Insights into ?-ketoacyl-chain recognition for ?-ketoacyl-ACP utilizing AHL synthases.

ABSTRACT: Beta-ketoacyl-ACP utilizing enzymes in fatty acid, polyketide and acyl-homoserine lactone biosynthetic pathways are important targets for developing antimicrobial, anticancer and antiparasitic compounds. Published reports on successful isolation of beta-ketoacyl-ACPs in a laboratory remain scarce to date and thus most beta-ketoacyl-ACP utilizing enzymes are routinely characterized using small molecule substrates in lieu of the bonafide 3-oxoacyl-ACPs. We report the systematic investigation into the electronic, geometric and spatial aspects of beta-ketoacyl-chain recognition to develop 3-oxoacyl-ACP substrate mimics for two beta-ketoacyl-ACP utilizing quorum signal synthases.

SUBMITTER: Nhu Lam M 

PROVIDER: S-EPMC6124316 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature