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Volumn 62, Issue 3, 2000, Pages 255-270

Structural basis for the positional specificity of lipoxygenases

Author keywords

Atherosclerosis; Eicosanoids; Inflammation; Molecular enzymology; Structural biology

Indexed keywords

ARACHIDONATE 12 LIPOXYGENASE; ARACHIDONATE 15 LIPOXYGENASE; ARACHIDONIC ACID; LIPOXYGENASE;

EID: 0033837450     PISSN: 00906980     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0090-6980(00)00084-8     Document Type: Review
Times cited : (73)

References (59)
  • 1
  • 3
    • 0003040453 scopus 로고    scopus 로고
    • Mammalian lipoxygenases. Structure, function and evolutionary aspects
    • In: Rowley AF, Kühn H, Schewe T, editors. London: Portland Press
    • Ueda N, Suzuki H, Yamamoto S. Mammalian lipoxygenases. Structure, function and evolutionary aspects. In: Rowley AF, Kühn H, Schewe T, editors. Eicosanoids and related compounds in plants and animals. London: Portland Press, 1998. p. 47-68.
    • (1998) Eicosanoids and Related Compounds in Plants and Animals , pp. 47-68
    • Ueda, N.1    Suzuki, H.2    Yamamoto, S.3
  • 4
    • 0001443977 scopus 로고
    • Sur la presence d'une oxydase des lipides ou lipoxydase dans la graine de soja, Glycine soja Lieb
    • André E, Hou K. Sur la presence d'une oxydase des lipides ou lipoxydase dans la graine de soja, Glycine soja Lieb. Comptes. Rendus 1932;194:645.
    • (1932) Comptes. Rendus , vol.194 , pp. 645
    • André, E.1    Hou, K.2
  • 5
    • 0020014193 scopus 로고
    • The 5-lipoxygenase and leukotriene forming enzymes
    • Jakschik B.A., Harper T., Murphy R.C. The 5-lipoxygenase and leukotriene forming enzymes. Methods Enzymol. 86:1982;30.
    • (1982) Methods Enzymol , vol.86 , pp. 30
    • Jakschik, B.A.1    Harper, T.2    Murphy, R.C.3
  • 6
    • 0016780261 scopus 로고
    • A lipoxygenase in rabbit reticulocytes, which attacks biomembranes
    • Schewe T., Halangk W., Hiebsch C., Rapoport S.M. A lipoxygenase in rabbit reticulocytes, which attacks biomembranes. FEBS Lett. 60:1975;149.
    • (1975) FEBS Lett , vol.60 , pp. 149
    • Schewe, T.1    Halangk, W.2    Hiebsch, C.3    Rapoport, S.M.4
  • 7
    • 0025219139 scopus 로고
    • Expression of cloned human reticulocyte 15-lipoxygenase and immunological evidence that 15-lipoxygenases of different cell types are related
    • Sigal E., Grunberger D., Highland E., Gross C., Dixon R.A., Craik C.S. Expression of cloned human reticulocyte 15-lipoxygenase and immunological evidence that 15-lipoxygenases of different cell types are related. J Biol Chem. 265:1990;5113.
    • (1990) J Biol Chem , vol.265 , pp. 5113
    • Sigal, E.1    Grunberger, D.2    Highland, E.3    Gross, C.4    Dixon, R.A.5    Craik, C.S.6
  • 9
    • 0000822547 scopus 로고
    • Prostaglandin endoperoxides. Novel transformations of arachidonic acid in human platelets
    • Hamberg M., Samuelsson B. Prostaglandin endoperoxides. Novel transformations of arachidonic acid in human platelets. Proc Natl Acad Sci USA. 71:1974;3400.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 3400
    • Hamberg, M.1    Samuelsson, B.2
  • 10
    • 0032911057 scopus 로고    scopus 로고
    • The diversity of lipoxygenase family
    • Kuhn H., Thiele B.J. The diversity of lipoxygenase family. FEBS Lett. 449:1999;7.
