메뉴 건너뛰기




Volumn , Issue , 2007, Pages 15-35

Oxidative, Reductive, and Hydrolytic Metabolism of Drugs

Author keywords

Cellular location reaction stoichiometry; Enzymes and drug metabolism; Polyunsaturated fatty acids epoxide derivatives

Indexed keywords


EID: 84889459943     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470191699.ch2     Document Type: Chapter
Times cited : (13)

References (67)
  • 2
    • 0021363128 scopus 로고
    • Reductive halothane metabolite formation and halothane binding in rat hepatic microsomes
    • Baker MT, Van Dyke RA. Reductive halothane metabolite formation and halothane binding in rat hepatic microsomes. Chem-Biol Interact 1984;49:121-132.
    • (1984) Chem-Biol Interact , vol.49 , pp. 121-132
    • Baker, M.T.1    Van Dyke, R.A.2
  • 3
    • 0000912344 scopus 로고    scopus 로고
    • Selenium-dependent glutathione peroxidases
    • In: Guengerich FP, editor, Comprehensive Toxicology, first ed. Elsevier Science, Oxford
    • Burk RF. Selenium-dependent glutathione peroxidases. In: Guengerich FP, editor. Biotransformation, Vol. 3, Comprehensive Toxicology, first ed. Elsevier Science, Oxford; 1997. p 229-242.
    • (1997) Biotransformation , vol.3 , pp. 229-242
    • Burk, R.F.1
  • 4
    • 0001366947 scopus 로고
    • Mechanism of cytochrome P-450 catalysis. Mechanism of N-dealkylation and amine oxide deoxygenation
    • Burka LT, Guengerich FP, Willard RJ, Macdonald TL. Mechanism of cytochrome P-450 catalysis. Mechanism of N-dealkylation and amine oxide deoxygenation. J Am Chem Soc 1985;107:2549-2551.
    • (1985) J Am Chem Soc , vol.107 , pp. 2549-2551
    • Burka, L.T.1    Guengerich, F.P.2    Willard, R.J.3    Macdonald, T.L.4
  • 5
    • 0003085358 scopus 로고    scopus 로고
    • Monoamine oxidase and flavin-containing monooxygenases
    • In:Guengerich FP, editor, Comprehensive Toxicology, first ed. Elsevier Science, Oxford
    • Cashman JR. Monoamine oxidase and flavin-containing monooxygenases. In:Guengerich FP, editor. Biotransformation, Vol. 3, Comprehensive Toxicology, first ed. Elsevier Science, Oxford; 1997. p 69-96.
    • (1997) Biotransformation , vol.3 , pp. 69-96
    • Cashman, J.R.1
  • 7
    • 0021800939 scopus 로고
    • Studies on the molecular mechanism of bioactivation of the selective nigrostriatal toxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
    • Chiba K, Peterson LA, Castagnoli KP, Trevor AJ, Castagnoli N Jr. Studies on the molecular mechanism of bioactivation of the selective nigrostriatal toxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine. Drug Metab Dispos 1985;13:342-347.
    • (1985) Drug Metab Dispos , vol.13 , pp. 342-347
    • Chiba, K.1    Peterson, L.A.2    Castagnoli, K.P.3    Trevor, A.J.4    Castagnoli Jr, N.5
  • 8
    • 0036230088 scopus 로고    scopus 로고
    • CYP2C9 polymorphism and warfarin dose requirements
    • Daly AK, Day CP, Aithal GP. CYP2C9 polymorphism and warfarin dose requirements. Br J Clin Pharmacol 2002;53:408-409.
    • (2002) Br J Clin Pharmacol , vol.53 , pp. 408-409
    • Daly, A.K.1    Day, C.P.2    Aithal, G.P.3
  • 9
    • 0036806568 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human alcohol dehydrogenase gene (ADHFel)
    • Deng Y, Wang Z, Gu S, Ji C, Ying K, Xie Y, Mao Y. Cloning and characterization of a novel human alcohol dehydrogenase gene (ADHFel). DNA Seq 2002;13:301-306.
