SCSIO OpenIR  > 中科院海洋生物资源可持续利用重点实验室
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
Source PublicationJOURNAL OF THE AMERICAN CHEMICAL SOCIETY
ISSN0002-7863
Volume135Issue:33Pages:12152-12155
AbstractThe 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.
DepartmentLMB
Subject AreaChemistry, Multidisciplinary
Funding OrganizationFinancial 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.
URL查看原文
Language英语
Funding OrganizationFinancial 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 IDWOS:000323536100001
Citation statistics
Cited Times:17[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.scsio.ac.cn/handle/344004/10994
Collection中科院海洋生物资源可持续利用重点实验室
Corresponding Authorczhang2006@gmail.com
Recommended Citation
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.,...&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.
Files in This Item:
File Name/Size DocType Version Access License
Characterizing Amosa(642KB) 开放获取CC BY-NC-SAApplication Full Text
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.