A hypothetical model for the active site of human cytochrome P4502E1

References

• AMARNEH, B., CORBIN, C. J., PETERSON, J. A., SIMPSON, E. R. and GRAHAM, L. S., 1993, Functional domains of human aromatase cytochrome P450 characterized by linear alignment and site-directed mutagenesis. Molecular Endocrinology, 7, 1617–1624.
   PubMed Web of Science ®Google Scholar
• BERNSTEIN, F. C., KOETZLE, T. F., WILLIAMS, G. J., M EYER, E. J., BRICE, M. D., RODGERS, J. R., KENNARD, O., S HEVIANOUCHI, T. and T ASUMI, M., 1977, The Protein Data Bank: a computer-based archival file for macromolecular structures. Journal of Molecular Biology, 112, 535–542.
   PubMed Web of Science ®Google Scholar
• BOTTNER, B., S CHRAUBER, H. and BERNHARDT, R., 1996, Engineering a mineralocorticoid- to a glucocorticoid- synthesizing cytochrome P450. Journal of Biological Chemistry, 271, 8028–8033.
   PubMed Web of Science ®Google Scholar
• CHOU, P. Y. and FASMAN, G. D., 1978, Prediction of the secondary structure of proteins from their amino acid sequence [Review]. Advances in Enzymology and Related Areas of Molecular Biology, 47, 45–148.
   PubMedGoogle Scholar
• CUPP, V. J. and PouLos, T. L., 1995, Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nature Structural Biology, 2, 144–153.
   PubMedGoogle Scholar
• DAVIS, S. C., Sul, Z., PETERSON, J. A. and ORTIZ DE M ONTELLANO, P. R., 1996, Oxidation of omega-oxo fatty acids by cytochrome P450BM- 3 (CYP102). Archives of Biochemistry and Biophysics, 328, 35–42.
   Google Scholar
• EISENBERG, D., WEISS, R. M. and T ERWILLIGER, T. C., 1984, The hydrophobic moment detects periodicity in protein hydrophobicity. Proceedings of the National Academy of Sciences, USA, 81, 140–144.
   PubMed Web of Science ®Google Scholar
• FENG, D. F. and DOOLITTLE, R. F., 1987, Progressive sequence alignment as a prerequisite to correct phylogenetic trees. Journal of Molecular Evolution, 25, 351–360.
   PubMed Web of Science ®Google Scholar
• FERENCZY, G. G. and MORRIS, G. M., 1989, The active site of cytochrome P-450 nifedipine oxidase: a model-building study. Journal of Molecular Graphics, 7, 206–211.
   PubMedGoogle Scholar
• FUKUDA, T., I MAI, Y., KOMORI, M., NAKAMURA, M., KUSUNOSE, E., SATOUCHI, K. and KUSUNOSE, M., 1993, Replacement of Thr- 303 of P450 2E1 with serine modifies the regioselectivit y of its fatty acid hydroxylase activity. Journal of Biochemistry, 113, 7–12.
   PubMed Web of Science ®Google Scholar
• FURUYA, H, SHEvnzu, T., HIRANO, K., HATANO, M., F UHL, K. Y., RAAG, R. and PouLos, T. L., 1989, Site-directed mutageneses of rat liver cytochrome P-450d : catalytic activity towards benz-phetamine and 7-ethoxycoumarin. Biochemistry, 28, 6848–6857.
   PubMed Web of Science ®Google Scholar
• GARNIER, J., O SGUTHORPE, D. J. and RossoN, B., 1978, Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. Journal of Molecular Biology, 120, 97–120.
   PubMed Web of Science ®Google Scholar
• GONZALEZ, F. J. and NEBERT, D. W., 1990, Evolution of the P450 gene superfamily : animal—plant 'warfare', molecular drive and human genetic differences in drug oxidation [Review]. Trends in Genetics, 6, 182–186.
   PubMed Web of Science ®Google Scholar
• GOTOH, O., 1992, Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. Journal of Biology Chemistry, 267, 83–90.
   PubMed Web of Science ®Google Scholar
• GRAHAM, L. S., AMARNEH, B., WHITE, R. E., PETERSON, J. A. and SIMPSON, E. R., 1995, A three-dimensional model of aromatase cytochrome P450. Protein Science, 4, 1065–1080.
