|
type |
Journal Article |
authors |
Wang M., Chen D, Zhao Q, Liu W |
title |
Isolation, Structure Elucidation, and Biosynthesis of a Cysteate-Containing Nonribosomal Peptide in Streptomyces lincolnensis
|
journal |
J Org Chem |
Activity |
2.5.1.76 |
Family |
2.5.1.76 |
sel |
selected |
ui |
29557172 |
year |
(2018) |
volume |
83 |
number |
13 |
pages |
7102-7108 |
| |
abstract |
The species Streptomyces lincolnensis is known as a producer of lincomycin A, a clinically important lincosamide antibiotic with activity against Gram-positive bacteria. Here, we report that S. lincolnensis produces a new cysteate-containing lactone product, cysteoamide (1), which arises from nonribosomal peptide synthetase-programmed sequential assembly of the monomers phenylacetic acid, valine, cysteate, threonine, β-hydroxyleucine, and β-alanine and subsequent intramolecular cyclization to form a lactone ring. The structure of 1 was determined by combined analysis of NMR and MS spectra, while the amino acid absolute configurations in 1 were assigned by Marfey's analysis following acid hydrolysis. The biosynthetic gene cluster of 1 was defined in the genome of S. lincolnensis by bioinformatics analysis and in vivo genetic study. In addition, in vitro assay revealed that OrfA, a pyridoxal 5'-phosphate-dependent protein, is responsible for the formation of the unusual cysteate unit. Cysteate-containing nonribosomal peptides appear to be widely present in various Streptomyces strains, and this study generates interest in their intrinsic functions that remain poorly understood.
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last changed |
2018/07/09 13:47 |
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