메뉴 건너뛰기




Volumn 47, Issue 12, 2008, Pages 3917-3925

Oxidative metabolism of a fatty acid amide hydrolase-regulated lipid, arachidonoyltaurine

Author keywords

[No Author keywords available]

Indexed keywords

ARACHIDONOYLTAURINE; FATTY ACID AMIDE HYDROLASE; OXIDATIVE METABOLISM; POLYUNSATURATED FATTY ACIDS;

EID: 41149171201     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702530z     Document Type: Article
Times cited : (21)

References (62)
  • 1
    • 33748703859 scopus 로고    scopus 로고
    • The endocannabinoid system as an emerging target of pharmacotherapy
    • Pacher, P., Batkai, S., and Kunos, G. (2006) The endocannabinoid system as an emerging target of pharmacotherapy. Pharmacol. Rev. 58, 389-462.
    • (2006) Pharmacol. Rev , vol.58 , pp. 389-462
    • Pacher, P.1    Batkai, S.2    Kunos, G.3
  • 2
    • 0142166330 scopus 로고    scopus 로고
    • Cannabinoids: Potential anticancer agents
    • Guzman, M. (2003) Cannabinoids: Potential anticancer agents. Nat. Rev. Cancer 3, 745-755.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 745-755
    • Guzman, M.1
  • 5
    • 0034766553 scopus 로고    scopus 로고
    • Pharmacological actions and therapeutic uses of cannabis and cannabinoids
    • Kumar, R., Chambers, W., and Pertwee, R. (2001) Pharmacological actions and therapeutic uses of cannabis and cannabinoids. Anaesthesia 56, 1059-1068.
    • (2001) Anaesthesia , vol.56 , pp. 1059-1068
    • Kumar, R.1    Chambers, W.2    Pertwee, R.3
  • 6
    • 0035120753 scopus 로고    scopus 로고
    • Involvement of cannabinoids in the cardioprotection induced by lipopolysaccharide
    • Lagneux, C., and Lamontagne, D. (2001) Involvement of cannabinoids in the cardioprotection induced by lipopolysaccharide. Br. J. Pharmacol. 132, 793-796.
    • (2001) Br. J. Pharmacol , vol.132 , pp. 793-796
    • Lagneux, C.1    Lamontagne, D.2
  • 8
    • 0242583853 scopus 로고    scopus 로고
    • The endocannabinoid system in the basal ganglia and in the mesolimbic reward system: Implications for neurological and psychiatric disorders
    • van der Stelt, M., and Di Marzo, V. (2003) The endocannabinoid system in the basal ganglia and in the mesolimbic reward system: Implications for neurological and psychiatric disorders. Eur. J. Pharmacol. 480, 133-150.
    • (2003) Eur. J. Pharmacol , vol.480 , pp. 133-150
    • van der Stelt, M.1    Di Marzo, V.2
  • 9
    • 0042572380 scopus 로고    scopus 로고
    • Fatty acid amide hydrolase: An emerging therapeutic target in the endocannabinoid system
    • Cravatt, B. F., and Lichtman, A. H. (2003) Fatty acid amide hydrolase: An emerging therapeutic target in the endocannabinoid system. Curr. Opin. Chem. Biol. 7, 469-475.
    • (2003) Curr. Opin. Chem. Biol , vol.7 , pp. 469-475
    • Cravatt, B.F.1    Lichtman, A.H.2
  • 12
    • 0036669583 scopus 로고    scopus 로고
    • Mammalian arachidonate 15-lipoxygenases structure, function, and biological implications
    • Kuhn, H., Walther, M., and Kuban, R. J. (2002) Mammalian arachidonate 15-lipoxygenases structure, function, and biological implications. Prostaglandins Other Lipid Mediators 68-69, 263-290.
    • (2002) Prostaglandins Other Lipid Mediators , vol.68-69 , pp. 263-290
    • Kuhn, H.1    Walther, M.2    Kuban, R.J.3
  • 13
    • 4143107932 scopus 로고    scopus 로고
    • Cyclooxygenase isozymes: The biology of prostaglandin synthesis and inhibition
    • Simmons, D. L., Botting, R. M., and Hla, T. (2004) Cyclooxygenase isozymes: The biology of prostaglandin synthesis and inhibition. Pharmacol. Rev. 56, 387-437.