    • (2002) DNA Seq , vol.13 , pp. 301-306
    • Deng, Y.1    Wang, Z.2    Gu, S.3    Ji, C.4    Ying, K.5    Xie, Y.6    Mao, Y.7
  • 10
    • 0022263133 scopus 로고
    • Purification and characterization of the human liver cytochromes P450 involved in debrisoquine 4-hydroxylation and phenacetin O-deethylation, two prototypes for genetic polymorphism in oxidative drug metabolism
    • Distlerath LM, Reilly PEB, Martin MV, Davis GG, Wilkinson GR, Guengerich FP. Purification and characterization of the human liver cytochromes P450 involved in debrisoquine 4-hydroxylation and phenacetin O-deethylation, two prototypes for genetic polymorphism in oxidative drug metabolism. J Biol Chem 1985;260:9057-9067.
    • (1985) J Biol Chem , vol.260 , pp. 9057-9067
    • Distlerath, L.M.1    Reilly, P.E.B.2    Martin, M.V.3    Davis, G.G.4    Wilkinson, G.R.5    Guengerich, F.P.6
  • 12
    • 0000122129 scopus 로고    scopus 로고
    • Alcohol dehydrogenases
    • In: Guengerich FP, editor, Comprehesive Toxicology, first ed. Elsevier Science, Oxford
    • Edenberg HJ, Bosron WF. Alcohol dehydrogenases. In: Guengerich FP, editor. Biotransformation, Vol. 3, Comprehesive Toxicology, first ed. Elsevier Science, Oxford; 1997. p 119-131.
    • (1997) Biotransformation , vol.3 , pp. 119-131
    • Edenberg, H.J.1    Bosron, W.F.2
  • 13
    • 0027381443 scopus 로고
    • An ethoxyquin-inducible aldehyde reductase from rat liver that metabolizes aflatoxin B1 defines a subfamily of aldo-keto reductases
    • Ellis EM, Judah DJ, Neal GE, Hayes JD. An ethoxyquin-inducible aldehyde reductase from rat liver that metabolizes aflatoxin B1 defines a subfamily of aldo-keto reductases. Proc Natl Acad Sci USA 1993;90:10350-10354.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10350-10354
    • Ellis, E.M.1    Judah, D.J.2    Neal, G.E.3    Hayes, J.D.4
  • 14
    • 0005430822 scopus 로고    scopus 로고
    • Aldo-keto reductases: structure, mechanism, and function
    • In: Guengerich FP, editor, Comprehensive Toxicology. first ed. Elsevier Science, Oxford
    • Flynn TG, Kubiseski TJ. Aldo-keto reductases: structure, mechanism, and function. In: Guengerich FP, editor. Biotransformation, Vol. 3, Comprehensive Toxicology. first ed. Elsevier Science, Oxford; 1997. p 133-147.
    • (1997) Biotransformation , vol.3 , pp. 133-147
    • Flynn, T.G.1    Kubiseski, T.J.2
  • 15
    • 0019990422 scopus 로고
    • Cytochrome P450 and flavin-containing monooxygenase-catalyzed formation of the carcinogen Nhydroxy-2-aminofluorene, and its covalent binding to nuclear DNA
    • Frederick CB, Mays JB, Ziegler DM, Guengerich FP, Kadlubar FF. Cytochrome P450 and flavin-containing monooxygenase-catalyzed formation of the carcinogen Nhydroxy-2-aminofluorene, and its covalent binding to nuclear DNA. Cancer Res 1982;42:2671-2677.
    • (1982) Cancer Res , vol.42 , pp. 2671-2677
    • Frederick, C.B.1    Mays, J.B.2    Ziegler, D.M.3    Guengerich, F.P.4    Kadlubar, F.F.5
  • 16
    • 29244479504 scopus 로고    scopus 로고
    • Merging protein, gene and genomic data: the evolution of the MDR-ADH family
    • Gonzalez-Duarte R, Albalat R. Merging protein, gene and genomic data: the evolution of the MDR-ADH family. Heredity 2005;95:184-197.
    • (2005) Heredity , vol.95 , pp. 184-197
    • Gonzalez-Duarte, R.1    Albalat, R.2
  • 17
    • 0019505849 scopus 로고
    • The effect of epoxide hydratase on benzo[a]pyrene diol epoxide hydrolysis and binding to DNA and mixed-function oxidase proteins
    • Gozukara EM, Belvedere G, Robinson RC, Deutsch J, Coon MJ, Guengerich FP, Gelboin HV. The effect of epoxide hydratase on benzo[a]pyrene diol epoxide hydrolysis and binding to DNA and mixed-function oxidase proteins. Mol Pharmacol 1981;19:153-161.
