Characterizing Amosamine Biosynthesis in Amicetin Reveals AmiG as a Reversible Retaining Glycosyltransferase
[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; czhang2006@gmail.com
2013
发表期刊JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
ISSN0002-7863
卷号135期号:33页码:12152-12155
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.
部门归属LMB
学科领域Chemistry, Multidisciplinary
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. ; 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. ; 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. ; 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.
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语种英语
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. ; 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. ; 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. ; 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.
WOS记录号WOS:000323536100001
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被引频次:15[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.scsio.ac.cn/handle/344004/10994
专题中科院海洋生物资源可持续利用重点实验室
通讯作者czhang2006@gmail.com
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[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.,...&czhang2006@gmail.com.(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.
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