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2篇 您的检索式:作者名="Changbiao Chi"
    题名 作者 年代 出处 被引量
1Functional Characterization and Crystal Structure of the Type Ei Peptidyl Carrier Protein ColAia in Collismydns Biosynthesis显示文摘Summary of main observation and conclusion Collismycins(COLs)are antibiotics characterized by a 2,2'-bipyridine(2,2'-BP)core composed of a tri­substituted ring A and an unmodified ring B.The 2,2'-BP core,which possesses metal-chelating ability and plays key roles in various biological activities of COLs,is biosynthesized by a nonribosomal peptide synthetase(NRPS)-polyketide synthase(PKS)hybrid machinery.The starter module of the NRPS-PKS hybrid machinery consists of a type II peptidyl carrier protein(PCP)ColA1a and an adenylation protein ColA1b.We here report the functional characteri­zation of ColAia and ColAlb in vitro,confirming their functions in selection and loading of picolinic acid(PA),instead of normal amino acid substrates,as the origin of ring B in COLs.The 2.1 A crystal structure of ColAia was solved,revealing structural features including the additional helices ala,alb and missing helix a3,which may reflect unique interactions of ColAia with other NRPS-PKS proteins/domains or substrate.Primary and tertiary structural comparison of ColAia with other PCPs revealed the structural basis for their typical a-helical bundle,providing a better understanding of the structural flexibility of PCPs.These results facilitate the starter module engineering for the generation of COL derivatives with ring B modifications in the future.Xueyang Ma Guiyang Wang Tan Liu Changbiao Chi Zhongyi Zhang Donghui Yang Wen Liu Ming Ma 2020Chinese Journal of Chemistry2020,38,9:1
2Enzymatic Synthesis of a Diastereomer of Neoabyssomicin Derivative Using the Diels-Alderase AbyU显示文摘Main observation and conclusion The enzyme AbyU catalyses a Diels-Alder(DA)reaction during abyssomicin C biosynthesis.In this study,AbyU is shown to convert the native substrate of another Diels-Alderase(DAase),AbmU,to a new abyssomicin derivative,abyssomicin 7.Wenjuan Ding Changbiao Chi Xiaoyi Wei Changli Sun Jiajia Tu Ming Ma Qinglian Li Jianhua Ju 2021Chinese Journal of Chemistry2021,39,7:0
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