    • (2004) Pharmacol. Rev , vol.56 , pp. 387-437
    • Simmons, D.L.1    Botting, R.M.2    Hla, T.3
  • 18
    • 0029911267 scopus 로고    scopus 로고
    • Flexibility of the nsaid binding site in the structure of human cyclooxygenase-2
    • Luong, C., Miller, A., Barnett, J., Chow, J., Ramesha, C., and Browner, M. F. (1996) Flexibility of the nsaid binding site in the structure of human cyclooxygenase-2. Nat. Struct. Biol. 3, 927-933.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 927-933
    • Luong, C.1    Miller, A.2    Barnett, J.3    Chow, J.4    Ramesha, C.5    Browner, M.F.6
  • 19
    • 0041664897 scopus 로고    scopus 로고
    • Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid anandamide
    • Kozak, K. R., Prusakiewicz, J. J., Rowlinson, S. W., Prudhomme, D. R., and Marnett, L. J. (2003) Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid anandamide. Biochemistry 42, 9041-9049.
    • (2003) Biochemistry , vol.42 , pp. 9041-9049
    • Kozak, K.R.1    Prusakiewicz, J.J.2    Rowlinson, S.W.3    Prudhomme, D.R.4    Marnett, L.J.5
  • 20
    • 0035839520 scopus 로고    scopus 로고
    • Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid 2-arachidonylglycerol
    • Kozak, K. R., Prusakiewicz, J. J., Rowlinson, S. W., Schneider, C., and Marnett, L. J. (2001) Amino acid determinants in cyclooxygenase-2 oxygenation of the endocannabinoid 2-arachidonylglycerol. J. Biol. Chem. 276, 30072-30077.
    • (2001) J. Biol. Chem , vol.276 , pp. 30072-30077
    • Kozak, K.R.1    Prusakiewicz, J.J.2    Rowlinson, S.W.3    Schneider, C.4    Marnett, L.J.5
  • 21
    • 0034721794 scopus 로고    scopus 로고
    • Oxygenation of the endocannabinoid, 2-arachidonylglycerol, to glyceryl prostaglandins by cyclooxygenase-2
    • Kozak, K. R., Rowlinson, S. W., and Marnett, L. J. (2000) Oxygenation of the endocannabinoid, 2-arachidonylglycerol, to glyceryl prostaglandins by cyclooxygenase-2. J. Biol. Chem. 275, 33744-33749.
    • (2000) J. Biol. Chem , vol.275 , pp. 33744-33749
    • Kozak, K.R.1    Rowlinson, S.W.2    Marnett, L.J.3
  • 24
    • 0030611859 scopus 로고    scopus 로고
    • Synthesis of prostaglandin e2 ethanolamide from anandamide by cyclooxygenase-2
    • Yu, M., Ives, D., and Ramesha, C. S. (1997) Synthesis of prostaglandin e2 ethanolamide from anandamide by cyclooxygenase-2. J. Biol. Chem. 272, 21181-21186.
    • (1997) J. Biol. Chem , vol.272 , pp. 21181-21186
    • Yu, M.1    Ives, D.2    Ramesha, C.S.3
  • 25
    • 0026100805 scopus 로고
    • Enzymatic lipid peroxidation: Reactions of mammalian lipoxygenases
    • Yamamoto, S. (1991) "Enzymatic" lipid peroxidation: Reactions of mammalian lipoxygenases. Free Radical Biol. Med. 10, 149-159.
    • (1991) Free Radical Biol. Med , vol.10 , pp. 149-159
    • Yamamoto, S.1
  • 26
    • 0021924345 scopus 로고
    • Metabolic profile of linoleic acid in porcine leukocytes through the lipoxygenase pathway
    • Claeys, M., Kivits, G. A., Christ-Hazelhof, E., and Nugteren, D. H. (1985) Metabolic profile of linoleic acid in porcine leukocytes through the lipoxygenase pathway. Biochim. Biophys. Acta 837, 35-51.
    • (1985) Biochim. Biophys. Acta , vol.837 , pp. 35-51
    • Claeys, M.1    Kivits, G.A.2    Christ-Hazelhof, E.3    Nugteren, D.H.4
  • 27
    • 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
    • Kuhn, H., Sprecher, H., and Brash, A. R. (1990) 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, 16300-16305.
    • (1990) J. Biol. Chem , vol.265 , pp. 16300-16305
    • Kuhn, H.1    Sprecher, H.2    Brash, A.R.3
  • 28
    • 0019791853 scopus 로고
    • Arachidonic acid 15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes. Partial purification and properties
    • Narumiya, S., Salmon, J. A., Cottee, F. H., Weatherley, B. C., and Flower, R. J. (1981) Arachidonic acid 15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes. Partial purification and properties. J. Biol. Chem. 256, 9583-9592.
