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Insights into Caerulomycin A Biosynthesis: A Two-Component Monooxygenase CrmH-Catalyzed Oxime Formation
Alternative Titlemannual of IR1
[Zhu, Yiguang; Zhang, Qingbo; Li, Sumei; Lin, Qinheng; Zhang, Guangtao; Zhang, Haibo; Zhang, Changsheng] Chinese Acad Sci, CAS Key Lab Trop Marine Bioresources & Ecol, RNAM Ctr Marine Microbiol, Guangdong Key Lab Marine Mat Med,South China Sea, Guangzhou 510301, Guangdong, Peoples R China; [Zhang, Qingbo; Lin, Qinheng] Univ Chinese Acad Sci, Beijing 100049, Peoples R China; [Fu, Peng; Zhu, Weiming] Ocean Univ China, Sch Med & Pharm, Key Lab Marine Drugs, Chinese Minist Educ, Qingdao 266003, Peoples R China; [Shi, Rong] Univ Laval, Dept Biochim Microbiol & Bioinformat, PROTEO, Quebec City, PQ G1V 0A6, Canada; [Shi, Rong] Univ Laval, IBIS, Quebec City, PQ G1V 0A6, Canada; weimingzhu@ouc.edu.cn; czhang2006@gmail.com
2013
Source PublicationJOURNAL OF THE AMERICAN CHEMICAL SOCIETY
ISSN0002-7863
Volume135Issue:50Pages:18750-18753
Contribution Rank产权排序
Cooperation Status填入合作性质等
AbstractThe immunosuppressive agent caerulomycin A features a unique 2,2'-bipyridine core structure and an unusual oxime functionality. Genetic and biochemical evidence confirms that the oxime formation in caerulomycin A biosynthesis is catalyzed by CrmH, a flavin-dependent two-component monooxygenase that is compatible with multiple flavin reductases, from a primary amine via a N-hydroxylamine intermediate. Structure homologue-guided site-directed mutagenesis studies identify four amino acid residues that are essential for CrmH catalysis. This study provides the first biochemical evidence of a two-component monooxygenase that catalyzes oxime formation.; description.abstract
DepartmentLMB
Subject AreaChemistry, Multidisciplinary
Funding OrganizationFinancial support was provided by MOST (2010CB833805), NSFC (31125001 and 31070045), and CAS (KZCX2-YW-JC202, KSCX2-EW-G-12, 08SL111002). We thank Profs. Yi Tang (UCLA), Shu-Ming Li (Philipps Universitat Marburg), and Shuangjun Lin (Shanghai Jiao Tong University) for help discussions. We are grateful to the analytical facilities in SCSIO. ; Financial support was provided by MOST (2010CB833805), NSFC (31125001 and 31070045), and CAS (KZCX2-YW-JC202, KSCX2-EW-G-12, 08SL111002). We thank Profs. Yi Tang (UCLA), Shu-Ming Li (Philipps Universitat Marburg), and Shuangjun Lin (Shanghai Jiao Tong University) for help discussions. We are grateful to the analytical facilities in SCSIO. ; Financial support was provided by MOST (2010CB833805), NSFC (31125001 and 31070045), and CAS (KZCX2-YW-JC202, KSCX2-EW-G-12, 08SL111002). We thank Profs. Yi Tang (UCLA), Shu-Ming Li (Philipps Universitat Marburg), and Shuangjun Lin (Shanghai Jiao Tong University) for help discussions. We are grateful to the analytical facilities in SCSIO. ; Financial support was provided by MOST (2010CB833805), NSFC (31125001 and 31070045), and CAS (KZCX2-YW-JC202, KSCX2-EW-G-12, 08SL111002). We thank Profs. Yi Tang (UCLA), Shu-Ming Li (Philipps Universitat Marburg), and Shuangjun Lin (Shanghai Jiao Tong University) for help discussions. We are grateful to the analytical facilities in SCSIO.
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Indexed Bysci
Language英语
Funding Projectdescription.project
Funding OrganizationFinancial support was provided by MOST (2010CB833805), NSFC (31125001 and 31070045), and CAS (KZCX2-YW-JC202, KSCX2-EW-G-12, 08SL111002). We thank Profs. Yi Tang (UCLA), Shu-Ming Li (Philipps Universitat Marburg), and Shuangjun Lin (Shanghai Jiao Tong University) for help discussions. We are grateful to the analytical facilities in SCSIO. ; Financial support was provided by MOST (2010CB833805), NSFC (31125001 and 31070045), and CAS (KZCX2-YW-JC202, KSCX2-EW-G-12, 08SL111002). We thank Profs. Yi Tang (UCLA), Shu-Ming Li (Philipps Universitat Marburg), and Shuangjun Lin (Shanghai Jiao Tong University) for help discussions. We are grateful to the analytical facilities in SCSIO. ; Financial support was provided by MOST (2010CB833805), NSFC (31125001 and 31070045), and CAS (KZCX2-YW-JC202, KSCX2-EW-G-12, 08SL111002). We thank Profs. Yi Tang (UCLA), Shu-Ming Li (Philipps Universitat Marburg), and Shuangjun Lin (Shanghai Jiao Tong University) for help discussions. We are grateful to the analytical facilities in SCSIO. ; Financial support was provided by MOST (2010CB833805), NSFC (31125001 and 31070045), and CAS (KZCX2-YW-JC202, KSCX2-EW-G-12, 08SL111002). We thank Profs. Yi Tang (UCLA), Shu-Ming Li (Philipps Universitat Marburg), and Shuangjun Lin (Shanghai Jiao Tong University) for help discussions. We are grateful to the analytical facilities in SCSIO.
WOS IDWOS:000328865100012
Citation statistics
Cited Times:25[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.scsio.ac.cn/handle/344004/10944
Collection中科院海洋生物资源可持续利用重点实验室
Corresponding Authorweimingzhu@ouc.edu.cn; czhang2006@gmail.com
Recommended Citation
GB/T 7714
[Zhu, Yiguang,Zhang, Qingbo,Li, Sumei,et al. Insights into Caerulomycin A Biosynthesis: A Two-Component Monooxygenase CrmH-Catalyzed Oxime Formation[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2013,135(50):18750-18753.
APA [Zhu, Yiguang.,Zhang, Qingbo.,Li, Sumei.,Lin, Qinheng.,Zhang, Guangtao.,...&czhang2006@gmail.com.(2013).Insights into Caerulomycin A Biosynthesis: A Two-Component Monooxygenase CrmH-Catalyzed Oxime Formation.JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,135(50),18750-18753.
MLA [Zhu, Yiguang,et al."Insights into Caerulomycin A Biosynthesis: A Two-Component Monooxygenase CrmH-Catalyzed Oxime Formation".JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 135.50(2013):18750-18753.
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