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Volumn 110, Issue 1-2, 1998, Pages 103-121

Cytochrome P450-dependent desaturation of lauric acid: Isoform selectivity and mechanism of formation of 11-dodecenoic acid

Author keywords

Cytochrome P450; Dehydrogenation; Isotope effect; Lauric acid; Mechanism; Rabbit liver

Indexed keywords

CYTOCHROME P450; HEMOPROTEIN; ISOTOPE; LAURIC ACID; VALPROIC ACID;

EID: 0031918678     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(97)00145-2     Document Type: Article
Times cited : (54)

References (31)
  • 3
    • 0029115761 scopus 로고
    • On the mechanism of amine oxidations by P450
    • Karki S.B., Dinnocenzo J.P. On the mechanism of amine oxidations by P450. Xenobiotica. 25:1995;711-724.
    • (1995) Xenobiotica , vol.25 , pp. 711-724
    • Karki, S.B.1    Dinnocenzo, J.P.2
  • 5
    • 0024429854 scopus 로고
    • Cytochrome P-450 catalysis: Radical intermediates and dehydrogenation reactions
    • Ortiz de Montellano P.R. Cytochrome P-450 catalysis: Radical intermediates and dehydrogenation reactions. Trends in Pharmacological Sciences. 10:1989;354-359.
    • (1989) Trends in Pharmacological Sciences , vol.10 , pp. 354-359
    • Ortiz De Montellano, P.R.1
  • 6
    • 0025336922 scopus 로고
    • Chemical synthesis and cytotoxic properties of N-alkylcarbamic acid thioesters, metabolites of hepatotoxic formamides
    • Han D.H., Pearson P.G., Baillie T.A., Dayal R., Tsang L.H., Gescher A. Chemical synthesis and cytotoxic properties of N-alkylcarbamic acid thioesters, metabolites of hepatotoxic formamides. Chem. Res. Toxicol. 3:1990;118-124.
    • (1990) Chem. Res. Toxicol. , vol.3 , pp. 118-124
    • Han, D.H.1    Pearson, P.G.2    Baillie, T.A.3    Dayal, R.4    Tsang, L.H.5    Gescher, A.6
  • 7
    • 0026063020 scopus 로고
    • Enzymatic oxidation of ethyl carbamate to vinyl carbamate and its role as an intermediate in the formation of 1,N6-ethenoadenosine
    • Guengerich F.P., Kim D.-H. Enzymatic oxidation of ethyl carbamate to vinyl carbamate and its role as an intermediate in the formation of 1,N6-ethenoadenosine. Chem. Res. Toxicol. 4:1991;413-421.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 413-421
    • Guengerich, F.P.1    Kim, D.-H.2
  • 8
    • 0030050265 scopus 로고    scopus 로고
    • Mechanistic studies on the cytochrome P450-catalyzed dehydrogenation of 3-methylindole
    • Skiles G.L., Yost G.S. Mechanistic studies on the cytochrome P450-catalyzed dehydrogenation of 3-methylindole. Chem. Res. Toxicol. 9:1996;291-297.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 291-297
    • Skiles, G.L.1    Yost, G.S.2
  • 10
    • 0023697057 scopus 로고
    • Cytochrome P-450-catalyzed desaturation of valproic acid in vitro
    • Rettie A.E., Boberg M., Rettenmeier A.W., Baillie T.A. Cytochrome P-450-catalyzed desaturation of valproic acid in vitro. J. Biol. Chem. 263:1988;13733-13738.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13733-13738
    • Rettie, A.E.1    Boberg, M.2    Rettenmeier, A.W.3    Baillie, T.A.4
  • 11
    • 0029079640 scopus 로고
    • CYP4 isozyme specificity and the relationship between ω-hydroxylation and terminal desaturation of valproic acid
    • Rettie A.E., Sheffels P.R., Korzekwa K.R., Gonzalez F.J., Philpot R.M., Baillie T.A. CYP4 isozyme specificity and the relationship between ω-hydroxylation and terminal desaturation of valproic acid. Biochemistry. 34:1995;7889-7895.
    • (1995) Biochemistry , vol.34 , pp. 7889-7895
    • Rettie, A.E.1    Sheffels, P.R.2    Korzekwa, K.R.3    Gonzalez, F.J.4    Philpot, R.M.5    Baillie, T.A.6
  • 13
    • 0029953241 scopus 로고    scopus 로고
    • CYP enzymes catalyze the formation of a terminal olefin from 2-ethylhexanoic acid in rat and human liver
    • Pennannen S., Kojo A., Pasanen M., Liesivuori J., Juvonen R.O., Komulainen H. CYP enzymes catalyze the formation of a terminal olefin from 2-ethylhexanoic acid in rat and human liver. Hum. Exp. Toxicol. 15:1996;435-442.
    • (1996) Hum. Exp. Toxicol. , vol.15 , pp. 435-442
    • Pennannen, S.1    Kojo, A.2    Pasanen, M.3    Liesivuori, J.4    Juvonen, R.O.5    Komulainen, H.6