    • (1999) FEBS Lett , vol.449 , pp. 7
    • Kuhn, H.1    Thiele, B.J.2
  • 11
    • 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
  • 12
    • 0033153412 scopus 로고    scopus 로고
    • CDNA cloning, genomic structure, and chromosomal localization of a novel murine epidermis-type lipoxygenase
    • Kinzig A., Heidt M., Fürstenberger G., Marks F., Krieg P. cDNA cloning, genomic structure, and chromosomal localization of a novel murine epidermis-type lipoxygenase. Genomics. 58:1999;158.
    • (1999) Genomics , vol.58 , pp. 158
    • Kinzig, A.1    Heidt, M.2    Fürstenberger, G.3    Marks, F.4    Krieg, P.5
  • 15
    • 0014217378 scopus 로고
    • On the specificity of the oxygenation of unsaturated fatty acids catalyzed by soybean lipoxidase
    • Hamberg M., Samuelsson B. On the specificity of the oxygenation of unsaturated fatty acids catalyzed by soybean lipoxidase. J Biol Chem. 242:1967;5329.
    • (1967) J Biol Chem , vol.242 , pp. 5329
    • Hamberg, M.1    Samuelsson, B.2
  • 16
    • 0025144594 scopus 로고
    • On singular or dual positional specificity of lipoxygenases. The number of chiral products varies with alignment of methylene groups at the active site of the enzyme
    • Kühn H., Sprecher H., Brash A.R. On singular or dual positional specificity of lipoxygenases. The number of chiral products varies with alignment of methylene groups at the active site of the enzyme. J Biol Chem. 265:1990;16300.
    • (1990) J Biol Chem , vol.265 , pp. 16300
    • Kühn, H.1    Sprecher, H.2    Brash, A.R.3
  • 17
    • 0024562115 scopus 로고
    • Soybean lipoxygenase-1 enzymically forms both (9S)- And (13S)-hydroperoxides from linoleic acid by a pH-dependent mechanism
    • Gardner H.W. Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-hydroperoxides from linoleic acid by a pH-dependent mechanism. Biochim Biophys Acta. 1001:1989;274.
    • (1989) Biochim Biophys Acta , vol.1001 , pp. 274
    • Gardner, H.W.1
  • 18
    • 0344500896 scopus 로고    scopus 로고
    • Change in the positional specificity of lipoxygenase 1 due to insertion of the fatty acids into phosphatidylcholine deoxycholate mixed micelles
    • Began G., Sudharshan E., Rao A.G.A. Change in the positional specificity of lipoxygenase 1 due to insertion of the fatty acids into phosphatidylcholine deoxycholate mixed micelles. Biochemistry. 38:1999;13920.
    • (1999) Biochemistry , vol.38 , pp. 13920
    • Began, G.1    Sudharshan, E.2    Rao, A.G.A.3
  • 19
    • 0345368074 scopus 로고    scopus 로고
    • Probing the substrate alignment at the active site of 15-lipoxygenases by targeted substrate modification and site directed mutagenesis. Evidence for an Inverse substrate orientation
    • Schwarz K., Borngräber S., Anton M., Kuhn H. Probing the substrate alignment at the active site of 15-lipoxygenases by targeted substrate modification and site directed mutagenesis. Evidence for an Inverse substrate orientation. Biochemistry. 37:1998;15327.
    • (1998) Biochemistry , vol.37 , pp. 15327
    • Schwarz, K.1    Borngräber, S.2    Anton, M.3    Kuhn, H.4
  • 20
    • 0028216578 scopus 로고
    • CDNA cloning, expression, mutagenesis of C-terminal isoleucine, genomic structure, and chromosomal localizations of murine 12-lipoxygenases
    • 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. 269:1994;13979.
    • (1994) J Biol Chem , vol.269 , pp. 13979
    • Chen, X.S.1    Kurre, U.2    Jenkins, N.A.3    Copeland, N.G.4    Funk, C.D.5
  • 22
    • 0342710359 scopus 로고    scopus 로고
    • Murine epidermal lipoxygenase (aloxe) encodes a 12-lipoxygenase isoform
    • Kinzig A., Fürstenberger G., Bürger F., et al. Murine epidermal lipoxygenase (aloxe) encodes a 12-lipoxygenase isoform. FEBS Lett. 402:1997;162.
