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

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


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 languageEnglish
Pages (from-to)2219-2222
Number of pages4
JournalOrganic & Biomolecular Chemistry
Issue number12
Early online date4 Mar 2020
Publication statusPublished - 28 Mar 2020

Bibliographical note

FM thanks the University of the Philippines for the Faculty, Reps and Staff Development Program (FRAS DP) for the PhD grant fellowship. SA is grateful to the College of Science and Arts, Jouf University, King Khaled Road, Kingdom of Saudi Arabia and the Royal Embassy of Saudi Arabia Cultural Bureau in the UK for the PhD scholarship. HD is grateful to the Leverhulme Trust Research Project (RPG-2014-418). CV is thankful for the Erasmus scholarship. HD and KK acknowledge the financial supports from the Leverhulme Trust-Royal Society Africa award (AA090088) and the UK Medical Research Council-UK Department for International Development (MRC/DFID) Concordat agreement African Research Leaders Award (MR/S00520X/1).




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