Combining substrate dynamics, binding statistics, and energy barriers to rationalize regioselective hydroxylation of octane and lauric acid by CYP102A1 and mutants

Hydroxylations of octane and lauric acid by Cytochrome P450-BM3 (CYP102A1) wild-type and three active site mutants—F87A, L188Q/A74G, and F87V/L188Q/A74G—were rationalized using a combination of substrate orientation from docking, substrate binding statistics from molecular dynamics simulations, and...

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Gorde:
Xehetasun bibliografikoak
Egile Nagusiak: Feenstra, K. Anton, Starikov, Eugene B., Urlacher, Vlada B., Commandeur, Jan N.M., Vermeulen, Nico P.E.
Formatua: Artigo
Hizkuntza:Inglês
Argitaratua: Cold Spring Harbor Laboratory Press 2007
Gaiak:
Article
Sarrera elektronikoa:https://ncbi.nlm.nih.gov/pmc/articles/PMC2203314/
https://ncbi.nlm.nih.gov/pubmed/17322527
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.062224407
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