메뉴 건너뛰기




Volumn 66, Issue 4, 1998, Pages 217-233

Molecular modelling of steroidogenic cytochromes P450 from families CYP11, CYP17, CYP19 and CYP21 based on the CYP102 crystal structure

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450;

EID: 0031709649     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-0760(98)00032-6     Document Type: Article
Times cited : (61)

References (70)
  • 3
    • 0021189932 scopus 로고
    • The role of Cytochromes P-450 in adrenal steroidogenesis
    • Takemori S. and Kominami S., The role of Cytochromes P-450 in adrenal steroidogenesis. Trends in Biological Sciences 9 (1984) 393-396.
    • (1984) Trends in Biological Sciences , vol.9 , pp. 393-396
    • Takemori, S.1    Kominami, S.2
  • 5
    • 0002270104 scopus 로고
    • Cytochrome P-450 enzymes in sterol biosynthesis and metabolism
    • ed. P.R. Ortiz de Montellano. Plenum, New York
    • Jefcoate, C. R., Cytochrome P-450 enzymes in sterol biosynthesis and metabolism, in: Cytochrome P-450, ed. P.R. Ortiz de Montellano. Plenum, New York, 1986, pp. 387-428.
    • (1986) Cytochrome P-450 , pp. 387-428
    • Jefcoate, C.R.1
  • 7
    • 0027058038 scopus 로고
    • Steroidogenic enzymes: Structure, function and role in regulation of steroid hormone biosynthesis
    • Hanukoglu L., Steroidogenic enzymes: Structure, function and role in regulation of steroid hormone biosynthesis. Journal of Steroid Biochemistry and Molecular Biology 43 (1992) 779-804.
    • (1992) Journal of Steroid Biochemistry and Molecular Biology , vol.43 , pp. 779-804
    • Hanukoglu, L.1
  • 8
    • 0344367354 scopus 로고
    • Aromatase: Function, reaction mechanism and biological significance
    • Tan L., Aromatase: Function, reaction mechanism and biological significance. Frontiers in Biotransformation 6 (1991) 63-113.
    • (1991) Frontiers in Biotransformation , vol.6 , pp. 63-113
    • Tan, L.1
  • 9
    • 0000633429 scopus 로고
    • Regulation of steroidogenic and related P450s
    • ed. P. R. Ortiz de Montellano. Plenum, New York
    • Kagawa, N. and Waterman, M. R., Regulation of steroidogenic and related P450s, in: Cytochrome P450, ed. P. R. Ortiz de Montellano. Plenum, New York, 1995, pp. 419-442.
    • (1995) Cytochrome P450 , pp. 419-442
    • Kagawa, N.1    Waterman, M.R.2
  • 12
  • 18
    • 0344799148 scopus 로고
    • Structure-function analysis of eukaryotic P450s expressed in E coli
    • ed. M. C. Lechner. Libbey, Paris
    • Pikuleva, I. A., Jenkins, C. M. and Waterman, M. R., Structure-function analysis of eukaryotic P450s expressed in E coli, in: Cytochrome P450. 8th International Conference, ed. M. C. Lechner. Libbey, Paris, 1994, pp. 293-297.
    • (1994) Cytochrome P450. 8th International Conference , pp. 293-297
    • Pikuleva, I.A.1    Jenkins, C.M.2    Waterman, M.R.3
  • 23
    • 0026488375 scopus 로고
    • Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding
    • Wada A. and Waterman M. R., Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding. Journal of Biological Chemistry 267 (1992) 22877-22882.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 22877-22882
    • Wada, A.1    Waterman, M.R.2
  • 24
    • 0028794689 scopus 로고
    • Cytochrome P450: Structure, function and generation of reactive oxygen species
    • Bernhardt R., Cytochrome P450: Structure, function and generation of reactive oxygen species. Reviews of Physiology, Biochemistry and Pharmacology 127 (1995) 137-221.