    • (1981) Mol Pharmacol , vol.19 , pp. 153-161
    • Gozukara, E.M.1    Belvedere, G.2    Robinson, R.C.3    Deutsch, J.4    Coon, M.J.5    Guengerich, F.P.6    Gelboin, H.V.7
  • 18
    • 0023664534 scopus 로고
    • Oxidative cleavage of carboxylic esters by cytochrome P-450
    • Guengerich FP. Oxidative cleavage of carboxylic esters by cytochrome P-450. J Biol Chem 1987;262:8459-8462.
    • (1987) J Biol Chem , vol.262 , pp. 8459-8462
    • Guengerich, F.P.1
  • 19
    • 0003047034 scopus 로고    scopus 로고
    • Biotransformation
    • Compr Toxicology, first ed. Elsevier Science, Oxford
    • Guengerich FP. Biotransformation, Vol. 3, Compr Toxicology, first ed. Elsevier Science, Oxford; 1997.
    • (1997) , vol.3
    • Guengerich, F.P.1
  • 20
    • 0032924934 scopus 로고    scopus 로고
    • Human cytochrome P-450 3A4: regulation and role in drug metabolism
    • Guengerich FP. Human cytochrome P-450 3A4: regulation and role in drug metabolism. Annu Rev Pharmacol Toxicol 1999;39:1-17.
    • (1999) Annu Rev Pharmacol Toxicol , vol.39 , pp. 1-17
    • Guengerich, F.P.1
  • 21
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • Guengerich FP. Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem Res Toxicol 2001;14:611-650.
    • (2001) Chem Res Toxicol , vol.14 , pp. 611-650
    • Guengerich, F.P.1
  • 22
    • 0037223878 scopus 로고    scopus 로고
    • Cytochrome P450 oxidations in the generation of reactive electrophiles:epoxidations and related reactions
    • Guengerich FP. Cytochrome P450 oxidations in the generation of reactive electrophiles:epoxidations and related reactions. Arch Biochem Biophys 2003;409:59-71.
    • (2003) Arch Biochem Biophys , vol.409 , pp. 59-71
    • Guengerich, F.P.1
  • 23
    • 84892246340 scopus 로고    scopus 로고
    • Human cytochrome P450 enzymes
    • In: Ortiz de Montellano PR, editor Cytochrome P450: Structure, Mechanism, and Biochemistry, third ed. Kluwer Academic/Plenum Publishers; New York
    • Guengerich FP. Human cytochrome P450 enzymes, In: Ortiz de Montellano PR, editor. Cytochrome P450: Structure, Mechanism, and Biochemistry, third ed. Kluwer Academic/Plenum Publishers; New York: 2005. p 377-531.
    • (2005) , pp. 377-531
    • Guengerich, F.P.1
  • 24
    • 33845469510 scopus 로고
    • Chemical mechanisms of catalysis by cytochromes P-450: a unified view
    • Guengerich FP, Macdonald TL. Chemical mechanisms of catalysis by cytochromes P-450: a unified view. Acc Chem Res 1984;17:9-16.
    • (1984) Acc Chem Res , vol.17 , pp. 9-16
    • Guengerich, F.P.1    Macdonald, T.L.2
  • 26
    • 27544495165 scopus 로고    scopus 로고
    • Function of human cytochrome P450s: characterization of the remaining orphans
    • Guengerich FP,Wu Z-L, Bartleson CJ. Function of human cytochrome P450s: characterization of the remaining orphans. Biochem Biophys Res Commun 2005;338:465-469.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 465-469
    • Guengerich, F.P.1    Wu, Z.-L.2    Bartleson, C.J.3
  • 27
    • 0001564040 scopus 로고    scopus 로고
    • Epoxide hydrolases
    • In: Guengerich FP, editor, Comprehensive Toxicology, first ed. Elsevier Science, Oxford
    • Hammock BD, Grant DF, Storms DH. Epoxide hydrolases. In: Guengerich FP, editor. Biotransforrnation, Vol. 3, Comprehensive Toxicology, first ed. Elsevier Science, Oxford; 1997. p 283-305.
