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

Fleurdeliz Maglangit; Saad Alrashdi; Justine Renault; Laurent Trembleau; Catherine Victoria; Ming Him Tong; Shan Wang; Kwaku Kyeremeh; Hai Deng

doi:10.1039/d0ob00320d

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

Fleurdeliz Maglangit, Saad Alrashdi, Justine Renault, Laurent Trembleau, Catherine Victoria, Ming Him Tong, Shan Wang, Kwaku Kyeremeh, Hai Deng

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

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.

Original language	English
Pages (from-to)	2219-2222
Number of pages	4
Journal	Organic and Biomolecular Chemistry
Volume	18
Issue number	12
DOIs	https://doi.org/10.1039/d0ob00320d
Publication status	Published - 28 Mar 2020

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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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T1 - Characterization of the promiscuous

T2 - N-Acyl CoA transferase, LgoC, in legonoxamine biosynthesis

AU - Maglangit, Fleurdeliz

AU - Alrashdi, Saad

AU - Renault, Justine

AU - Trembleau, Laurent

AU - Victoria, Catherine

AU - Tong, Ming Him

AU - Wang, Shan

AU - Kyeremeh, Kwaku

AU - Deng, Hai

PY - 2020/3/28

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N2 - 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.

AB - 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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JO - Organic and Biomolecular Chemistry

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

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