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Biochemical and Structural Insights into the Aminotransferase CrmG in Caerulomycin Biosynthesis
Zhu, Yiguang; Xu, Jinxin; Mei, Xiangui; Feng, Zhan; Zhang, Liping; Zhang, Qingbo; Zhang, Guangtao; Zhu, Weiming; Liu, Jinsong; Zhang, Changsheng; Zhang, CS (reprint author), Chinese Acad Sci, South China Sea Inst Oceanol, RNAM Ctr Marine Microbiol, CAS Key Lab Trop Marine Bioresources & Ecol,Guang, 164 West Xingang Rd, Guangzhou 510301, Guangdong, Peoples R China.; Liu, JS (reprint author), Chinese Acad Sci, Guangzhou Inst Biomed & Hlth, Key Lab Resp Dis, Guangzhou 510530, Guangdong, Peoples R China.; Zhu, WM (reprint author), Ocean Univ China, Sch Med & Pharm, Minist Educ China, Key Lab Marine Drugs, Qingdao 266003, Peoples R China.
2016
Source PublicationACS CHEMICAL BIOLOGY
Volume11Issue:4Pages:943-952
AbstractCaerulomycin A (CRM A 1) belongs to a family of natural products containing a 2,2'-bipyridyl ring core structure and is currently under development as a potent novel immunosuppressive agent. Herein, we report the functional characterization, kinetic analysis, substrate specificity, and structure insights of an aminotransferase CrmG in 1 biosynthesis. The aminotransferase CrmG was confirmed to catalyze a key transamination reaction to convert an aldehyde group to an amino group in the 1 biosynthetic pathway, preferring L-glutamate and L-glutamine as the amino donor substrates. The crystal structures of CrmG in complex with the cofactor 5'-pyridoxal phosphate (PLP) or 5'-pyridoxamine phosphate (PMP) or the acceptor substrate were determined to adopt a canonical fold-type I of PLP-dependent enzymes with a unique small additional domain. The structure guided site-directed mutagenesis identified key amino acid residues for substrate binding and catalytic activities, thus providing insights into the transamination mechanism of CrmG.
Department[Zhu, Yiguang; Zhang, Liping; Zhang, Qingbo; Zhang, Guangtao; Zhang, Changsheng] Chinese Acad Sci, South China Sea Inst Oceanol, RNAM Ctr Marine Microbiol, CAS Key Lab Trop Marine Bioresources & Ecol,Guang, 164 West Xingang Rd, Guangzhou 510301, Guangdong, Peoples R China; [Xu, Jinxin; Feng, Zhan; Liu, Jinsong] Chinese Acad Sci, Guangzhou Inst Biomed & Hlth, Key Lab Resp Dis, Guangzhou 510530, Guangdong, Peoples R China; [Mei, Xiangui; Zhu, Weiming] Ocean Univ China, Sch Med & Pharm, Minist Educ China, Key Lab Marine Drugs, Qingdao 266003, Peoples R China ; LMB
Subject AreaBiochemistry & Molecular Biology
Document Type期刊论文
Identifierhttp://ir.scsio.ac.cn/handle/344004/15467
Collection中科院海洋生物资源可持续利用重点实验室
Corresponding AuthorZhang, CS (reprint author), Chinese Acad Sci, South China Sea Inst Oceanol, RNAM Ctr Marine Microbiol, CAS Key Lab Trop Marine Bioresources & Ecol,Guang, 164 West Xingang Rd, Guangzhou 510301, Guangdong, Peoples R China.; Liu, JS (reprint author), Chinese Acad Sci, Guangzhou Inst Biomed & Hlth, Key Lab Resp Dis, Guangzhou 510530, Guangdong, Peoples R China.; Zhu, WM (reprint author), Ocean Univ China, Sch Med & Pharm, Minist Educ China, Key Lab Marine Drugs, Qingdao 266003, Peoples R China.
Recommended Citation
GB/T 7714
Zhu, Yiguang,Xu, Jinxin,Mei, Xiangui,et al. Biochemical and Structural Insights into the Aminotransferase CrmG in Caerulomycin Biosynthesis[J]. ACS CHEMICAL BIOLOGY,2016,11(4):943-952.
APA Zhu, Yiguang.,Xu, Jinxin.,Mei, Xiangui.,Feng, Zhan.,Zhang, Liping.,...&Zhu, WM .(2016).Biochemical and Structural Insights into the Aminotransferase CrmG in Caerulomycin Biosynthesis.ACS CHEMICAL BIOLOGY,11(4),943-952.
MLA Zhu, Yiguang,et al."Biochemical and Structural Insights into the Aminotransferase CrmG in Caerulomycin Biosynthesis".ACS CHEMICAL BIOLOGY 11.4(2016):943-952.
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