    • (1995) Reviews of Physiology, Biochemistry and Pharmacology , vol.127 , pp. 137-221
    • Bernhardt, R.1
  • 27
    • 0026773548 scopus 로고
    • The cholesterol-side-chain-cleaving cytochrome P450 spin-state equilibrium 1. Thermodynamic analysis
    • Lange R., Larroque C. and Anzenbacher P., The cholesterol-side-chain-cleaving cytochrome P450 spin-state equilibrium 1. Thermodynamic analysis. European Journal of Biochemistry 207 (1992) 69-73.
    • (1992) European Journal of Biochemistry , vol.207 , pp. 69-73
    • Lange, R.1    Larroque, C.2    Anzenbacher, P.3
  • 28
    • 0026654003 scopus 로고
    • The cholesterol-side-chain-cleaving cytochrome P450 spin-state equilibrium 2. Conformational analysis
    • Lange R., Pantaloni A. and Saldana L.-L., The cholesterol-side-chain-cleaving cytochrome P450 spin-state equilibrium 2. Conformational analysis. European Journal of Biochemistry 207 (1992) 75-79.
    • (1992) European Journal of Biochemistry , vol.207 , pp. 75-79
    • Lange, R.1    Pantaloni, A.2    Saldana, L.-L.3
  • 30
    • 0025095684 scopus 로고
    • Inhibitors of the P450 enzymes aromatase and lyase. Crystallographic and molecular modelling studies suggest structural features of pyridylacetic acid derivatives responsible for differences in enzyme inhibitory activity
    • Laughton C. A. and Neidle S., Inhibitors of the P450 enzymes aromatase and lyase. Crystallographic and molecular modelling studies suggest structural features of pyridylacetic acid derivatives responsible for differences in enzyme inhibitory activity. Journal of Medicinal Chemistry 33 (1990) 3055-3060.
    • (1990) Journal of Medicinal Chemistry , vol.33 , pp. 3055-3060
    • Laughton, C.A.1    Neidle, S.2
  • 33
    • 0022997597 scopus 로고
    • 21 side-chain cleavage P450 from porcine adrenal and testicular microsomes
    • 21 side-chain cleavage P450 from porcine adrenal and testicular microsomes. Journal of Biological Chemistry 261 (1986) 8429-8433.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 8429-8433
    • Yanagibashi, K.1    Hall, P.F.2
  • 41
    • 0030159247 scopus 로고    scopus 로고
    • Three-dimensional quantitative structure-activity relationships of steroid aromatase inhibitors
    • Oprea T. I. and Garcia A. E., Three-dimensional quantitative structure-activity relationships of steroid aromatase inhibitors. Journal of Computer-Aided Molecular Design 10 (1996) 186-200.
    • (1996) Journal of Computer-Aided Molecular Design , vol.10 , pp. 186-200
    • Oprea, T.I.1    Garcia, A.E.2
  • 42
    • 0025955439 scopus 로고
    • Structure-fimction relationships of human aromatase cytochrome P-450 using molecular modeling and site-directed mutagenesis
    • Graham-Lorence S., Khalil M. W., Lorence M. C., Mendelson C. R. and Simpson E. R., Structure-fimction relationships of human aromatase cytochrome P-450 using molecular modeling and site-directed mutagenesis. Journal of Biological Chemistry 266 (1991) 11939-11946.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 11939-11946
    • Graham-Lorence, S.1    Khalil, M.W.2    Lorence, M.C.3    Mendelson, C.R.4    Simpson, E.R.5
  • 43
    • 0026685937 scopus 로고
    • Kinetic properties of aromatase mutants Pro308Phe, Asp309Asn, and Asp309Ala and their interactions with aromatase inhibitors
    • Kadohama N., Yarborough C., Zhou D., Chen S. and Osawa Y., Kinetic properties of aromatase mutants Pro308Phe, Asp309Asn, and Asp309Ala and their interactions with aromatase inhibitors. Journal of Steroid Biochemistry and Molecular Biology 43 (1992) 693-700.
