p-Nitrophenyl esters provide new insights and applications for the thiolase enzyme OleA.

ABSTRACT: The OleA enzyme is distinct amongst thiolase enzymes in binding two long (≥C₈) acyl chains into structurally-opposed hydrophobic channels, denoted A and B, to carry out a non-decarboxylative Claisen condensation reaction and initiate the biosynthesis of membrane hydrocarbons and β-lactone natural products. OleA has now been identified in hundreds of diverse bacteria via bioinformatics and high-throughput screening using p-nitrophenyl alkanoate esters as surrogate substrates. In the present study, p-nitrophenyl esters were used to probe the reaction mechanism of OleA and shown to be incorporated into Claisen condensation products for the first time. p-Nitrophenyl alkanoate substrates alone were shown not to undergo Claisen condensation, but co-incubation of <

SUBMITTER: Smith MD 

PROVIDER: S-EPMC8180931 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature