Ontology highlight
ABSTRACT:
SUBMITTER: Schleinkofer K
PROVIDER: S-EPMC1369091 | biostudies-literature | 2005 Jun
REPOSITORIES: biostudies-literature
Schleinkofer Karin K Sudarko Winn Peter J PJ Lüdemann Susanne K SK Wade Rebecca C RC
EMBO reports 20050601 6
Understanding substrate binding and product release in cytochrome P450 (CYP) enzymes is important for explaining their key role in drug metabolism, toxicity, xenobiotic degradation and biosynthesis. Here, molecular simulations of substrate and product exit from the buried active site of a mammalian P450, the microsomal CYP2C5, identified a dominant exit channel, termed pathway (pw) 2c. Previous simulations with soluble bacterial P450s showed a different dominant egress channel, pw2a. Combining t ...[more]