    • (1981) J. Biol. Chem , vol.256 , pp. 9583-9592
    • Narumiya, S.1    Salmon, J.A.2    Cottee, F.H.3    Weatherley, B.C.4    Flower, R.J.5
  • 29
    • 0031820286 scopus 로고    scopus 로고
    • Human platelets and polymorphonuclear leukocytes synthesize oxygenated derivatives of arachidonylethanolamide (anandamide): Their affinities for cannabinoid receptors and pathways of inactivation
    • Edgemond, W. S., Hillard, C. J., Falck, J. R., Kearn, C. S., and Campbell, W. B. (1998) Human platelets and polymorphonuclear leukocytes synthesize oxygenated derivatives of arachidonylethanolamide (anandamide): Their affinities for cannabinoid receptors and pathways of inactivation. Mol. Pharmacol. 54, 180-188.
    • (1998) Mol. Pharmacol , vol.54 , pp. 180-188
    • Edgemond, W.S.1    Hillard, C.J.2    Falck, J.R.3    Kearn, C.S.4    Campbell, W.B.5
  • 30
    • 0037189536 scopus 로고    scopus 로고
    • 15-Lipoxygenase metabolism of 2-arachidonylglycerol. Generation of a peroxisome proliferator-activated receptor α agonist
    • Kozak, K. R., Gupta, R. A., Moody, J. S., Ji, C., Boeglin, W. E., DuBois, R. N., Brash, A. R., and Marnett, L. J. (2002) 15-Lipoxygenase metabolism of 2-arachidonylglycerol. Generation of a peroxisome proliferator-activated receptor α agonist. J. Biol. Chem. 277, 23278-23286.
    • (2002) J. Biol. Chem , vol.277 , pp. 23278-23286
    • Kozak, K.R.1    Gupta, R.A.2    Moody, J.S.3    Ji, C.4    Boeglin, W.E.5    DuBois, R.N.6    Brash, A.R.7    Marnett, L.J.8
  • 31
    • 0035969952 scopus 로고    scopus 로고
    • Selective oxygenation of the endocannabinoid 2-arachidonylglycerol by leukocyte-type 12-lipoxygenase
    • Moody, J. S., Kozak, K. R., Ji, C., and Marnett, L. J. (2001) Selective oxygenation of the endocannabinoid 2-arachidonylglycerol by leukocyte-type 12-lipoxygenase. Biochemistry 40, 861-866.
    • (2001) Biochemistry , vol.40 , pp. 861-866
    • Moody, J.S.1    Kozak, K.R.2    Ji, C.3    Marnett, L.J.4
  • 33
    • 0025084538 scopus 로고
    • Oxygenation of biological membranes by the pure reticulocyte lipoxygenase
    • Kuhn, H., Belkner, J., Wiesner, R., and Brash, A. R. (1990) Oxygenation of biological membranes by the pure reticulocyte lipoxygenase. J. Biol. Chem. 265, 18351-18361.
    • (1990) J. Biol. Chem , vol.265 , pp. 18351-18361
    • Kuhn, H.1    Belkner, J.2    Wiesner, R.3    Brash, A.R.4
  • 34
    • 0027485473 scopus 로고
    • Investigation of the oxygenation of phospholipids by the porcine leukocyte and human platelet arachidonate 12-lipoxygenases
    • Takahashi, Y., Glasgow, W. C., Suzuki, H., Taketani, Y., Yamamoto, S., Anton, M., Kuhn, H., and Brash, A. R. (1993) Investigation of the oxygenation of phospholipids by the porcine leukocyte and human platelet arachidonate 12-lipoxygenases. Eur. J. Biochem. 218, 165-171.
    • (1993) Eur. J. Biochem , vol.218 , pp. 165-171
    • Takahashi, Y.1    Glasgow, W.C.2    Suzuki, H.3    Taketani, Y.4    Yamamoto, S.5    Anton, M.6    Kuhn, H.7    Brash, A.R.8
  • 35
    • 0025753586 scopus 로고
    • Catalytic properties of human platelet 12-lipoxygenase as compared with the enzymes of other origins
    • Hada, T., Ueda, N., Takahashi, Y., and Yamamoto, S. (1991) Catalytic properties of human platelet 12-lipoxygenase as compared with the enzymes of other origins. Biochim. Biophys. Acta 1083, 89-93.