    • (1992) Journal of Steroid Biochemistry and Molecular Biology , vol.43 , pp. 693-700
    • Kadohama, N.1    Yarborough, C.2    Zhou, D.3    Chen, S.4    Osawa, Y.5
  • 44
    • 0026592208 scopus 로고
    • Functional domains of aromatase cytochrome P450 inferred from comparative analyses of amino acid sequences and substantiated by site-directed mutagenesis experiments
    • Chen S. and Zhou D., Functional domains of aromatase cytochrome P450 inferred from comparative analyses of amino acid sequences and substantiated by site-directed mutagenesis experiments. Journal of Biological Chemistry 267 (1992) 22587-22594.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 22587-22594
    • Chen, S.1    Zhou, D.2
  • 45
    • 0025965047 scopus 로고
    • Structure-function studies of human aromatase by site-directed mutagenesis: Kinetic properties of mutants Pro-308 → Phe, Tyr361 → Phe, Tyr-361 → Leu and Phe-406 → Arg
    • Zhou D., Pompon D. and Chen S., Structure-function studies of human aromatase by site-directed mutagenesis: Kinetic properties of mutants Pro-308 → Phe, Tyr361 → Phe, Tyr-361 → Leu and Phe-406 → Arg. Proceedings of the National Academy of Sciences USA 88 (1991) 410-414.
    • (1991) Proceedings of the National Academy of Sciences USA , vol.88 , pp. 410-414
    • Zhou, D.1    Pompon, D.2    Chen, S.3
  • 48
    • 0001828104 scopus 로고
    • Aromatase inhibitors: Specific inhibitors of oestrogen biosynthesis
    • eds, D. Berg and M. Plempel. VCH, Weinheim
    • Covey, D. F., Aromatase inhibitors: Specific inhibitors of oestrogen biosynthesis, in: Sterol Biosynthesis Inhibitors, eds, D. Berg and M. Plempel. VCH, Weinheim, 1988, pp. 534-571.
    • (1988) Sterol Biosynthesis Inhibitors , pp. 534-571
    • Covey, D.F.1
  • 49
    • 0342834498 scopus 로고
    • Inhibitors of cytochrome P-450 and possibilities for their therapeutic application
    • Correia M. A. and Ortiz de Montellano P. R., Inhibitors of cytochrome P-450 and possibilities for their therapeutic application. Frontiers in Biotransformation 8 (1993) 74-146.
    • (1993) Frontiers in Biotransformation , vol.8 , pp. 74-146
    • Correia, M.A.1    Ortiz De Montellano, P.R.2
  • 50
    • 0002561458 scopus 로고
    • Inhibition of cytochrome P450 enzymes
    • ed., P. R. Ortiz de Montellano. Plenum, New York
    • Ortiz de Montellano, P. R. and Correia, M. A., Inhibition of cytochrome P450 enzymes, in: Cytochrome P450, ed., P. R. Ortiz de Montellano. Plenum, New York, 1995, pp. 305-364.
    • (1995) Cytochrome P450 , pp. 305-364
    • Ortiz De Montellano, P.R.1    Correia, M.A.2
  • 53
    • 0025887195 scopus 로고
    • Theoretical studies on the mechanism of conversion of androgens to estrogens by aromatase
    • Korzekwa K. R., Trager W. F., Smith S. J., Osawa Y. and Gillette J. R., Theoretical studies on the mechanism of conversion of androgens to estrogens by aromatase. Biochemistry 30 (1991) 6155-6162.
    • (1991) Biochemistry , vol.30 , pp. 6155-6162
    • Korzekwa, K.R.1    Trager, W.F.2    Smith, S.J.3    Osawa, Y.4    Gillette, J.R.5
  • 56
    • 0029056146 scopus 로고
    • A molecular model for the interaction between vorozole and other non-steroidal inhibitors and human cytochrome P450 19 (P450 aromatase)
    • Koymans L. M. H., Moereels H. and Van den Bosche E., A molecular model for the interaction between vorozole and other non-steroidal inhibitors and human cytochrome P450 19 (P450 aromatase). Journal of Steroid Biochemistry and Molecular Biology 53 (1995) 191-197.