  • 14
    • 0024331651 scopus 로고
    • Identification and induction of cytochromes P450, P450IIE1 and P450IA1 in rabbit bone marrow
    • Schnier G.G., Laethem C.L., Koop D.R. Identification and induction of cytochromes P450, P450IIE1 and P450IA1 in rabbit bone marrow. J. Pharm. Exp. Ther. 251:1989;790-796.
    • (1989) J. Pharm. Exp. Ther. , vol.251 , pp. 790-796
    • Schnier, G.G.1    Laethem, C.L.2    Koop, D.R.3
  • 15
    • 0019773541 scopus 로고
    • Properties of electrophoretically homogenous constitutive forms of cytochrome P-450
    • Koop D.R., Persson A.V., Coon M.J. Properties of electrophoretically homogenous constitutive forms of cytochrome P-450. J. Biol. Chem. 256:1981;10704-10711.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10704-10711
    • Koop, D.R.1    Persson, A.V.2    Coon, M.J.3
  • 16
    • 0020458459 scopus 로고
    • Purification and characterization of a unique isozyme of cytochrome P-450 from liver microsomes of ethanol-treated rabbits
    • Koop D.R., Morgan E.T., Tarr G.E., Coon M.J. Purification and characterization of a unique isozyme of cytochrome P-450 from liver microsomes of ethanol-treated rabbits. J. Biol. Chem. 257:1982;8471-8480.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8471-8480
    • Koop, D.R.1    Morgan, E.T.2    Tarr, G.E.3    Coon, M.J.4
  • 17
    • 0021166729 scopus 로고
    • Purification of liver microsomal cytochrome P-450 isozymes 3a and 6 from imidazole-treated rabbits. Evidence for the identity of isozyme 3a with the form obtained from ethanol treatment
    • Koop D.R., Coon M.J. Purification of liver microsomal cytochrome P-450 isozymes 3a and 6 from imidazole-treated rabbits. Evidence for the identity of isozyme 3a with the form obtained from ethanol treatment. Mol. Pharmacol. 25:1984;494-501.
    • (1984) Mol. Pharmacol. , vol.25 , pp. 494-501
    • Koop, D.R.1    Coon, M.J.2
  • 18
    • 0026739489 scopus 로고
    • Purification and properties of a cytochrome P450 arachidonic acid epoxygenase from rabbit renal cortex
    • Laethem R.M., Laethem C.L., Koop D.R. Purification and properties of a cytochrome P450 arachidonic acid epoxygenase from rabbit renal cortex. J. Biol. Chem. 267:1992;5552-5559.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5552-5559
    • Laethem, R.M.1    Laethem, C.L.2    Koop, D.R.3
  • 20
    • 0030587544 scopus 로고    scopus 로고
    • Allelic variants of human cytochrome P450 2C9:Baculovirus-mediated expression, purification, structural characterization, substrate stereoselectivity and prochiral selectivity of the wild-type and 1359L mutant forms
    • Haining R.L., Hunter A.P., Veronese M.E., Trager W.F., Rettie A.E. Allelic variants of human cytochrome P450 2C9:Baculovirus-mediated expression, purification, structural characterization, substrate stereoselectivity and prochiral selectivity of the wild-type and 1359L mutant forms. Arch. Biochem. Biophys. 333:1996;447-458.
    • (1996) Arch. Biochem. Biophys. , vol.333 , pp. 447-458
    • Haining, R.L.1    Hunter, A.P.2    Veronese, M.E.3    Trager, W.F.4    Rettie, A.E.5
  • 21
    • 0024370045 scopus 로고
    • Primary structures of cytochrome P-450 isozyme 5 from rabbit and rat and regulation of species-dependent expression and induction in lung and liver: Identification of cytochrome P-450 gene subfamily IVB
    • Gasser R., Philpot R.M. Primary structures of cytochrome P-450 isozyme 5 from rabbit and rat and regulation of species-dependent expression and induction in lung and liver: identification of cytochrome P-450 gene subfamily IVB. Mol. Pharmacol. 35:1989;617-625.
    • (1989) Mol. Pharmacol. , vol.35 , pp. 617-625
    • Gasser, R.1    Philpot, R.M.2
  • 22
    • 0014429295 scopus 로고
    • Role of hemoprotein P450 in fatty acid ω-hydroxylation in a soluble enzyme system from liver microsomes
    • Lu A.Y.H., Coon M.J. Role of hemoprotein P450 in fatty acid ω-hydroxylation in a soluble enzyme system from liver microsomes. J. Biol. Chem. 243:1968;1331-1332.
    • (1968) J. Biol. Chem. , vol.243 , pp. 1331-1332
