Active site mechanics of liver microsomal cytochrome P-450☆
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Drug metabolism in drug discovery and development
2018, Acta Pharmaceutica Sinica BCitation Excerpt :Whereas the structure–metabolism relationship of drugs involving CYPs is complex and not completely understood, it is generally accepted that major drug-metabolizing CYP enzymes, e.g., CYP3A, have a large active site and prefer lipophilic substrates. The binding and orientation of a substrate are often determined by hydrophobic and steric interactions of the substrate with the specific amino acids at the active site of a CYP enzyme, although infrequently substrates interact with CYP via hydrogen bonding or ionic interactions5,12–16. These hydrophobic and steric interactions mainly depend on the lipophilicity (e.g, logP) and steric structures of the substrates17,18.
Structural determinants of cytochrome P450 substrate specificity, binding affinity and catalytic rate
1998, Chemico-Biological InteractionsThe substrate specificity of cytochrome P450(cam)
1998, Bioorganic and Medicinal ChemistryCytochrome P450(cam) substrate specificity: Relationship between structure and catalytic oxidation of alkylbenzenes
1998, Archives of Biochemistry and BiophysicsThe steric course of enzymic hydroxylation at primary carbon atoms
1998, Tetrahedron
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This research was supported by Research Grants GM28737 and ESO3600 from the United States Public Health Service and by the University of Connecticut Research Foundation. A preliminary report of part of this article has been presented (1).