Isolation and structure determination of new siderophore albachelin from Amycolatopsis alba
- 647 Downloads
A new siderophore named albachelin was isolated from iron deficient culture of Amycolatopsis alba. The planar structure of albachelin was elucidated by the combination of ESI–MS/MS experiment and NMR spectroscopic analyses of the gallium (III) complex. The structure of albachelin was determined to be a linear peptide consisting of 6 mol of amino acids including 3 mol of serine, one mol each of N-α-acethyl-N-δ-hydroxy-N-δ-formylornithine, N-α-methyl-N-δ-hydroxyornithine, and cyclic N-hydroxyornithine. The stereochemistries of amino acids constituting albachelin were analyzed by applying modified Marfey method to the hydrolysate of albachelin. Based on bioinformatics, we deduced and discussed the possible biosynthetic gene cluster involved in albachelin biosynthesis from the genome sequence of A. alba. By prediction of substrates for adenylation domains, a non-ribosomal peptide biosynthetase gene (AMYAL_RS0130210) was proposed to be the main biosynthetic gene for albachelin biosynthesis. The related genes including transporter for siderophore were found near the NRPS gene as a gene cluster.
KeywordsSiderophore Amycolatopsis alba Peptide Biosynthesis
This study was supported by the Japan Society for the Promotion of Science by Grants-in-aids (Grant Number 25350964).
Conflict of interest
The authors had no conflict of interest in undertaking this project.
- Lazos O, Tosin M, Slusarczyk AL, Boakes S, Cortes J, Sidebottom PJ, Leadlay PF (2010) Biosynthesis of the putative siderophore erythrochelin requires unprecedented crosstalk between separate nonribosomal peptide gene clusters. Chem Biol 17:160–173. doi: 10.1016/j.chembiol.2010.01.011 CrossRefPubMedGoogle Scholar