    • Lu, A.Y.H.1    Coon, M.J.2
  • 23
    • 0014531747 scopus 로고
    • Fatty acid interaction with the hydroxylating enzyme system of rat liver microsomes
    • Orrenius S., Thor H. Fatty acid interaction with the hydroxylating enzyme system of rat liver microsomes. Eur. J. Biochem. 9:1969;415-418.
    • (1969) Eur. J. Biochem. , vol.9 , pp. 415-418
    • Orrenius, S.1    Thor, H.2
  • 24
    • 0018074896 scopus 로고
    • Purification and properties of cytochrome P450 obtained from liver microsomes of untreated rats by lauric acid affinity chromatography
    • Gibson G.G., Schenkman J.B. Purification and properties of cytochrome P450 obtained from liver microsomes of untreated rats by lauric acid affinity chromatography. J. Biol. Chem. 253:1978;5957-5963.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5957-5963
    • Gibson, G.G.1    Schenkman, J.B.2
  • 25
    • 0025270931 scopus 로고
    • ω and (ω-1)-hydroxylation of arachidonic acid, lauric acid and prostaglandin A1 by multiple forms of cytochrome P450 purified from rat hepatic microsomes
    • Tanaka S., Imaoka S., Kusunose E., Kusunose M., Maekawa M., Funae Y. ω and (ω-1)-hydroxylation of arachidonic acid, lauric acid and prostaglandin A1 by multiple forms of cytochrome P450 purified from rat hepatic microsomes. Biochim. Biophys. Acta. 1043:1990;177-181.
    • (1990) Biochim. Biophys. Acta , vol.1043 , pp. 177-181
    • Tanaka, S.1    Imaoka, S.2    Kusunose, E.3    Kusunose, M.4    Maekawa, M.5    Funae, Y.6
  • 26
    • 0030269976 scopus 로고    scopus 로고
    • Effects of steric bulk and conformational rigidity on fatty acid omega hydroxylation by a cytochrome P450 4A1 fusion protein
    • Bambal R.B., Hanzlik R.P. Effects of steric bulk and conformational rigidity on fatty acid omega hydroxylation by a cytochrome P450 4A1 fusion protein. Arch. Biochem. Biophys. 334:1996;59-66.
    • (1996) Arch. Biochem. Biophys. , vol.334 , pp. 59-66
    • Bambal, R.B.1    Hanzlik, R.P.2
  • 28
    • 0026324038 scopus 로고
    • ω and (ω-1)-hydroxylation of eicosanoids and fatty acids by high-performance liquid chromatography
    • Okita R.T., Clark J.E., Masters B.S.S. ω and (ω-1)-hydroxylation of eicosanoids and fatty acids by high-performance liquid chromatography. Methods. Enzymol. 206:1991;432-441.
    • (1991) Methods. Enzymol. , vol.206 , pp. 432-441
    • Okita, R.T.1    Clark, J.E.2    Masters, B.S.S.3
  • 29
    • 0024501044 scopus 로고
    • Prostaglandin and fatty acid ω- And (ω-1)-oxidation in rabbit lung: Acetylenic fatty acid mechanism-based inactivators as specific inhibitors
    • Muerhoff A.S., Williams D.E., Reich N.O., CaJacob C.A., Ortiz de Montellano P.R., Masters B.S.S. Prostaglandin and fatty acid ω- and (ω-1)-oxidation in rabbit lung: acetylenic fatty acid mechanism-based inactivators as specific inhibitors. J. Biol. Chem. 264:1989;749-756.
    • (1989) J. Biol. Chem. , vol.264 , pp. 749-756
    • Muerhoff, A.S.1    Williams, D.E.2    Reich, N.O.3    Cajacob, C.A.4    Ortiz De Montellano, P.R.5    Masters, B.S.S.6
  • 30
    • 0025083935 scopus 로고
    • Characterization of rabbit liver P450IIE1 synthesised in transformed yeast cells
    • Imai Y., Uno T., Nakamura M. Characterization of rabbit liver P450IIE1 synthesised in transformed yeast cells. J. Biochem. 108:1990;522-524.
    • (1990) J. Biochem. , vol.108 , pp. 522-524
    • Imai, Y.1    Uno, T.2    Nakamura, M.3
  • 31
    • 0000497670 scopus 로고
    • Isotopically sensitive branching and its effect on the observed intramolecular isotope effects in cytochrome P450 catalyzed reactions: A new method for the estimation of intrinsic isotope effects
    • Jones J.P., Korzekwa K.R., Rettie A.E., Trager W.F. Isotopically sensitive branching and its effect on the observed intramolecular isotope effects in cytochrome P450 catalyzed reactions: A new method for the estimation of intrinsic isotope effects. J. Am. Chem. Soc. 108:1986;7074-7078.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 7074-7078
    • Jones, J.P.1    Korzekwa, K.R.2    Rettie, A.E.3    Trager, W.F.4


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