.3    Passi, S.4
  • 53
    • 0032557426 scopus 로고    scopus 로고
    • Manganese lipoxygenase. Purification and characterization
    • Su C., Oliw E.H. Manganese lipoxygenase. Purification and characterization. J. Biol. Chem. 273:1998;13072.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13072
    • Su, C.1    Oliw, E.H.2
  • 54
    • 0034705603 scopus 로고    scopus 로고
    • Kinetics of manganese lipoxygenase with a catalytic mononuclear redox center
    • Su C., Sahlin M., Oliw E.H. Kinetics of manganese lipoxygenase with a catalytic mononuclear redox center. J. Biol. Chem. 275:2000;18830.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18830
    • Su, C.1    Sahlin, M.2    Oliw, E.H.3
  • 55
    • 0032557580 scopus 로고    scopus 로고
    • Man, manganese lipoxygenase. Discovery of a bis-allylic hydroperoxide as product and intermediate in a lipoxygenase reaction
    • Hamberg M., Su C., Oliw E.H. Man, manganese lipoxygenase. Discovery of a bis-allylic hydroperoxide as product and intermediate in a lipoxygenase reaction. J. Biol. Chem. 273:1998;13080.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13080
    • Hamberg, M.1    Su, C.2    Oliw, E.H.3
  • 56
    • 0036276402 scopus 로고    scopus 로고
    • Cloning and characterization of the manganese lipoxygenase gene and homology with the lipoxygenase gene family
    • Hörnsten L, Su C, Osbourn AE, Hellman U, Oliw EH. Cloning and characterization of the manganese lipoxygenase gene and homology with the lipoxygenase gene family. Eur J Biochem 2002;269:2690.
    • (2002) Eur J Biochem , vol.269 , pp. 2690
    • Hörnsten, L.1    Su, C.2    Osbourn, A.E.3    Hellman, U.4    Oliw, E.H.5
  • 57
    • 0031473227 scopus 로고    scopus 로고
    • Structural chemistry and biology of manganese metalloenzymes
    • Christianson D.W. Structural chemistry and biology of manganese metalloenzymes. Prog. Biophys. Mol. Biol. 67:1997;217.
    • (1997) Prog. Biophys. Mol. Biol. , vol.67 , pp. 217
    • Christianson, D.W.1
  • 58
    • 0035528062 scopus 로고    scopus 로고
    • Assignment of EPR transitions in a manganese-containing lipoxygenase and prediction of local structure
    • Gaffney BJ, Su C, Oliw EH. Assignment of EPR transitions in a manganese-containing lipoxygenase and prediction of local structure. Appl Mag Reson 2001;21:411.
    • (2001) Appl Mag Reson , vol.21 , pp. 411
    • Gaffney, B.J.1    Su, C.2    Oliw, E.H.3
  • 60
    • 0001300916 scopus 로고
    • The mechanism of the rearrangement of linoleate hydroperoxides
    • Chan D.W.-S., Levett G., Matthew J.A. The mechanism of the rearrangement of linoleate hydroperoxides. Chem. Phys. Lipids. 24:1979;245.
    • (1979) Chem. Phys. Lipids , vol.24 , pp. 245
    • Chan, D.W.-S.1    Levett, G.2    Matthew, J.A.3
  • 61
    • 0024820007 scopus 로고
    • Lipid peroxyl radical intermediates in the peroxidation of polyunsaturated fatty acids by lipoxygenase. Direct electron spin resonance investigations
    • Chamulitrat W., Mason R.P. Lipid peroxyl radical intermediates in the peroxidation of polyunsaturated fatty acids by lipoxygenase. Direct electron spin resonance investigations. J. Biol. Chem. 264:1989;20968.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20968
    • Chamulitrat, W.1    Mason, R.P.2


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