Methylene Oxidation of Alkyl Sulfates by Cytochrome P450_BM-3 and a Role for Conformational Selection in Substrate Recognition.

ABSTRACT: Cytochrome P450_BM-3 (P450_BM-3) is a flavoprotein reductase-heme fusion protein from the bacterium Bacillus megaterium that has been well-characterized in many biophysical aspects. Although the enzyme is known to catalyze the hydroxylation of medium and long-chain fatty acids at high rates, no definitive physiological function has been associated with this process in the organism other than a possible protective role. We found that P450_BM-3 rapidly hydroxylates alkyl sulfates, particularly those with 12-16 carbons (i.e., including dodecyl sulfate) in a similar manner to the fatty acids. The products were characterized as primarily ω-1 hydroxylated alkyl sulfates (plus some ω-2 and ω-3 hydroxylation products), and some further oxid

SUBMITTER: Guengerich FP 

PROVIDER: S-EPMC8317952 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature