Issue 12, 2020

Characterization of the promiscuous N-acyl CoA transferase, LgoC, in legonoxamine biosynthesis

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.

Graphical abstract: Characterization of the promiscuous N-acyl CoA transferase, LgoC, in legonoxamine biosynthesis

Supplementary files

Article information

Article type
Communication
Submitted
13 Feb 2020
Accepted
04 Mar 2020
First published
04 Mar 2020

Org. Biomol. Chem., 2020,18, 2219-2222

Characterization of the promiscuous N-acyl CoA transferase, LgoC, in legonoxamine biosynthesis

F. Maglangit, S. Alrashdi, J. Renault, L. Trembleau, C. Victoria, M. H. Tong, S. Wang, K. Kyeremeh and H. Deng, Org. Biomol. Chem., 2020, 18, 2219 DOI: 10.1039/D0OB00320D

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