Title of article
The substrate specificity of cytochrome P450cam Original Research Article
Author/Authors
Zhoupeng Zhang، نويسنده , , Ole Sibbesen، نويسنده , , Roy A Johnson، نويسنده , , Paul R. Ortiz de Montellano، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 1998
Pages
8
From page
1501
To page
1508
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.
Keywords
DOCK , Cytochrome P450 , P450 uncoupling , substrate specificity , Molecular modeling
Journal title
Bioorganic and Medicinal Chemistry
Serial Year
1998
Journal title
Bioorganic and Medicinal Chemistry
Record number
1301680
Link To Document