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Click-Chemistry Based Fluorometric Assay for Apolipoprotein N-acyltransferase from Enzyme Characterization to High-Throughput Screening
Published on: May 13, 2020
Characterization of the promiscuous N-acyl CoA transferase, LgoC, in legonoxamine biosynthesis
Fleurdeliz Maglangit1, Saad Alrashdi2, Justine Renault3
1Marine Biodiscovery Centre, Department of Chemistry, University of Aberdeen, Meston Walk, Old Aberdeen, Aberdeen AB24 3UE, Scotland, UK. h.deng@abdn.ac.uk and Department of Biology and Environmental Science, College of Science, University of the Philippines Cebu, Lahug, Cebu City, 6000, Philippines. ffmaglangit@up.edu.ph.
Abstract:
More than 500 siderophores are known to date, but only three were identified to be aryl-containing hydroxamate siderophores, legonoxamines A and B from Streptomyces sp. MA37, and aryl ferrioxamine 2 from Micrococcus luteus KLE1011. Siderophores are produced by microorganisms to scavenge iron from the environment, thereby making this essential metal nutrient available to the microbe. We demonstrate here that LgoC from MA37 is responsible for the key aryl-hydroxamate forming step in legonoxamine biosynthesis. Biochemical characterization established that LgoC displays considerable promiscuity for the acylation between N-hydroxy-cadaverine and SNAC (N-acetylcysteamines) thioester derivatives.
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