    • (1991) Biochim. Biophys. Acta , vol.1083 , pp. 89-93
    • Hada, T.1    Ueda, N.2    Takahashi, Y.3    Yamamoto, S.4
  • 36
    • 0016665429 scopus 로고
    • Arachidonate lipoxygenase in blood platelets
    • Nugteren, D. H. (1975) Arachidonate lipoxygenase in blood platelets. Biochim. Biophys. Acta 380, 299-307.
    • (1975) Biochim. Biophys. Acta , vol.380 , pp. 299-307
    • Nugteren, D.H.1
  • 37
    • 0021738403 scopus 로고
    • Mechanism of the stimulation of prostaglandin h synthase and prostacyclin synthase by the antithrombotic and antimetastatic agent, nafazatrom
    • Marnett, L. J., Siedlik, P. H., Ochs, R. C., Pagels, W. R., Das, M., Honn, K. V., Warnock, R. H., Tainer, B. E., and Eling, T. E. (1984) Mechanism of the stimulation of prostaglandin h synthase and prostacyclin synthase by the antithrombotic and antimetastatic agent, nafazatrom. Mol. Pharmacol. 26, 328-335.
    • (1984) Mol. Pharmacol , vol.26 , pp. 328-335
    • Marnett, L.J.1    Siedlik, P.H.2    Ochs, R.C.3    Pagels, W.R.4    Das, M.5    Honn, K.V.6    Warnock, R.H.7    Tainer, B.E.8    Eling, T.E.9
  • 38
    • 0033551732 scopus 로고    scopus 로고
    • The binding of arachidonic acid in the cyclooxygenase active site of mouse prostaglandin endoperoxide synthase-2 (cox-2). A putative L-shaped binding conformation utilizing the top channel region
    • Rowlinson, S. W., Crews, B. C., Lanzo, C. A., and Marnett, L. J. (1999) The binding of arachidonic acid in the cyclooxygenase active site of mouse prostaglandin endoperoxide synthase-2 (cox-2). A putative L-shaped binding conformation utilizing the top channel region. J. Biol. Chem. 274, 23305-23310.
    • (1999) J. Biol. Chem , vol.274 , pp. 23305-23310
    • Rowlinson, S.W.1    Crews, B.C.2    Lanzo, C.A.3    Marnett, L.J.4
  • 39
    • 0013801574 scopus 로고
    • The in vitro differentiation of mononuclear phagocytes. 3. The reversibility of granule and hydrolytic enzyme formation and the turnover of granule constituents
    • Cohn, Z. A., and Benson, B. (1965) The in vitro differentiation of mononuclear phagocytes. 3. The reversibility of granule and hydrolytic enzyme formation and the turnover of granule constituents. J. Exp. Med. 122, 455-466.
    • (1965) J. Exp. Med , vol.122 , pp. 455-466
    • Cohn, Z.A.1    Benson, B.2
  • 40
    • 0029687682 scopus 로고    scopus 로고
    • Electrospray/collision-induced dissociation mass spectrometry of mono-, di- and tri-hydroxylated lipoxygenase products, including leukotrienes of the b-series and lipoxins
    • Griffiths, W. J., Yang, Y., Sjovall, J., and Lindgren, J. A. (1996) Electrospray/collision-induced dissociation mass spectrometry of mono-, di- and tri-hydroxylated lipoxygenase products, including leukotrienes of the b-series and lipoxins. Rapid Commun. Mass Spectrom. 10, 183-196.
    • (1996) Rapid Commun. Mass Spectrom , vol.10 , pp. 183-196
    • Griffiths, W.J.1    Yang, Y.2    Sjovall, J.3    Lindgren, J.A.4
  • 42
    • 0017264641 scopus 로고
    • Preparation and purification of lipid hydroperoxides from arachidonic and g-linolenic acids
    • Funk, M. O., Isaac, R., and Porter, N. A. (1976) Preparation and purification of lipid hydroperoxides from arachidonic and g-linolenic acids. Lipids 11, 113-117.
    • (1976) Lipids , vol.11 , pp. 113-117
    • Funk, M.O.1    Isaac, R.2    Porter, N.A.3
  • 43
    • 0022469232 scopus 로고
    • Bacterial lipopolysaccharides prime macrophages for enhanced release of arachidonic acid metabolites
    • Aderem, A. A., Cohen, D. S., Wright, S. D., and Cohn, Z. A. (1986) Bacterial lipopolysaccharides prime macrophages for enhanced release of arachidonic acid metabolites. J. Exp. Med. 164, 165-179.