    • (1997) FEBS Lett , vol.402 , pp. 162
    • Kinzig, A.1    Fürstenberger, G.2    Bürger, F.3
  • 23
    • 20644448592 scopus 로고    scopus 로고
    • Human 12(R)-lipoxygenase and the mouse ortholog
    • Sun D., McDonnell M., Chen X.S., et al. Human 12(R)-lipoxygenase and the mouse ortholog. J Biol Chem. 273:1998;33540.
    • (1998) J Biol Chem , vol.273 , pp. 33540
    • Sun, D.1    McDonnell, M.2    Chen, X.S.3
  • 24
    • 0032499790 scopus 로고    scopus 로고
    • A 12(R)-lipoxygenase in human skin: Mechanistic evidence, molecular cloning, and expression
    • Boeglin W.E., Kim R.B., Brash A.R. A 12(R)-lipoxygenase in human skin mechanistic evidence, molecular cloning, and expression . Proc Natl Acad Sci USA. 95:1998;6744.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6744
    • Boeglin, W.E.1    Kim, R.B.2    Brash, A.R.3
  • 26
    • 0030827131 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a phorbol ester-inducible 8S-lipoxygenase from mouse skin
    • Jisaka M., Kim R.B., Boeglin W.E., Nanney L.B., Brash A.R. Molecular cloning and functional expression of a phorbol ester-inducible 8S-lipoxygenase from mouse skin. J Biol Chem. 272:1997;24410.
    • (1997) J Biol Chem , vol.272 , pp. 24410
    • Jisaka, M.1    Kim, R.B.2    Boeglin, W.E.3    Nanney, L.B.4    Brash, A.R.5
  • 27
    • 0026565597 scopus 로고
    • Specific inflammatory cytokines regulate the expression of 15-lipoxygenase in human monocyte
    • Conrad D.J., Kühn H., Mulkins M., Highland E., Sigal E. Specific inflammatory cytokines regulate the expression of 15-lipoxygenase in human monocyte. Proc Natl Acad Sci USA. 89:1992;217.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 217
    • Conrad, D.J.1    Kühn, H.2    Mulkins, M.3    Highland, E.4    Sigal, E.5
  • 28
    • 0032189017 scopus 로고    scopus 로고
    • IL-4 and -13 induced upregulation of the murine macrophage 12/15-lipoxygenase activity: Evidence for the involvement of transcription factor STAT6
    • Heydeck D., Thomas L., Schnurr K., et al. IL-4 and -13 induced upregulation of the murine macrophage 12/15-lipoxygenase activity evidence for the involvement of transcription factor STAT6 . Blood. 92:1998;2503.
    • (1998) Blood , vol.92 , pp. 2503
    • Heydeck, D.1    Thomas, L.2    Schnurr, K.3
  • 30
    • 0024517459 scopus 로고
    • Mechanism of biosynthesis of 11R- And 12R-hydroxyeicosatetraenoic acids by eggs of the sea urchin Strongylocentrotus purpuratus
    • Hawkins D.J., Brash A.R. Mechanism of biosynthesis of 11R- and 12R-hydroxyeicosatetraenoic acids by eggs of the sea urchin Strongylocentrotus purpuratus. FEBS Lett. 247:1989;9.
    • (1989) FEBS Lett , vol.247 , pp. 9
    • Hawkins, D.J.1    Brash, A.R.2
  • 31
    • 0029808212 scopus 로고    scopus 로고
    • Purification, and molecular cloning of an 8R-lipoxygenase from the coral Plexaura homomalla reveal the related primary structures of R- And S-lipoxygenases
    • Brash A.R., Boeglin W.E., Chang M.S., Shieh B.H. Purification, and molecular cloning of an 8R-lipoxygenase from the coral Plexaura homomalla reveal the related primary structures of R- and S-lipoxygenases. J Biol Chem. 271:1996;20949.