    • (1997) Biotransforrnation , vol.3 , pp. 283-305
    • Hammock, B.D.1    Grant, D.F.2    Storms, D.H.3
  • 28
    • 0018801379 scopus 로고
    • The oxidation-reduction potentials of compound I/compound II and compound II/ferric couples of horseradish peroxidases A2 and C
    • Hayashi Y, Yamazaki I. The oxidation-reduction potentials of compound I/compound II and compound II/ferric couples of horseradish peroxidases A2 and C. J Biol Chem 1979;254:9101-9106.
    • (1979) J Biol Chem , vol.254 , pp. 9101-9106
    • Hayashi, Y.1    Yamazaki, I.2
  • 29
    • 0018574996 scopus 로고
    • Rat liver cytosolic azoreductase. Electron transport properties and the mechanism of dicoumarol inhibition of the purified enzyme
    • Huang M-T, Miwa GT, Cronheim N, Lu AYH. Rat liver cytosolic azoreductase. Electron transport properties and the mechanism of dicoumarol inhibition of the purified enzyme. J Biol Chem 1979;254:11223-11227.
    • (1979) J Biol Chem , vol.254 , pp. 11223-11227
    • Huang, M.-T.1    Miwa, G.T.2    Cronheim, N.3    Lu, A.Y.H.4
  • 30
    • 0028318860 scopus 로고
    • Human NAD(P)H-quinone oxidoredutase. Gene structure, activity, and tissue-specific expression
    • Jaiswal AK. Human NAD(P)H-quinone oxidoredutase. Gene structure, activity, and tissue-specific expression. J Biol Chem 1994;269:14502-14508.
    • (1994) J Biol Chem , vol.269 , pp. 14502-14508
    • Jaiswal, A.K.1
  • 31
    • 0030876351 scopus 로고    scopus 로고
    • A new nomenclature for the aldo-keto reductase superfamily
    • Jez JM, Flynn TG, Penning TM. A new nomenclature for the aldo-keto reductase superfamily. Biochem Pharmacol 1997;54:639-647.
    • (1997) Biochem Pharmacol , vol.54 , pp. 639-647
    • Jez, J.M.1    Flynn, T.G.2    Penning, T.M.3
  • 33
    • 33645086788 scopus 로고    scopus 로고
    • Phase 1 and phase 2 drug metabolism:terminology that we should phase out
    • Josephy PD, Guengerich FP, Miners JO. Phase 1 and phase 2 drug metabolism:terminology that we should phase out. Drug Metab Dispos 2005;37:579-584.
    • (2005) Drug Metab Dispos , vol.37 , pp. 579-584
    • Josephy, P.D.1    Guengerich, F.P.2    Miners, J.O.3
  • 35
    • 0024429460 scopus 로고
    • Glutathione transferases: a possible role in the detoxication and repair of DNA and lipid hydroperoxides
    • Ketterer B, Meyer DJ. Glutathione transferases: a possible role in the detoxication and repair of DNA and lipid hydroperoxides. Mut Res 1989;214:33-40.
    • (1989) Mut Res , vol.214 , pp. 33-40
    • Ketterer, B.1    Meyer, D.J.2
  • 36
    • 1942518251 scopus 로고    scopus 로고
    • Formation and reduction of aryl and heterocyclic nitroso compounds and significance in the flux of hydroxylamines
    • Kim D, Kadlubar FF, Teitel CH, Guengerich FP. Formation and reduction of aryl and heterocyclic nitroso compounds and significance in the flux of hydroxylamines. Chem Res Toxicol 2004;17:529-536.
    • (2004) Chem Res Toxicol , vol.17 , pp. 529-536
    • Kim, D.1    Kadlubar, F.F.2    Teitel, C.H.3    Guengerich, F.P.4
  • 37
    • 9644262449 scopus 로고    scopus 로고
    • The aldehyde oxidase gene cluster in mice and rat. Aldehyde oxidase homologue 3, a novel member of the molybdo-flavoenzyme family with selective expression in the olfactory mucosa
    • Kurosaki M, Terao M, Barzago MM, Bastone A, Bemardinello D, Salmona M, Garattini E. The aldehyde oxidase gene cluster in mice and rat. Aldehyde oxidase homologue 3, a novel member of the molybdo-flavoenzyme family with selective expression in the olfactory mucosa. J Biol Chem 2004;279:50482-50498.
