THE ROLE OF PROTEIN PLASTICITY IN COMPUTATIONAL RATIONALIZATION STUDIES ON REGIOSELECTIVITY IN TESTOSTERONE HYDROXYLATION BY CYTOCHROME P450 BM3 MUTANTS Adapted from: The role of protein plasticity in computational rationalization studies on regioselectivity in testosterone hydroxylation by Cytochrome P450 BM3 mutants
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Role of Residue 87 in Substrate- and Regioselectivity of Drug Metabolizing Cytochrome P450 Bm3 M11
BM3, originating from Bacillus megaterium, is a highly active enzyme which has attracted much attention because of its potential applicability as a biocatalyst for oxidative reactions. Previously we developed a drug metabolizing mutant BM3 M11 by a combination of site-directed and random mutagenesis. BM3 M11 contains ten mutations, when compared to wild-type BM3 and is able to produce human-rel...
متن کاملAnalysis of the oxidation of short chain alkynes by flavocytochrome P450 BM3.
Bacillus megaterium flavocytochrome P450 BM3 (BM3) is a high activity fatty acid hydroxylase, formed by the fusion of soluble cytochrome P450 and cytochrome P450 reductase modules. Short chain (C6, C8) alkynes were shown to be substrates for BM3, with productive outcomes (i.e. alkyne hydroxylation) dependent on position of the carbon-carbon triple bond in the molecule. Wild-type P450 BM3 cataly...
متن کاملProbing Steroidal Substrate Specificity of Cytochrome P450 BM3 Variants.
M01A82W, M11A82W and M01A82WS72I are three cytochrome P450 BM3 (CYP102A1) variants. They can catalyze the hydroxylation of testosterone (TES) and norethisterone at different positions, thereby making them promising biocatalysts for steroid hydroxylation. With the aim of obtaining more hydroxylated steroid precursors it is necessary to probe the steroidal substrate diversity of these BM3 variant...
متن کاملSteroids hydroxylation catalyzed by the monooxygenase mutant 139-3 from Bacillus megaterium BM3
The search of new substrates with pharmaceutical and industrial potential for biocatalysts including cytochrome P450 enzymes is always challenging. Cytochrome P450 BM3 mutant 139-3, a versatile biocatalyst, exhibited hydroxylation activities towards fatty acids and alkanes. However, there were limited reports about its hydroxylation activity towards steroids. Herein, an Escherichia coli-based w...
متن کاملGeneration of the human metabolite piceatannol from the anticancer-preventive agent resveratrol by bacterial cytochrome P450 BM3.
In recent studies, the wild-type and mutant forms of cytochrome P450 (P450) BM3 (CYP102A1) from Bacillus megaterium were found to metabolize various drugs through reactions similar to those catalyzed by human P450 enzymes. Therefore, it was suggested that CYP102A1 can be used to produce large quantities of the metabolites of human P450-catalyzed reactions. trans-Resveratrol (3,4',5-trihydroxyst...
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تاریخ انتشار 2012