Kosinostatin(KST)contains an uncommon aminopyrrole moiety,whose biosynthesis has remained elusive.Herein,aminopyrrolinic acid,which was generated by an L-ectoine synthase-like enzyme KstB3 via cyclization of L-glutami...Kosinostatin(KST)contains an uncommon aminopyrrole moiety,whose biosynthesis has remained elusive.Herein,aminopyrrolinic acid,which was generated by an L-ectoine synthase-like enzyme KstB3 via cyclization of L-glutamine,was identified to be the real substrate of adenylation enzyme KstB1.Subsequently,a FAD-dependent dehydrogenase KstB4 along with a transglutaminase-like enzyme KstB6 were also involved in formation of aminopyrrole.These results provided an unusual pathway for 2-aminopyrrole formation in KST biosynthesis.展开更多
基金We thank Prof.Zixin Deng's Lab.at Shanghai Jiao Tong University and Dr.Chao Peng of the Mass Spectrometry System at the National Facility for Protein Science in Shanghai(NFPS),Zhangjiang Lab,China for obtaining MS data of proteins.Supporting grants including the National Natural Science Foundation of China(21632007 and 21621002)the Chinese Academy of Sciences(QYZDJ-SSW-SLH037)+1 种基金the Academy of Finland(285971)the Sigrid Juselius Foundation are highly acknowledged.
文摘Kosinostatin(KST)contains an uncommon aminopyrrole moiety,whose biosynthesis has remained elusive.Herein,aminopyrrolinic acid,which was generated by an L-ectoine synthase-like enzyme KstB3 via cyclization of L-glutamine,was identified to be the real substrate of adenylation enzyme KstB1.Subsequently,a FAD-dependent dehydrogenase KstB4 along with a transglutaminase-like enzyme KstB6 were also involved in formation of aminopyrrole.These results provided an unusual pathway for 2-aminopyrrole formation in KST biosynthesis.