    • (1996) J Biol Chem , vol.271 , pp. 20949
    • Brash, A.R.1    Boeglin, W.E.2    Chang, M.S.3    Shieh, B.H.4
  • 32
    • 0031548849 scopus 로고    scopus 로고
    • Discovery of 5R-lipoxygenase activity in oocytes of the surf clam, Spisula solidissima
    • Hada T., Swift L.L., Brash A.R. Discovery of 5R-lipoxygenase activity in oocytes of the surf clam, Spisula solidissima. Biochim Biophys Acta. 1346:1997;109.
    • (1997) Biochim Biophys Acta , vol.1346 , pp. 109
    • Hada, T.1    Swift, L.L.2    Brash, A.R.3
  • 33
    • 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
  • 34
    • 0022480333 scopus 로고
    • The stereochemistry of the reactions of lipoxygenases and their metabolites. Proposed nomenclature of lipoxygenases and related enzymes
    • Kühn 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. 58:1986;273.
    • (1986) Adv Enzymol , vol.58 , pp. 273
    • Kühn, H.1    Schewe, T.2    Rapoport, S.M.3
  • 35
    • 0007909804 scopus 로고
    • Evidence for a lipoxygenase mechanism in the biosynthesis of epoxide and dihydroxy leukotrienes from 15(S)-hydroperoxyicosatetraenoic acid by human platelets and porcine leukocytes
    • Maas R.L., Brash A.R. Evidence for a lipoxygenase mechanism in the biosynthesis of epoxide and dihydroxy leukotrienes from 15(S)-hydroperoxyicosatetraenoic acid by human platelets and porcine leukocytes. Proc. Natl Acad Sci USA. 80:1983;2884.
    • (1983) Proc. Natl Acad Sci USA , vol.80 , pp. 2884
    • Maas, R.L.1    Brash, A.R.2
  • 36
    • 0027246677 scopus 로고
    • The three-dimensional structure of an arachidonic acid 15-lipoxygenase
    • Boyington J.C., Gaffney B.J., Amzel L.M. The three-dimensional structure of an arachidonic acid 15-lipoxygenase. Science. 260:1993;1482.
    • (1993) Science , vol.260 , pp. 1482
    • Boyington, J.C.1    Gaffney, B.J.2    Amzel, L.M.3
  • 37
    • 0029740369 scopus 로고    scopus 로고
    • Crystal structure of soybean lipoxygenase L-1 at 1.4 Å resolution
    • Minor W., Steczko J., Stec B., et al. Crystal structure of soybean lipoxygenase L-1 at 1.4 Å resolution. Biochemistry. 35:1996;10687.
    • (1996) Biochemistry , vol.35 , pp. 10687
    • Minor, W.1    Steczko, J.2    Stec, B.3
  • 38
    • 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
  • 39
    • 0030736867 scopus 로고    scopus 로고
    • The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate binding
    • 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 binding. Nat Struct Biol. 4:1997;1003.
    • (1997) Nat Struct Biol , vol.4 , pp. 1003
    • Gillmor, S.A.1    Villasenor, A.2    Fletterick, R.3    Sigal, E.4    Browner, M.F.5
  • 40
    • 0020479088 scopus 로고
    • Positional specificity of a reticulocyte lipoxygenase. Conversion of arachidonic Acid to 15-S-hydroperoxy-eicosatetraenoic acid
    • Bryant R.W., Bailey J.M., Schewe T., Rapoport S.M. Positional specificity of a reticulocyte lipoxygenase. Conversion of arachidonic Acid to 15-S-hydroperoxy-eicosatetraenoic acid. J Biol Chem. 257:1982;6050.
    • (1982) J Biol Chem , vol.257 , pp. 6050
    • Bryant, R.W.1    Bailey, J.M.2    Schewe, T.3    Rapoport, S.M.4
  • 41
    • 0016665429 scopus 로고
    • Arachidonate lipoxygenase in blood platelets
    • Nugteren D.H. Arachidonate lipoxygenase in blood platelets. Biochim Biophys Acta. 380:1975;299.