    • (2004) J Biol Chem , vol.279 , pp. 50482-50498
    • Kurosaki, M.1    Terao, M.2    Barzago, M.M.3    Bastone, A.4    Bemardinello, D.5    Salmona, M.6    Garattini, E.7
  • 38
    • 0000353408 scopus 로고
    • The catalytic mechanism of microsomal epoxide hydrolase involves an ester intermediate
    • Lacourciere GM, Armstrong RN. The catalytic mechanism of microsomal epoxide hydrolase involves an ester intermediate. J Am Chem Soc 1993;115:10466-10467.
    • (1993) J Am Chem Soc , vol.115 , pp. 10466-10467
    • Lacourciere, G.M.1    Armstrong, R.N.2
  • 39
    • 0028354487 scopus 로고
    • Microsomal and soluble epoxide hydrolases are members of the same family of C-X bond hydrolase enzymes
    • Lacourciere GM, Armstrong RN. Microsomal and soluble epoxide hydrolases are members of the same family of C-X bond hydrolase enzymes. Chem Res Toxicol 1994;7:121-124.
    • (1994) Chem Res Toxicol , vol.7 , pp. 121-124
    • Lacourciere, G.M.1    Armstrong, R.N.2
  • 40
    • 0024538443 scopus 로고
    • Oxidation of substituted N,N-dimethylanilines by cytochrome P450: estimation of the effective oxidation-reduction potential of cytochrome P450
    • Macdonald TL, Gutheim WG, Martin RB, Guengerich FP. Oxidation of substituted N,N-dimethylanilines by cytochrome P450: estimation of the effective oxidation-reduction potential of cytochrome P450. Biochemistry 1989;28:2071-2077.
    • (1989) Biochemistry , vol.28 , pp. 2071-2077
    • Macdonald, T.L.1    Gutheim, W.G.2    Martin, R.B.3    Guengerich, F.P.4
  • 41
    • 0343553140 scopus 로고    scopus 로고
    • Peroxidases
    • In: Guengerich FP, editor, Comprehensive Toxicology, first ed. Elsevier Science, Oxford
    • Marnett LJ, Landino LM, Reddy GR. Peroxidases. In: Guengerich FP, editor. Biotransformation, Vol. 3, Comprehensive Toxicology, first ed. Elsevier Science, Oxford; 1997. p 149-163.
    • (1997) Biotransformation , vol.3 , pp. 149-163
    • Marnett, L.J.1    Landino, L.M.2    Reddy, G.R.3
  • 42
    • 0033851115 scopus 로고    scopus 로고
    • The chemical and biological versatility of riboflavin
    • Massey V. The chemical and biological versatility of riboflavin. Biochem Soc Trans 2000;28:283-296.
    • (2000) Biochem Soc Trans , vol.28 , pp. 283-296
    • Massey, V.1
  • 43
    • 0030989616 scopus 로고    scopus 로고
    • Oxidation of diclofenac to reactive intermediates by neutrophils, myeloperoxidase, and hypochlorous acid
    • Miyamoto G, Zahid N, Uetrecht JP. Oxidation of diclofenac to reactive intermediates by neutrophils, myeloperoxidase, and hypochlorous acid. Chem Res Toxicol 1997;10:414-419.
    • (1997) Chem Res Toxicol , vol.10 , pp. 414-419
    • Miyamoto, G.1    Zahid, N.2    Uetrecht, J.P.3
  • 44
    • 0033588227 scopus 로고    scopus 로고
    • Targeted disruption of the microsomal epoxide hydrolase gene. Microsomal epoxide hydrolase is required for the carcinogenic acitvity of 7,12-dimethylbenz[a]anthracene
    • Miyate M, Kudo G, Lee Y-H, Y.mg TJ, Gelboin HV, Fernandez-Salguero, Kimura S, Gonzalez FJ. Targeted disruption of the microsomal epoxide hydrolase gene. Microsomal epoxide hydrolase is required for the carcinogenic acitvity of 7,12-dimethylbenz[a]anthracene. J Biol Chem 1999;274:23963-23968.
    • (1999) J Biol Chem , vol.274 , pp. 23963-23968
    • Miyate, M.1    Kudo, G.2    Lee, Y.-H.3    Mg, Y.4    Gelboin, T.J.5    Fernandez-Salguero, H.V.6    Kimura, S.7    Gonzalez, F.J.8
  • 45
    • 2642550761 scopus 로고    scopus 로고
    • UV-dependent alternative splicing uncouples p53 activity and PIG3 gene function through rapid proteolytic degradation
    • Nicholls CD, Shields MA, Lee PWK, Robbins SM, Beattie TL. UV-dependent alternative splicing uncouples p53 activity and PIG3 gene function through rapid proteolytic degradation. J Biol Chem 2004;279:24171-24178.