    • (1995) Journal of Steroid Biochemistry and Molecular Biology , vol.53 , pp. 191-197
    • Koymans, L.M.H.1    Moereels, H.2    Van Den Bosche, E.3
  • 57
    • 0002751786 scopus 로고
    • Oxygen activation and reactivity
    • ed., P. R. Ortiz de Montellano. Plenum, New York
    • Ortiz de Montellano, P. R., Oxygen activation and reactivity, in: Cytochrome P450, ed., P. R. Ortiz de Montellano. Plenum, New York, 1995, pp. 245-303.
    • (1995) Cytochrome P450 , pp. 245-303
    • Ortiz De Montellano, P.R.1
  • 58
    • 0029948686 scopus 로고    scopus 로고
    • Function and membrane topology of wild-type and mutated cytochrome P450c21
    • Hu M.-C., Hsu L.-C., Hsu N.-C. and Chung B.-C., Function and membrane topology of wild-type and mutated cytochrome P450c21. Biochemical Journal 316 (1996) 325-329.
    • (1996) Biochemical Journal , vol.316 , pp. 325-329
    • Hu, M.-C.1    Hsu, L.-C.2    Hsu, N.-C.3    Chung, B.-C.4
  • 59
    • 0025868941 scopus 로고
    • Expression and functional study of wild-type and mutant human cytochrome P450c21 in Saccharomyces cerevisiae
    • Wii D.-A., Hu M.-C. and Chung B.-C., Expression and functional study of wild-type and mutant human cytochrome P450c21 in Saccharomyces cerevisiae. DNA and Cell Biology 10 (1991) 201-209.
    • (1991) DNA and Cell Biology , vol.10 , pp. 201-209
    • Wii, D.-A.1    Hu, M.-C.2    Chung, B.-C.3
  • 60
    • 0025772912 scopus 로고
    • 268 result in complete, partial, or no loss of enzymatic activity, respectively
    • 268 result in complete, partial, or no loss of enzymatic activity, respectively. Journal of Clinical Investigation 85 (1991) 519-523.
    • (1991) Journal of Clinical Investigation , vol.85 , pp. 519-523
    • Wu, D.-A.1    Chung, B.-C.2
  • 61
    • 0027096408 scopus 로고
    • Dynamic structures of adrenocortical cytochrome P-450 in proteoliposomes and microsomes: Protein rotation study
    • Ohta Y., Kawato S., Tagashira H., Takemori S. and Kominami S., Dynamic structures of adrenocortical cytochrome P-450 in proteoliposomes and microsomes: Protein rotation study. Biochemistry 31 (1992) 12680-12687.
    • (1992) Biochemistry , vol.31 , pp. 12680-12687
    • Ohta, Y.1    Kawato, S.2    Tagashira, H.3    Takemori, S.4    Kominami, S.5
  • 62
    • 0024457089 scopus 로고
    • Design of specific mechanism-based inactivators, of hepatic and adrenal microsomal cytochromes P-450 responsible for progesterone 21-hydroxylation
    • Halpert J. R., Jaw J.-Y. and Johnson E. F., Design of specific mechanism-based inactivators, of hepatic and adrenal microsomal cytochromes P-450 responsible for progesterone 21-hydroxylation. Drug Metabolism Reviews 20 (1989) 645-655.
    • (1989) Drug Metabolism Reviews , vol.20 , pp. 645-655
    • Halpert, J.R.1    Jaw, J.-Y.2    Johnson, E.F.3
  • 63
    • 0029892263 scopus 로고    scopus 로고
    • P450s: Structural similarities and functional differences
    • Graham-Lorence S. and Peterson J. A., P450s: Structural similarities and functional differences. FASEB Journal 10 (1996) 206-214.
    • (1996) FASEB Journal , vol.10 , pp. 206-214
    • Graham-Lorence, S.1    Peterson, J.A.2
  • 64
    • 0027198401 scopus 로고
    • Expression and purification of functional human 17α-hydroxylase/17,20-lyase (P450c17) in Escherichia coli
    • Imai T., Globerman H., Gertner J. M., Kagawa N. and Waterman M. R., Expression and purification of functional human 17α-hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Journal of Biological Chemistry 268 (1993) 19681-19689.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 19681-19689
    • Imai, T.1    Globerman, H.2    Gertner, J.M.3    Kagawa, N.4    Waterman, M.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.