   PubMed Web of Science ®Google Scholar
• GUENGERICH, F. P., 1992, Cytochrome P450: advances and prospects. FASEB Journal, 6, 667–668.
   PubMed Web of Science ®Google Scholar
• GUENGERICH, F. P., Kim, D. H. and IwAsAxi, M., 1991, Role of human cytochrome P-450 IIE1 in the oxidation of many low molecular weight cancer suspects. Chemical Research in Toxicology, 4, 168–179.
   PubMed Web of Science ®Google Scholar
• HASEMANN, C. A., KURUMBAIL, R. G., BODDUPALLI, S. S., PETERSON, J. A. and DEISENHOFER, J., 1995, Structure and function of cytochromes P450: a comparative analysis of three crystal structures. Structure, 3, 41–62.
   PubMed Web of Science ®Google Scholar
• HASEMANN, C. A., RAVICHANDRAN, K. G., PETERSON, J.A. and DEISENHOFER, J., 1994, Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution. Journal of Molecular Biology, 236, 1169–1185.
   PubMed Web of Science ®Google Scholar
• HE, Y. A., BALFOUR, C. A., KEDZIE, K. M. and H ALPERT, J. R., 1992, Role of residue 478 as a determinant of the substrate specificity of cytochrome P450 2B1. Biochemistry, 31, 9220–9226.
   PubMed Web of Science ®Google Scholar
• HSU, L. C., Hsu, N. C., GUZOVA, J. A., Guzov, V. M., CHANG, S. F. and CHUNG, B. C., 1996, The common I172N mutation causes conformational change of cytochrome P450c21 revealed by systematic mutation, kinetic, and structural studies. Journal of Biological Chemistry, 271, 3306–3310.
   Google Scholar
• I BEANU G. C., GHANAYEM, B. I., LINKO, P., LI, L., PEDERSON, L. G. and GOLDSTEIN, J. A., 1996, Identification of residues 99, 220, and 221 of human cytochrome P450 2C19 as key determinants of omeprazole activity. Journal of Biological Chemistry, 271, 12496–12501.
   Google Scholar
• KOOP, D. R., 1992, Oxidative and reductive metabolism by cytochrome P450 2E1. FASEB Journal, 6, 724–730.
   PubMed Web of Science ®Google Scholar
• KOYMANS, L., DONNE, OP, D. K. G., K OPPELE, T. J. and VERMEULEN, N. P., 1993, Cytochromes P450: their active-site structure and mechanism of oxidation [Review]. Drug Metabolism Reviews, 25, 325–387.
   Google Scholar
• KRONBACH, T., KEMPER, B. and JOHNSON, E. F., 1991, A hypervariable region of P4501105 confers progesterone 21-hydroxylase activity to P45011C1. Biochemistry, 30, 6097–6102.
   PubMed Web of Science ®Google Scholar
• LEWIS, D. F. V., 1995, Molecular modelling of mammalian cytochrome P450. In Cytochromes P450 : Metabolic and Toxicological Aspects, edited by C. Ioannides (Boca Raton: CRC Press).
   Google Scholar
• LINDBERG, R. L. and NEGISHI, M., 1989, Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residue. Nature, 339, 632–634.
   PubMed Web of Science ®Google Scholar
• MACKMAN, R., Guo, Z., GUENGERICH, F. P. and ORTIZ DE M ONTELLANO, P. R., 1996, Active site topology of human cytochrome P450 2E1. Chemical Research in Toxicology, 9,223–226.
   Google Scholar
• NEGISHI, M., UNo, T., D ARDEN, T. A., SUEYOSHI, T. and PEDERSEN, L. G., 1996, Structural flexibility and functional versatility of mammalian P450 enzymes [Review], FASEB Journal, 10, 683–689.
   Google Scholar
• NELSON, D. R., K AMATAKI, T., WAXMAN, D. J., GUENGERICH, F. P., ESTABROOK, R. W., FEYEREISEN, R., GONZALEZ, F. J., CooN, M. J., GUNSALUS I. C., GOTOH, O. and 1993, The P450 superfamily : update on new sequences, gene mapping, accession numbers, early trivial names of enzymes, and nomenclature [Review]. DNA and Cell Biology, 12, 1–51.
   Google Scholar