中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Characterizing Amosamine Biosynthesis in Amicetin Reveals AmiG as a Reversible Retaining Glycosyltransferase

文献类型:期刊论文

作者[Chen, Ruidong ; Zhang, Haibo ; Li, Sumei ; Zhang, Guangtao ; Zhu, Yiguang ; Zhang, Changsheng] Chinese Acad Sci, South China Sea Inst Oceanol, Guangdong Key Lab Marine Mat Med, CAS Key Lab Trop Marine Bioresources & Ecol,RNAM, Guangzhou 510301, Guangdong, Peoples R China ; [Chen, Ruidong] Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China ; [Zhang, Gaiyun] State Ocean Adm, Inst Oceanog 3, Key Lab Marine Biogenet Resources, Xiamen 361005, Peoples R China ; [Liu, Jinsong] Chinese Acad Sci, Guangzhou Inst Biomed & Hlth, State Key Lab Resp Dis, Guangzhou 510530, Guangdong, Peoples R China
刊名JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
出版日期2013
卷号135期号:33页码:12152-12155
ISSN号0002-7863
通讯作者czhang2006@gmail.com
中文摘要The antibacterial and antiviral agent amicetin is a disaccharide nucleoside antibiotic featuring a unique alpha-(1 -> 4)-glycoside bond between amosamine and amicetose, characteristic of a retaining glycosylation. In this study, two key steps for amosamine biosynthesis were investigated: the N-methyltransferase AmiH was demonstrated to be requisite for the dimethylation in amosamine, and the glycosyltransferase AmiG was shown to be necessary for amosaminylation. Biochemical and kinetic characterization of AmiG revealed for the first time the catalytic reversibility of a retaining glycosyltransferase involved in secondary metabolite biosynthesis. AmiG displayed substrate flexibility by utilizing five additional sugar nucleotides as surrogate donors. AmiG was also amenable to sugar and aglycon exchange reactions. This study indicates that AmiG is a potential catalyst for diversifying nucleoside antibiotics and paves the way for mechanistic studies of a natural-product retaining glycosyltransferase.
学科主题Chemistry, Multidisciplinary
资助信息Financial support was provided in part by NNSFC (31125001, 31170708, 30870060), MOST (2010CB833805), and CAS (KZCX2-YW-JC202, KSCX2-EW-G-12). C.Z. is a scholar of the "100 Talents Project" of CAS (08SL111002). We are grateful for the analytical facilities at SCSIO.
原文出处AMER CHEMICAL SOC
语种英语
WOS记录号WOS:000323536100001
公开日期2015-01-22
源URL[http://ir.scsio.ac.cn/handle/344004/10994]  
专题南海海洋研究所_中科院海洋生物资源可持续利用重点实验室
推荐引用方式
GB/T 7714
[Chen, Ruidong,Zhang, Haibo,Li, Sumei,et al. Characterizing Amosamine Biosynthesis in Amicetin Reveals AmiG as a Reversible Retaining Glycosyltransferase[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2013,135(33):12152-12155.
APA [Chen, Ruidong.,Zhang, Haibo.,Li, Sumei.,Zhang, Guangtao.,Zhu, Yiguang.,...&[Liu, Jinsong] Chinese Acad Sci, Guangzhou Inst Biomed & Hlth, State Key Lab Resp Dis, Guangzhou 510530, Guangdong, Peoples R China.(2013).Characterizing Amosamine Biosynthesis in Amicetin Reveals AmiG as a Reversible Retaining Glycosyltransferase.JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,135(33),12152-12155.
MLA [Chen, Ruidong,et al."Characterizing Amosamine Biosynthesis in Amicetin Reveals AmiG as a Reversible Retaining Glycosyltransferase".JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 135.33(2013):12152-12155.

入库方式: OAI收割

来源:南海海洋研究所

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