    • (1986) J. Exp. Med , vol.164 , pp. 165-179
    • Aderem, A.A.1    Cohen, D.S.2    Wright, S.D.3    Cohn, Z.A.4
  • 44
    • 0022374102 scopus 로고
    • Lipoxygenase pathways of macrophages
    • Bonney, R. J., Opas, E. E., and Humes, J. L. (1985) Lipoxygenase pathways of macrophages. Fed. Proc. 44, 2933-2936.
    • (1985) Fed. Proc , vol.44 , pp. 2933-2936
    • Bonney, R.J.1    Opas, E.E.2    Humes, J.L.3
  • 45
    • 0018113995 scopus 로고
    • Regulation of prostaglandin synthesis and of the selective release of lysosomal hydrolases by mouse peritoneal macrophages
    • Bonney, R. J., Wightman, P. D., Davies, P., Sadowski, S. J., Kuehl, F. A., Jr., and Humes, J. L. (1978) Regulation of prostaglandin synthesis and of the selective release of lysosomal hydrolases by mouse peritoneal macrophages. Biochem. J. 176, 433-442.
    • (1978) Biochem. J , vol.176 , pp. 433-442
    • Bonney, R.J.1    Wightman, P.D.2    Davies, P.3    Sadowski, S.J.4    Kuehl Jr., F.A.5    Humes, J.L.6
  • 46
    • 0017848104 scopus 로고
    • Prostaglandin e production by human blood monocytes and mouse peritoneal macrophages
    • Kurland, J. I., and Bockman, R. (1978) Prostaglandin e production by human blood monocytes and mouse peritoneal macrophages. J. Exp. Med. 147, 952-957.
    • (1978) J. Exp. Med , vol.147 , pp. 952-957
    • Kurland, J.I.1    Bockman, R.2
  • 47
    • 0019836299 scopus 로고
    • Metabolism of polyunsaturated fatty acids by mouse peritoneal macrophages: The lipoxygenase metabolic pathway
    • Rabinovitch, H., Durand, J., Gualde, N., and Rigaud, M. (1981) Metabolism of polyunsaturated fatty acids by mouse peritoneal macrophages: The lipoxygenase metabolic pathway. Agents Actions 11, 580-583.
    • (1981) Agents Actions , vol.11 , pp. 580-583
    • Rabinovitch, H.1    Durand, J.2    Gualde, N.3    Rigaud, M.4
  • 48
    • 0019186817 scopus 로고
    • Mouse peritoneal macrophages release leukotriene c in response to a phagocytic stimulus
    • Rouzer, C. A., Scott, W. A., Cohn, Z. A., Blackburn, P., and Manning, J. M. (1980) Mouse peritoneal macrophages release leukotriene c in response to a phagocytic stimulus. Proc. Natl. Acad. Sci. U.S.A. 77, 4928-4932.
    • (1980) Proc. Natl. Acad. Sci. U.S.A , vol.77 , pp. 4928-4932
    • Rouzer, C.A.1    Scott, W.A.2    Cohn, Z.A.3    Blackburn, P.4    Manning, J.M.5
  • 49
    • 0018956931 scopus 로고
    • Regulation of arachidonic acid metabolites in macrophages
    • Scott, W. A., Zrike, J. M., Hamill, A. L., Kempe, J., and Cohn, Z. A. (1980) Regulation of arachidonic acid metabolites in macrophages. J. Exp. Med. 152, 324-335.
    • (1980) J. Exp. Med , vol.152 , pp. 324-335
    • Scott, W.A.1    Zrike, J.M.2    Hamill, A.L.3    Kempe, J.4    Cohn, Z.A.5
  • 50
    • 0020025017 scopus 로고
    • Resting macrophages produce distinct metabolites from exogenous arachidonic acid
    • Scott, W. A., Pawlowski, N. A., Andreach, M., and Cohn, Z. A. (1982) Resting macrophages produce distinct metabolites from exogenous arachidonic acid. J. Exp. Med. 155, 535-547.
    • (1982) J. Exp. Med , vol.155 , pp. 535-547
    • Scott, W.A.1    Pawlowski, N.A.2    Andreach, M.3    Cohn, Z.A.4
  • 51
    • 0035836521 scopus 로고    scopus 로고
    • Inhibition studies of soybean and human 15-lipoxygenases with long-chain alkenyl sulfate substrates
    • Mogul, R., and Holman, T. R. (2001) Inhibition studies of soybean and human 15-lipoxygenases with long-chain alkenyl sulfate substrates. Biochemistry 40, 4391-4397.
