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学科主题: Chemistry, Multidisciplinary
题名: Characterizing Amosamine Biosynthesis in Amicetin Reveals AmiG as a Reversible Retaining Glycosyltransferase
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
通讯作者: czhang2006@gmail.com
刊名: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
发表日期: 2013
卷: 135, 期:33, 页:12152-12155
部门归属: LMB
资助者: 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.
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.
语种: 英语
原文出处: 查看原文
WOS记录号: WOS:000323536100001
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内容类型: 期刊论文
URI标识: http://ir.scsio.ac.cn/handle/344004/10994
Appears in Collections:中科院海洋生物资源可持续利用重点实验室_期刊论文

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[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.Characterizing Amosamine Biosynthesis in Amicetin Reveals AmiG as a Reversible Retaining Glycosyltransferase,JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2013,135(33):12152-12155
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