title: The substrate specificity of cytochrome P450cam.
abstract: The catalytic turnover of xenobiotics by cytochrome P450cam results in both the formation of organic metabolites and the uncoupled production of H2O2, and H2O. Previous studies have shown that a receptor-constrained three-dimensional screening program (DOCK) can be used to identify potential ligands (ergo substrates) for the enzyme (De Voss, J. J.; Sibbesen, O.; Zhang, Z.; Ortiz de Montellano, P. R. J. Am. Chem. Soc. 1997, 119, 5489). A new set of 10 compounds has now been examined to further test the substrate specificity of P450cam and the ability of DOCK to identify substrates for this enzyme. The results expand the known specificity of P450cam and define limitations in the use of DOCK to predict its substrate specificity.
authors.affiliation: Department of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446, USA.
authors.forename: Z
authors.initials: Z
authors.lastname: Zhang
authors.forename: O
authors.initials: O
authors.lastname: Sibbesen
authors.forename: R A
authors.initials: RA
authors.lastname: Johnson
authors.forename: P R
authors.initials: PR
authors.lastname: Ortiz de Montellano
mesh_terms: D002164:Camphor / Q000378:metabolism; D019475:Camphor 5-Monooxygenase / Q000378:metabolism*; D002384:Catalysis; D006861:Hydrogen Peroxide / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure; D009243:NAD / Q000378:metabolism; D010100:Oxygen / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D011994:Recombinant Proteins; D009243:NAD; D002164:Camphor; D006861:Hydrogen Peroxide; D019475:Camphor 5-Monooxygenase; D010100:Oxygen