Amide N-glycosylation by Asm25, an N-glycosyltransferase of ansamitocins

doi:10.1016/j.chembiol.2008.06.007

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	Amide N-glycosylation by Asm25, an N-glycosyltransferase of ansamitocins
	Zhao, Peiji 2; Bai, Linquan 1; Ma, Juan 2; Zeng, Ying2 ; Li, Lei 1; Zhang, Yirong 1; Lu, Chunhua 3; Dai, Huanqin 2; Wu, Zhaoxian 3; Li, Yaoyao 3
刊名	CHEMISTRY & BIOLOGY
	2008-08-25
卷号	15 期号:8 页码:863-874
关键词	Biosynthetic Gene-cluster Lechevalieria-aerocolonigenes Atcc-39243 Escherichia-coli 3-amino-5-hydroxybenzoic Acid Actinosynnema-pretiosum Maytansinoid Antibiotics Streptomyces Sp Indolocarbazole Expression Substrate
ISSN号	1074-5521
DOI	10.1016/j.chembiol.2008.06.007
文献子类	Article
英文摘要	Ansamitocins are potent antitumor maytansinoids produced by Actinosynnema pretiosum. Their biosynthesis involves the initial assembly of a macrolactam polyketide, followed by a series of postpolyketide synthase (PKS) modifications. Three ansamitocin glycosides were isolated from A. pretiosum and fully characterized structurally as novel ansamitocin derivatives, carrying a (3-D-glucosyl group attached to the macrolactam amide nitrogen in place of the N-methyl group. By gene inactivation and complementation, asm25 was identified as the N-glycosyltransferase gene responsible for the macrolactam amide N-glycosylation of ansamitocins. Soluble, enzymatically active Asm25 protein was obtained from asm25-expressing E, coli by solubilization from inclusion bodies. Its optimal reaction conditions, including temperature, pH, metal ion requirement, and Km/Kcat, were determined. Asm25 also showed broad substrate specificity toward other ansamycins and synthetic indolin-2-ones. To the best of our knowledge, this represents the first in vitro characterization of a purified antibiotic N-glycosyltransferase.
学科主题	Biochemistry & Molecular Biology
WOS关键词	BIOSYNTHETIC GENE-CLUSTER ; LECHEVALIERIA-AEROCOLONIGENES ATCC-39243 ; ESCHERICHIA-COLI ; 3-AMINO-5-HYDROXYBENZOIC ACID ; ACTINOSYNNEMA-PRETIOSUM ; MAYTANSINOID ANTIBIOTICS ; STREPTOMYCES SP ; INDOLOCARBAZOLE ; EXPRESSION ; SUBSTRATE
WOS研究方向	Biochemistry & Molecular Biology
语种	英语
WOS记录号	WOS:000258940000014
资助机构	National Natural Science Fund for Distinguished Young Scholars [30325044]; Natural Science Foundation of China [30600005, 30570019]; Ministry of Science and Technology
公开日期	2011-11-24
内容类型	期刊论文
源URL	[http://ir.kib.ac.cn:8080/handle/151853/1707]
专题	昆明植物研究所_植物化学与西部植物资源持续利用国家重点实验室
作者单位	1.Shanghai Jiao Tong Univ, Coll Life Sci & Biotechnol, Lab Microbial Metab, Shanghai 200240, Peoples R China 2.Chinese Acad Sci, Kunming Inst Bot, State Key Lab Phytochem & Plant Resources W China, Kunming 650204, Yunnan, Peoples R China 3.Xiamen Univ, Key Lab Minist Educ Cell Biol & Tumor Cell Engn, Sch Life Sci, Fujian 361005, Peoples R China 4.Univ Washington, Dept Chem, Seattle, WA 98195 USA
推荐引用方式 GB/T 7714	Zhao, Peiji,Bai, Linquan,Ma, Juan,et al. Amide N-glycosylation by Asm25, an N-glycosyltransferase of ansamitocins[J]. CHEMISTRY & BIOLOGY,2008,15(8):863-874.
APA	Zhao, Peiji.,Bai, Linquan.,Ma, Juan.,Zeng, Ying.,Li, Lei.,...&Floss, Heinz G..(2008).Amide N-glycosylation by Asm25, an N-glycosyltransferase of ansamitocins.CHEMISTRY & BIOLOGY,15(8),863-874.
MLA	Zhao, Peiji,et al."Amide N-glycosylation by Asm25, an N-glycosyltransferase of ansamitocins".CHEMISTRY & BIOLOGY 15.8(2008):863-874.