Journal
NATURE CHEMICAL BIOLOGY
Volume 12, Issue 11, Pages 967-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.2181
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Funding
- Japan Society for the Promotion of Science (KAKENHI) [24228001]
- Japan Foundation for Applied Enzymology
- Grants-in-Aid for Scientific Research [15K14714] Funding Source: KAKEN
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Amino-group carrier proteins (AmCPs) mediate the biosynthesis of lysine and arginine in some bacteria and archaea. Here we demonstrate that an uncharacterized AmCP-mediated biosynthetic system functions to biosynthesize the previously uncharacterized and nonproteinogenic amino acid (2S,6R)-diamino-(5R,7)-dihydroxy-heptanoic acid (DADH) in Streptomyces sp. SANK 60404. DADH is incorporated into a novel peptide metabolite, vazabitide A, featuring an azabicyclo-ring structure, by nonribosomal peptide synthetases and successive modification enzymes in this bacterium. As the AmCP-mediated machinery for DADH biosynthesis is widely distributed in bacteria, further analysis of uncharacterized AmCP-containing gene clusters will lead to the discovery of novel bioactive compounds and novel biosynthetic enzymes.
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