    • (1975) Biochim Biophys Acta , vol.380 , pp. 299
    • Nugteren, D.H.1
  • 42
    • 0025144594 scopus 로고
    • On singular or dual positional specificity of lipoxygenases. The number of chiral products varies with alignment of methylene groups at the active site of the enzyme
    • Kühn H., Sprecher H., Brash A.R. On singular or dual positional specificity of lipoxygenases. The number of chiral products varies with alignment of methylene groups at the active site of the enzyme. J Biol Chem. 265:1990;16300.
    • (1990) J Biol Chem , vol.265 , pp. 16300
    • Kühn, H.1    Sprecher, H.2    Brash, A.R.3
  • 43
    • 0019888819 scopus 로고
    • Double dioxygenation of arachidonic acid by soybean lipoxygenase-1. Kinetics and regio-stereo specificities of the reaction steps
    • Van Os C.P., Rijke-Schilder G.P., Van Halbeek H., Verhagen J., Vliegenthart J.F. Double dioxygenation of arachidonic acid by soybean lipoxygenase-1. Kinetics and regio-stereo specificities of the reaction steps. Biochim Biophys Acta. 663:1981;177.
    • (1981) Biochim Biophys Acta , vol.663 , pp. 177
    • Van Os, C.P.1    Rijke-Schilder, G.P.2    Van Halbeek, H.3    Verhagen, J.4    Vliegenthart, J.F.5
  • 44
    • 0026072935 scopus 로고
    • A primary determinant for lipoxygenase positional specificity
    • Sloane D.L., Leung R., Craik C.S., Sigal E. A primary determinant for lipoxygenase positional specificity. Nature. 354:1991;149.
    • (1991) Nature , vol.354 , pp. 149
    • Sloane, D.L.1    Leung, R.2    Craik, C.S.3    Sigal, E.4
  • 45
    • 0029042095 scopus 로고
    • Conversion of human 15-lipoxygenase to an efficient 12-lipoxygenase: The side-chain geometry of amino acids 417 and 418 determine positional specificity
    • 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. 8:1995;275.
    • (1995) Protein Eng , vol.8 , pp. 275
    • Sloane, D.L.1    Leung, R.2    Barnett, J.3    Craik, C.S.4    Sigal, E.5
  • 46
    • 0027274940 scopus 로고
    • Rat 12-lipoxygenase: mutations of amino acids implicated in the positional specificity of 15- And 12-lipoxygenases
    • Watanabe T, Haeggström JZ. Rat 12-lipoxygenase: mutations of amino acids implicated in the positional specificity of 15- and 12-lipoxygenases. Biochem Biophys Res Commun 1993;192;1023.
    • (1993) Biochem Biophys Res Commun , vol.192 , pp. 1023
    • Watanabe, T.1    Haeggström, J.Z.2
  • 47
    • 0030596087 scopus 로고    scopus 로고
    • Phenylalanine 353 is a primary determinant for the positional specificity of mammalian 15-lipoxygenases
    • Borngräber 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. 264:1996;1145.
    • (1996) J Mol Biol , vol.264 , pp. 1145
    • Borngräber, S.1    Kuban, R.J.2    Anton, M.3    Kuhn, H.4
  • 48
    • 0039134578 scopus 로고    scopus 로고
    • Shape and specificity in mammalian 15-lipoxygenase active site
    • Borngräber S., Browner M., Gillmor S., et al. Shape and specificity in mammalian 15-lipoxygenase active site. J Biol Chem. 274:1999;37345.
