Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 46, Pages 16324-16326Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja106571g
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Funding
- NIH of USA [CA094426]
- NNSF [20832009, 30525001, 20921091]
- MST [2009ZX09501-008]
- 973 program [2010CB833200]
- CAS [KJCX2-YW-H08, KSCX2-YW-G-06]
- STCSM of China [09QH1402700]
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The carboxyl-terminal amide group has been often found in many bioactive peptide natural products, including nosiheptide belonging to the over 80 entity-containing thiopeptide family. Upon functional characterization of a novel protein NosA in nosiheptide biosynthesis, herein we report an unusual C-terminal amide forming strategy in general for maturating certain amide-terminated thiopeptides by processing their precursor peptides featuring a serine extension. NosA acts on an intermediate bearing a bis-dehydroalanine tail and catalyzes an enamide dealkylation to remove the acrylate unit originating from the extended serine residue.
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