    • (2004) J Biol Chem , vol.279 , pp. 24171-24178
    • Nicholls, C.D.1    Shields, M.A.2    Lee, P.W.K.3    Robbins, S.M.4    Beattie, T.L.5
  • 46
    • 84892193594 scopus 로고    scopus 로고
    • Substrate oxidation by cytochrome P450 enzymes
    • In: Ortiz de Montellano PR, editor, third ed. Kluwer Academic/Plenum Publishers; New York
    • Ortiz de Montellano PR, De Voss JJ. Substrate oxidation by cytochrome P450 enzymes. In: Ortiz de Montellano PR, editor. Cytochrome P450: Structure, Mechanism, and Biochemistry, third ed. Kluwer Academic/Plenum Publishers; New York: 2005. p 183-245.
    • (2005) Cytochrome P450: Structure, Mechanism, and Biochemistry , pp. 183-245
    • Ortiz De Montellano, P.R.1    De Voss, J.J.2
  • 47
    • 6344270255 scopus 로고    scopus 로고
    • Contribution of aldehyde oxidase, xanthine oxidase, and aldehyde dehydrogenase on the oxidation of aromatic aldehydes
    • Panoutsopoulos GI, Kouretas D, Beedham C. Contribution of aldehyde oxidase, xanthine oxidase, and aldehyde dehydrogenase on the oxidation of aromatic aldehydes. Chem Res Toxicol 2004;17:1368-1376.
    • (2004) Chem Res Toxicol , vol.17 , pp. 1368-1376
    • Panoutsopoulos, G.I.1    Kouretas, D.2    Beedham, C.3
  • 48
    • 16444379563 scopus 로고    scopus 로고
    • Introduction and overview of the aldo-keto reductase superfamily
    • In:Penning TM, Petrash JM, editors, first ed. Washington, DC: American Chemical Society
    • Penning TM. Introduction and overview of the aldo-keto reductase superfamily. In:Penning TM, Petrash JM, editors. Aldo-Keto Reductases and Toxicant Metabolism. first ed. Washington, DC: American Chemical Society; 2004. p 3-20.
    • (2004) Aldo-Keto Reductases and Toxicant Metabolism , pp. 3-20
    • Penning, T.M.1
  • 49
    • 0012058904 scopus 로고    scopus 로고
    • Aldehyde dehydrogenases
    • In: Guengerich FP, (editor), Comprehensive Toxicology, first ed. Elsevier Science, Oxford
    • Petersen D, Lindahl R. Aldehyde dehydrogenases. In: Guengerich FP, (editor). Biotransformation, Vol. 3, Comprehensive Toxicology, first ed. Elsevier Science, Oxford; 1997. p 97-118.
    • (1997) Biotransformation , vol.3 , pp. 97-118
    • Petersen, D.1    Lindahl, R.2
  • 50
    • 0001687899 scopus 로고    scopus 로고
    • Esterases of the a,b hydrolase fold family
    • In: Guengerich FP, editor, Comprehensive Toxicology. first ed. Elsevier Science, Oxford
    • Quinn DM. Esterases of the a,b hydrolase fold family. In: Guengerich FP, editor. Biotransformation, Vol. 3, Comprehensive Toxicology. first ed. Elsevier Science, Oxford; 1997. p 243-264.
    • (1997) Biotransformation , vol.3 , pp. 243-264
    • Quinn, D.M.1
  • 51
    • 4244122702 scopus 로고    scopus 로고
    • Xanthine dehydrogenase and aldehyde oxidase
    • In: Guengerich FP, (editor), Comprehensive Toxicology. first ed. Elsevier Science, Oxford
    • Rajagopalan KV. Xanthine dehydrogenase and aldehyde oxidase. In: Guengerich FP, (editor). Biotransformation, Vol. 3, Comprehensive Toxicology. first ed. Elsevier Science, Oxford; 1997. p 165-178.
