Insights into β-ketoacyl-chain recognition for β-ketoacyl-ACP utilizing AHL synthases
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.
Nhu Lam, Mila,Dudekula, Dastagiri,Durham, Bri,Collingwood, Noah,Brown, Eric C.,Nagarajan, Rajesh
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p. 8838 - 8841
(2018/08/17)
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