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Volumn 29, Issue 4 I, 2001, Pages 368-374

Substrate inhibition kinetics for cytochrome P450-catalyzed reactions

Author keywords

[No Author keywords available]

Indexed keywords

CHLORZOXAZONE; CYTOCHROME P450; DEXTROMETHORPHAN; DIAZEPAM; ESTRONE; ETHOXYRESORUFIN; FLURBIPROFEN; MEPHENYTOIN; PACLITAXEL; PHENACETIN; PROGESTERONE; RECOMBINANT PROTEIN; RESORUFIN DERIVATIVE; TESTOSTERONE;

EID: 0035059509     PISSN: 00909556     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (147)

References (34)
  • 4
    • 0024236331 scopus 로고
    • The molecular biology of cytochrome P450s
    • published erratum appears in Pharmacol Rev (1989) 41:91-92
    • (1988) Pharmacol Rev , vol.40 , pp. 243-288
    • Gonzalez, F.J.1
  • 7
    • 0025298011 scopus 로고
    • Sequence requirements for cytochromes P450IIA1 and P450IIA2 catalytic activity: Evidence for both specific and non-specific substrate binding interactions through use of chimeric cDNAs and cDNA expression
    • (1990) Protein Eng , vol.3 , pp. 571-575
    • Hanioka, N.1    Korzekwa, K.2    Gonzalez, F.J.3
  • 8
    • 0032499691 scopus 로고    scopus 로고
    • Analysis of human cytochrome P450 3A4 cooperativity. Construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6636-6641
    • Harlow, G.R.1    Halpert, J.R.2
  • 9
    • 0027240916 scopus 로고
    • A new kinetic model for the steady-state reactions of the quinoprotein methanol dehydrogenase from Paracoccus denitrificans
    • (1993) Biochemistry , vol.32 , pp. 4362-4368
    • Harris, T.K.1    Davidson, V.L.2
  • 11
    • 0027952717 scopus 로고
    • Excess-substrate inhibition in enzymology and high-dose inhibition in pharmacology: A re-interpretation
    • (1994) Biochem J , vol.298 , pp. 171-180
    • Kuhl, P.W.1
  • 12
    • 0025809265 scopus 로고
    • Enzyme kinetic and inhibition analyses of cytochrome P450XVII, a protein with a bifunctional catalytic site. Quantification of effective substrate concentrations at the active site and their significance for intrinsic control of the hydroxylase/lyase reaction sequence
    • (1991) J Biol Chem , vol.266 , pp. 6291-6301
    • Kuhm-Velten, W.N.1    Bunse, T.2    Forster, M.E.C.3
  • 16
    • 0031046962 scopus 로고    scopus 로고
    • Uncompetitive substrate inhibition and noncompetitive inhibition by 5-N-undecyl-6-hydroxy-4,7-dioxobenzothiale (UHDBT) and 2-N-nony1-4-hydroxyquinoline-N-oxide (NQNO) is observed for the cytochrome bo3 complex: Implications for a Q(H2)-loop proton translocation mechanism
    • (1997) Biochemistry , vol.36 , pp. 894-902
    • Musser, S.M.1    Stowell, M.H.B.2    Lee, H.K.3    Rumbley, J.N.4    Chan, S.I.5
  • 20
    • 0033105118 scopus 로고    scopus 로고
    • Integrated cytochrome P450 reaction phenotyping: Attempting to bridge the gap between cDNA-expressed cytochromes P450 and native human liver microsomes
    • (1999) Biochem Pharmacol , vol.57 , pp. 465-480
    • Rodrigues, A.D.1
  • 22
    • 0028068828 scopus 로고
    • Role of substrate inhibition kinetics in enzymatic chemical oscillations
    • (1994) Biophys J , vol.67 , pp. 1414-1428
    • Shen, P.1    Larter, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.