    • (2001) Biochemistry , vol.40 , pp. 4391-4397
    • Mogul, R.1    Holman, T.R.2
  • 52
    • 0031587044 scopus 로고    scopus 로고
    • Excess substrate inhibition of soybean lipoxygenase-1 is mainly oxygen-dependent
    • Berry, H., Debat, H., and Larreta-Garde, V. (1997) Excess substrate inhibition of soybean lipoxygenase-1 is mainly oxygen-dependent. FEBS Lett. 408, 324-326.
    • (1997) FEBS Lett , vol.408 , pp. 324-326
    • Berry, H.1    Debat, H.2    Larreta-Garde, V.3
  • 54
    • 0023656547 scopus 로고
    • A kinetic model for lipoxygenases based on experimental data with the lipoxygenase of reticulocytes
    • Ludwig, P., Holzhutter, H.-G., Colosimo, A., Silvestrini, M. C., Schewe, T., and Rapoport, S. M. (1987) A kinetic model for lipoxygenases based on experimental data with the lipoxygenase of reticulocytes. Eur. J. Biochem. 168, 325-337.
    • (1987) Eur. J. Biochem , vol.168 , pp. 325-337
    • Ludwig, P.1    Holzhutter, H.-G.2    Colosimo, A.3    Silvestrini, M.C.4    Schewe, T.5    Rapoport, S.M.6
  • 55
    • 0033571064 scopus 로고    scopus 로고
    • Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 155-lipoxygenase
    • Kilty, I., Logan, A., and Vickers, P. J. (1999) Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 155-lipoxygenase. Eur. J. Biochem. 266, 83-93.
    • (1999) Eur. J. Biochem , vol.266 , pp. 83-93
    • Kilty, I.1    Logan, A.2    Vickers, P.J.3
  • 56
    • 0034214325 scopus 로고    scopus 로고
    • Burger, F., Krieg, P., Marks, F., and Furstenberger, G. (2000) Positional- and stereo-selectivity of fatty acid oxygenation catalysed by mouse (12S)-lipoxygenase isoenzymes. Biochem. J. 348, 329-335.
    • Burger, F., Krieg, P., Marks, F., and Furstenberger, G. (2000) Positional- and stereo-selectivity of fatty acid oxygenation catalysed by mouse (12S)-lipoxygenase isoenzymes. Biochem. J. 348, 329-335.
  • 58
    • 0027196413 scopus 로고
    • Purification and characterization of recombinant histidine-tagged human platelet 12-lipoxygenase expressed in a baculovirus/insect cell system
    • Chen, X. S., Brash, A. R., and Funk, C. D. (1993) Purification and characterization of recombinant histidine-tagged human platelet 12-lipoxygenase expressed in a baculovirus/insect cell system. Eur. J. Biochem. 214, 845-852.
    • (1993) Eur. J. Biochem , vol.214 , pp. 845-852
    • Chen, X.S.1    Brash, A.R.2    Funk, C.D.3
  • 59
    • 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., Villasenor, A., Fletterick, R., Sigal, E., and Browner, M. F. (1997) The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity. Nat. Struct. Biol. 4, 1003-1009.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 1003-1009
    • Gillmor, S.A.1    Villasenor, A.2    Fletterick, R.3    Sigal, E.4    Browner, M.F.5
  • 60
    • 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., and Sigal, E. (1995) 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, 275-282.
    • (1995) Protein Eng , vol.8 , pp. 275-282
    • Sloane, D.L.1    Leung, R.2    Barnett, J.3    Craik, C.S.4    Sigal, E.5
  • 61
    • 0026072935 scopus 로고
    • A primary determinant for lipoxygenase positional specificity
    • Sloane, D. L., Leung, R., Craik, C. S., and Sigal, E. (1991) A primary determinant for lipoxygenase positional specificity. Nature 354, 149-152.
    • (1991) Nature , vol.354 , pp. 149-152
    • Sloane, D.L.1    Leung, R.2    Craik, C.S.3    Sigal, E.4
  • 62
    • 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., and Sigal, E. (1996) Defining the arachidonic acid binding site of human 15-lipoxygenase. Molecular modeling and mutagenesis. J. Biol. Chem. 271, 25412-25418.
    • (1996) J. Biol. Chem , vol.271 , pp. 25412-25418
    • Gan, Q.F.1    Browner, M.F.2    Sloane, D.L.3    Sigal, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.