    • (1999) J Biol Chem , vol.274 , pp. 37345
    • Borngräber, S.1    Browner, M.2    Gillmor, S.3
  • 49
    • 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 USA. 96:1999;4192.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4192
    • Hornung, E.1    Walther, M.2    Kühn, H.3    Feussner, I.4
  • 50
    • 0027166718 scopus 로고
    • Structure-function properties of human platelet 12-lipoxygenase. Chimeric enzyme and in vitro mutagenesis studies
    • Chen X.S., Funk C.D. Structure-function properties of human platelet 12-lipoxygenase. Chimeric enzyme and in vitro mutagenesis studies. FASEB J. 7:1993;694.
    • (1993) FASEB J , vol.7 , pp. 694
    • Chen, X.S.1    Funk, C.D.2
  • 51
    • 0029795583 scopus 로고    scopus 로고
    • Defining the arachidonic acid binding site of human 15-lipoxygenase. Molecular modeling and mutagenesis
    • Gan Q.F., Browner M.F., Sloane D.L., Sigal E. Defining the arachidonic acid binding site of human 15-lipoxygenase. Molecular modeling and mutagenesis. J Biol Chem. 271:1996;25412.
    • (1996) J Biol Chem , vol.271 , pp. 25412
    • Gan, Q.F.1    Browner, M.F.2    Sloane, D.L.3    Sigal, E.4
  • 53
    • 0032011685 scopus 로고    scopus 로고
    • Relation between positional specificity and chirality in mammalian lipoxygenases
    • Prigge S.T., Gaffney B.J., Amzel L.M. Relation between positional specificity and chirality in mammalian lipoxygenases. Nature Structur Biol. 5:1998;178.
    • (1998) Nature Structur Biol , vol.5 , pp. 178
    • Prigge, S.T.1    Gaffney, B.J.2    Amzel, L.M.3
  • 54
    • 0032374064 scopus 로고    scopus 로고
    • ω-Oxidation Impairs Oxidizability of Polyenoic Fatty Acids by 15-Lipoxygenases. Consequences for substrate orientation at the active site
    • Ivanov I, Schwarz K, Holzhütter HG, Myagkova G, Kuhn H. ω-Oxidation Impairs Oxidizability of Polyenoic Fatty Acids by 15-Lipoxygenases. Consequences for substrate orientation at the active site. Biochem J 336:345.
    • Biochem J , vol.336 , pp. 345
    • Ivanov, I.1    Schwarz, K.2    Holzhütter, H.G.3    Myagkova, G.4    Kuhn, H.5
  • 56
    • 0028431011 scopus 로고
    • Expression of lipoxygenase in potato tubers of solanum tuberosum L
    • Geerts A., Feltkamp D., Rosahl S. Expression of lipoxygenase in potato tubers of solanum tuberosum L. Plant Physiol. 105:1994;269.
    • (1994) Plant Physiol , vol.105 , pp. 269
    • Geerts, A.1    Feltkamp, D.2    Rosahl, S.3
  • 57
    • 0027958244 scopus 로고
    • Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase
    • Suzuki H., Kishimoto K., Yoshimoto T., et al. 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. 1210:1994;308.
    • (1994) Biochim Biophys Acta , vol.1210 , pp. 308
    • Suzuki, H.1    Kishimoto, K.2    Yoshimoto, T.3
  • 58
    • 0032557633 scopus 로고    scopus 로고
    • Simultaneous expression of leukocyte-type 12-lipoxygenase and reticulocyte-type 15-lipoxygenase in rabbits
    • Berger M., Schwarz K., Thiele H., et al. Simultaneous expression of leukocyte-type 12-lipoxygenase and reticulocyte-type 15-lipoxygenase in rabbits. J Mol Biol. 278:1998;935.
    • (1998) J Mol Biol , vol.278 , pp. 935
    • Berger, M.1    Schwarz, K.2    Thiele, H.3
  • 59
    • 0033966938 scopus 로고    scopus 로고
    • Identification of amino acid determinants of the positional specificity of mouse 8S-lipoxygenase and human 15S-lipoxygenase-2
    • 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. 275:2000;1287.
    • (2000) J Biol Chem , vol.275 , pp. 1287
    • Jisaka, M.1    Kim, R.B.2    Boeglin, W.E.3    Brash, A.R.4


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