Hydroxylation Regiochemistry Is Robust to Active Site Mutations in Cytochrome P450cam (CYP101A1).
Sign Up to like & getrecommendations! Published in 2022 at "Biochemistry"
DOI: 10.1021/acs.biochem.2c00233
Abstract: Cytochrome P450cam (CYP101A1) catalyzes the hydroxylation of d-camphor by molecular oxygen. The enzyme-catalyzed hydroxylation exhibits a high degree of regioselectivity and stereoselectivity, with a single major product, d-5-exo-hydroxycamphor, suggesting that the substrate is oriented to… read more here.
Keywords: p450cam cyp101a1; hydroxylation; active site; site ... See more keywords
Conformational Heterogeneity and the Affinity of Substrate Molecular Recognition by Cytochrome P450cam.
Sign Up to like & getrecommendations! Published in 2017 at "Biochemistry"
DOI: 10.1021/acs.biochem.7b00238
Abstract: The broad and variable substrate specificity of cytochrome P450 enzymes makes them a model system for studying the determinants of protein molecular recognition. The archetypal cytochrome P450cam (P450cam) is a relatively specific P450, a feature… read more here.
Keywords: recognition; spectroscopy; molecular recognition; conformational heterogeneity ... See more keywords