    • (1997) Biotransformation , vol.3 , pp. 165-178
    • Rajagopalan, K.V.1
  • 52
    • 0036223831 scopus 로고    scopus 로고
    • Summary of information on human CYP enzymes: human P450 metabolism data
    • Rendic S. Summary of information on human CYP enzymes: human P450 metabolism data. Drug Metab Rev 2002;34:83-448.
    • (2002) Drug Metab Rev , vol.34 , pp. 83-448
    • Rendic, S.1
  • 53
    • 0000028560 scopus 로고    scopus 로고
    • Quinone reductases
    • In: Guengerich FP, (editor), Comprehensive Toxicology, first ed. Elsevier Science, Oxford
    • Ross D. Quinone reductases. In: Guengerich FP, (editor). Biotransformation, Vol. 3, Comprehensive Toxicology, first ed. Elsevier Science, Oxford; 1997. p 179-197.
    • (1997) Biotransformation , vol.3 , pp. 179-197
    • Ross, D.1
  • 55
    • 0027289112 scopus 로고
    • Partitioning between N-dealkylation and N-oxygenation in the oxidation of N,N-dialkylarylamines catalyzed by cytochrome P450 2B1
    • Seto Y, Guengerich FP. Partitioning between N-dealkylation and N-oxygenation in the oxidation of N,N-dialkylarylamines catalyzed by cytochrome P450 2B1. J Biol Chem 1993;268:9986-9997.
    • (1993) J Biol Chem , vol.268 , pp. 9986-9997
    • Seto, Y.1    Guengerich, F.P.2
  • 56
    • 21944432511 scopus 로고    scopus 로고
    • Theoretical perspective on the structure and mechanism of cytochrome P450 enzymes
    • Shaik S, Kumar D, de Visser SP, Altun A, Thiel W. Theoretical perspective on the structure and mechanism of cytochrome P450 enzymes. Chem Rev 2005;105:2279-2328.
    • (2005) Chem Rev , vol.105 , pp. 2279-2328
    • Shaik, S.1    Kumar, D.2    de Visser, S.P.3    Altun, A.4    Thiel, W.5
  • 57
    • 0034704156 scopus 로고    scopus 로고
    • Targeted disruption of soluble epoxide hydrolase reveals a role in blood pressure regulation
    • Sinal CJ, Miyate M, Tohkin M, Nagata K, Bend JR, Gonzalez FJ. Targeted disruption of soluble epoxide hydrolase reveals a role in blood pressure regulation. J Biol Chem 2000;275:40504-40510.
    • (2000) J Biol Chem , vol.275 , pp. 40504-40510
    • Sinal, C.J.1    Miyate, M.2    Tohkin, M.3    Nagata, K.4    Bend, J.R.5    Gonzalez, F.J.6
  • 58
    • 0001051934 scopus 로고    scopus 로고
    • Microsomal amidases and caraboxylesterases
    • In: Guengerich FP, (editor), Comprehensive Toxicology. first ed. Elsevier Science, Oxford
    • Sone T, Wang CY. Microsomal amidases and caraboxylesterases. In: Guengerich FP, (editor). Biotransformation, Vol. 3, Comprehensive Toxicology. first ed. Elsevier Science, Oxford; 1997. p 265-281.
    • (1997) Biotransformation , vol.3 , pp. 265-281
    • Sone, T.1    Wang, C.Y.2
  • 59
    • 0026453420 scopus 로고
    • Regulation of 2,3,7,8-tetrachlorodibenzo-p-dioxininducible expression of aldehyde dehydrogenase in hepatoma cells
    • Takimoto K, Lindahl R, Pitot HC. Regulation of 2,3,7,8-tetrachlorodibenzo-p-dioxininducible expression of aldehyde dehydrogenase in hepatoma cells. Arch Biochem Biophys 1992;298:492-497.
    • (1992) Arch Biochem Biophys , vol.298 , pp. 492-497
    • Takimoto, K.1    Lindahl, R.2    Pitot, H.C.3
  • 60
    • 0029911205 scopus 로고    scopus 로고
    • The catalytic mechanism of microsomal epoxide hydrolase involves reversible formation and rate-limiting hydrolysis of the alkyl-enzyme intermediate
    • Tzeng H-F, Laughlin LT, Lin S, Armstrong RN. The catalytic mechanism of microsomal epoxide hydrolase involves reversible formation and rate-limiting hydrolysis of the alkyl-enzyme intermediate. J Am Chem Soc 1996;118:9436-9437.
