Mutagenesis and redox partners analysis of the P450 fatty acid decarboxylase OleT_JE.

ABSTRACT: The cytochrome P450 enzyme OleT_JE from Jeotgalicoccus sp. ATCC 8456 is capable of converting free long-chain fatty acids into α-alkenes via one-step oxidative decarboxylation in presence of H₂O₂ as cofactor or using redox partner systems. This enzyme has attracted much attention due to its intriguing but unclear catalytic mechanism and potential application in biofuel production. Here, we investigated the functionality of a select group of residues (Arg245, Cys365, His85, and Ile170) in the active site of OleT_JE through extensive mutagenesis analysis. The key roles of these residues for catalytic activity and reaction type selectivity were identified. In addition, a range of heterologous redox partners were found to be able to efficiently support

SUBMITTER: Fang B 

PROVIDER: S-EPMC5343568 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature