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Volumn 62, Issue 1, 1997, Pages 112-116

Structure of cytochrome P450eryF: Substrate, inhibitors, and model compounds bound in the active site

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450; ERYTHROMYCIN; KETOCONAZOLE;

EID: 0031031676     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0039-128X(96)00168-7     Document Type: Conference Paper
Times cited : (28)

References (17)
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  • 5
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    • Crystal structure of substrate-free Pseudomonas putida cytochrome P-450
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  • 6
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    • High-resolution crystal structure of cytochrome P450cam
    • Poulos TL, Finzel BC, Howard AJ (1987). High-resolution crystal structure of cytochrome P450cam. J Mol Biol 195:687-700.
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    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 7
    • 0026500150 scopus 로고
    • Characterization of saccharopolyspora erythaea cytochrome p450 genes and enzymes, including 6-deoxyerythronolide B hydroxylase
    • Andersen JF, Hutchinson CR (1992). Characterization of Saccharopolyspora erythaea cytochrome P450 genes and enzymes, including 6-deoxyerythronolide B hydroxylase. J Bacteriol 174:725-735.
    • (1992) J Bacteriol , vol.174 , pp. 725-735
    • Andersen, J.F.1    Hutchinson, C.R.2
  • 8
    • 0027996974 scopus 로고
    • Preliminary crystallographic analysis of an enzyme involved in erythromycin biosynthesis: Cytochrome P450eryF
    • Cupp-Vickery JR, Li H, Poulos TL (1994). Preliminary crystallographic analysis of an enzyme involved in erythromycin biosynthesis: cytochrome P450eryF. Proteins 20:197-201.
    • (1994) Proteins , vol.20 , pp. 197-201
    • Cupp-Vickery, J.R.1    Li, H.2    Poulos, T.L.3
  • 9
    • 0029586252 scopus 로고
    • Structure of cytochrome P450eryF involved in erythromycin biosynthesis
    • Cupp-Vickery JR, Poulos TL (1995). Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nature Struct Biol 2:144-153.
    • (1995) Nature Struct Biol , vol.2 , pp. 144-153
    • Cupp-Vickery, J.R.1    Poulos, T.L.2
  • 10
    • 0024569996 scopus 로고
    • Secondary structure prediction of 52 membrane-bound cytochromes P450 shows a strong similarity to P450cam
    • Nelson DR, Strobel HW (1989). Secondary structure prediction of 52 membrane-bound cytochromes P450 shows a strong similarity to P450cam. Biochemistry 28:656-660.
    • (1989) Biochemistry , vol.28 , pp. 656-660
    • Nelson, D.R.1    Strobel, H.W.2
  • 11
    • 0024832753 scopus 로고
    • A conserved residue of P450 involved in heme-oxygen stability and activation
    • Matinis SA, Atkins WM, Stayton PS, Sligar SG (1989). A conserved residue of P450 involved in heme-oxygen stability and activation. J Am Chem Soc 111:9252-9253.
    • (1989) J Am Chem Soc , vol.111 , pp. 9252-9253
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    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7823-7827
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.