    • (1996) J Am Chem Soc , vol.118 , pp. 9436-9437
    • Tzeng, H.-F.1    Laughlin, L.T.2    Lin, S.3    Armstrong, R.N.4
  • 61
    • 0031801211 scopus 로고    scopus 로고
    • A new strategy for the design of monoamine oxidase inactivators. Exploratory studies with tertiary allylic and propargylic amino alcohols
    • Van Houten KA, Kim JM, Bogdan MA, Feni DC, Mariano PS. A new strategy for the design of monoamine oxidase inactivators. Exploratory studies with tertiary allylic and propargylic amino alcohols. J Am Chem Soc 1998;120:5864-5872.
    • (1998) J Am Chem Soc , vol.120 , pp. 5864-5872
    • Van Houten, K.A.1    Kim, J.M.2    Bogdan, M.A.3    Feni, D.C.4    Mariano, P.S.5
  • 62
    • 32444448861 scopus 로고    scopus 로고
    • Analysis and update of the human aldehyde dehydrogenase (ALDH) gene family
    • Vasiliou V, Nebert DW. Analysis and update of the human aldehyde dehydrogenase (ALDH) gene family. Hum Genomic 2005;2:138-143.
    • (2005) Hum Genomic , vol.2 , pp. 138-143
    • Vasiliou, V.1    Nebert, D.W.2
  • 63
    • 6944221357 scopus 로고    scopus 로고
    • Drug-drug interactions for UDP-glucuronosyltransferase substrates: a pharmacokinetic explanation for typically observed low exposure (AUCi/AUC) ratios
    • Williams JA, Hyland R, Jones BC, Smith DA, Hust S, Goosen TC, Peterkin V, Koup JR, Ball SE. Drug-drug interactions for UDP-glucuronosyltransferase substrates: a pharmacokinetic explanation for typically observed low exposure (AUCi/AUC) ratios. Drug Metab Dispos 2004;32:1201-1208.
    • (2004) Drug Metab Dispos , vol.32 , pp. 1201-1208
    • Williams, J.A.1    Hyland, R.2    Jones, B.C.3    Smith, D.A.4    Hust, S.5    Goosen, T.C.6    Peterkin, V.7    Koup, J.R.8    Ball, S.E.9
  • 64
    • 0000126071 scopus 로고
    • Reactions catalyzed by the cytochrome P-450 system
    • In: Jakoby WB, (editor), first ed. New York: Academic Press
    • Wislocki PG, Miwa GT, Lu AYH. Reactions catalyzed by the cytochrome P-450 system. In: Jakoby WB, (editor). Enzymatic Basis of Detoxication, Vol. I. first ed. New York: Academic Press; 1980. p 135-182.
    • (1980) Enzymatic Basis of Detoxication , vol.I , pp. 135-182
    • Wislocki, P.G.1    Miwa, G.T.2    Lu, A.Y.H.3
  • 65
    • 0026750647 scopus 로고
    • The human hepatic cytochromes P450 involved in drug metabolism
    • Wrighton SA, Stevens JC. The human hepatic cytochromes P450 involved in drug metabolism. CRC Crit Rev Toxicol 1992;22:1-21.
    • (1992) CRC Crit Rev Toxicol , vol.22 , pp. 1-21
    • Wrighton, S.A.1    Stevens, J.C.2
  • 66
    • 0027462628 scopus 로고
    • Recent studies on the structure and function of multisubstrate flavincontaining monooxygenases
    • Ziegler DM. Recent studies on the structure and function of multisubstrate flavincontaining monooxygenases. Annu Rev Pharmacol Toxicol 1993;33:179-199.
    • (1993) Annu Rev Pharmacol Toxicol , vol.33 , pp. 179-199
    • Ziegler, D.M.1
  • 67
    • 0015337668 scopus 로고
    • Microsomal oxidase IV: properties of a mixed-function amine oxidase isolated from pig liver microsomes
    • Ziegler DM, Mitchell CH. Microsomal oxidase IV: properties of a mixed-function amine oxidase isolated from pig liver microsomes. Arch Biochem Biophys 1972; 150:116-125.
    • (1972) Arch Biochem Biophys , vol.150 , pp. 116-125
    • Ziegler, D.M.1    Mitchell, C.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.