메뉴 건너뛰기




Volumn 1543, Issue 2, 2000, Pages 383-407

Protein engineering of cytochromes P-450

Author keywords

Chimeragenesis; Electron transfer; Genetic fusion; P 450; Protein engineering; Substrate specificity

Indexed keywords

CYTOCHROME B5; CYTOCHROME P450; CYTOCHROME P450 3A; CYTOCHROME P450 ISOENZYME; CYTOCHROME P450 REDUCTASE; LACTATE DEHYDROGENASE (CYTOCHROME); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

EID: 0034731474     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00236-3     Document Type: Review
Times cited : (64)

References (153)
  • 3
    • 0000350777 scopus 로고
    • Twenty-five years of P450cam research
    • Ortiz de Montellano (Ed.), Cytochrome P450: Structure, Mechanism and Biochemistry, New York: Plenum Press; Ch. 3
    • (1995) , pp. 473-535
    • Mueller, E.J.1    Loida, P.J.2    Sligar, S.G.3
  • 19
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • (1992) J. Biol. Chem. , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 34
    • 0034723195 scopus 로고    scopus 로고
    • Engineering microsomal P-450 2C5 to be a soluble, monomeric enzyme: Mutations that alter aggregation, phospholipid dependence of catalysis, and membrane binding
    • (2000) J. Biol. Chem. , vol.275 , pp. 2545-2553
    • Cosme, J.1    Johnson, E.F.2
  • 46
    • 0002888510 scopus 로고
    • Human cytochrome P450 enzymes
    • Ortiz de Montellano (Ed.), Cytochrome P450: Structure, Mechanism and Biochemistry, New York: Plenum Press; Ch. 14
    • (1995) , pp. 473-535
    • Guengerich, F.P.1
  • 49
    • 0002769936 scopus 로고    scopus 로고
    • J.G. Hardman, L.E. Limbird, P.B. Molinoff, R.W. Ruddon, A.D. Gilman (Eds.), Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th edn., McGraw-Hill, New York
    • Benet, L.Z.1    Kroetz, D.L.2    Sheiner, L.B.3
  • 54
    • 0032499691 scopus 로고    scopus 로고
    • Analysis of human cytochrome P450 3A4 cooperativity: Construction and characterisation 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
  • 76
    • 0030456054 scopus 로고    scopus 로고
    • Interaction of sulfaphenazole derivatives with human liver cytochromes P450 2C: Molecular origin of the specificity inhibitory effects of sulfaphenazole on CYP2C9 and consequences for the substrate binding site topology of CYP2C9
    • (1996) Biochemistry , vol.35 , pp. 16205-16212
    • Mancy, A.1    Dijols, S.2    Poli, S.3    Guengerich, F.P.4    Mansuy, D.5
  • 81
    • 0028052268 scopus 로고
    • Random chimeragenesis of G-protein-coupled receptors-mapping the affinity of the cAMP chemoattractant receptors in Dictyostelium
    • (1994) J. Biol. Chem. , vol.269 , pp. 28724-28731
    • Kim, J.-Y.1    Devreotes, P.N.2
  • 91
    • 0033554399 scopus 로고    scopus 로고
    • Substitutions in the C-terminal portion of the catalytic domain partially reverse assembly defects introduced by mutations in the N-terminal linker sequence of cytochrome P450 2C2
    • (1999) Biochemistry , vol.38 , pp. 12180-12186
    • Doray, B.1    Chen, C.D.2    Kemper, B.3
  • 94
    • 0032574756 scopus 로고    scopus 로고
    • NADPH-flavodoxin reductase and flavodoxin from Escherichia coli: Characteristics as a soluble microsomal P450 reductase
    • (1998) Biochemistry , vol.37 , pp. 6106-6113
    • Jenkins, C.M.1    Waterman, M.R.2
  • 102
    • 0018800750 scopus 로고
    • Adrenodoxin reductase-adrenodoxin complex: Flavin to iron-sulfur electron transfer as the rate-limiting step in the NADPH-cytochrome c reductase reaction
    • (1979) J. Biol. Chem. , vol.254 , pp. 2766-2774
    • Lambeth, J.D.1    Kamin, H.2
  • 103
    • 0022273753 scopus 로고
    • Cytochrome P-450scc-adrenodoxin interactions: Ionic effects on binding, and regulation of cytochrome reduction by bound steroid substrates
    • (1985) J. Biol. Chem. , vol.260 , pp. 8810-8816
    • Lambeth, J.D.1    Kriensiri, S.2
  • 105
    • 0018563695 scopus 로고
    • The formation of binary and ternary complexes of cytochrome P450 scc with adrenodoxin and adrenodoxin reductase-adrenodoxin complex
    • (1979) J. Biol. Chem. , vol.254 , pp. 11806-11815
    • Kido, T.1    Kimura, T.2
  • 108
    • 0026442895 scopus 로고
    • Genetic variants in the putidaredoxin-cytochrome P450 cam electron transfer complex: Identification of the residue responsible for redox-state-dependent conformers
    • (1992) Biochemistry , vol.31 , pp. 11383-11389
    • Davies, M.D.1    Sligar, S.G.2
  • 119
  • 122
    • 0023654954 scopus 로고
    • Identification and characterisation of two functional domains in cytochrome P450 BM3, a catalytically self-sufficient monooxygenase induced by barbiturates in Bacillus megaterium
    • (1987) J. Biol. Chem. , vol.262 , pp. 6683-6690
    • Narhi, L.O.1    Fulco, A.J.2
  • 140
    • 0029884802 scopus 로고    scopus 로고
    • Construction of a human cytochrome P4501A1: RatNADPH-cytochrome P450 reductase fusion cDNA and expression in Escherichia coli, purification and catalytic properties of the enzyme in bacterial cells and after purification
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 48-58
    • Chun, Y.-J.1    Shimada, T.2    Guengerich, F.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.