Biotechnology Research Center, The University of Tokyo, Tokyo, Japan.
Chemical Biology Research Group, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Nat Chem Biol. 2016 Nov;12(11):967-972. doi: 10.1038/nchembio.2181. Epub 2016 Sep 26.
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.
氨基载体蛋白（AmCPs）在一些细菌和古菌中介导赖氨酸和精氨酸的生物合成。在这里，我们证明了一个未被表征的 AmCP 介导的生物合成系统在链霉菌 SANK 60404 中发挥作用，以生物合成以前未被表征的非蛋白质氨基酸（2S，6R）-二氨基-（5R，7）-二羟基-庚酸（DADH）。DADH 被非核糖体肽合成酶和该细菌中的连续修饰酶掺入到具有氮杂双环结构的新型肽代谢物 vazabitide A 中。由于 DADH 生物合成的 AmCP 介导机制在细菌中广泛分布，对未被表征的含有 AmCP 的基因簇的进一步分析将导致发现新型生物活性化合物和新型生物合成酶。
