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| Enterococcus faecalis alpha 1-2-mannosidase (EfMan-I): an efficient catalyst for glycoprotein N-glycan modification | |
| Li, Yanhong1; Li, Riyao1; Yu, Hai1; Sheng, Xue1; Wang, Jing1,2; Fisher, Andrew J.1,3; Chen, Xi1 | |
| 2020-02-01 | |
| Source Publication | FEBS LETTERS
 |
| ISSN | 0014-5793 |
| Volume | 594Issue:3Pages:439-451 |
| Corresponding Author | Chen, Xi(xiichen@ucdavis.edu) |
| Abstract | While multiple alpha 1-2-mannosidases are necessary for glycoprotein N-glycan maturation in vertebrates, a single bacterial alpha 1-2-mannosidase can be sufficient to cleave all alpha 1-2-linked mannose residues in host glycoprotein N-glycans. We report here the characterization and crystal structure of a new alpha 1-2-mannosidase (EfMan-I) from Enterococcus faecalis, a Gram-positive opportunistic human pathogen. EfMan-I catalyzes the cleavage of alpha 1-2-mannose from not only oligomannoses but also high-mannose-type N-glycans on glycoproteins. Its 2.15 angstrom resolution crystal structure reveals a two-domain enzyme fold similar to other CAZy GH92 mannosidases. An unexpected potassium ion was observed bridging two domains near the active site. These findings support EfMan-I as an effective catalyst for in vitro N-glycan modification of glycoproteins with high-mannose-type N-glycans. |
| Keyword | alpha-mannosidase crystal structure glycoprotein modification mannosidase N-glycan enzymatic modification |
| DOI | 10.1002/1873-3468.13618 |
| Indexed By | SCI |
| Language | 英语 |
| Funding Project | United State Defense Threat Reduction Agency[HDTRA1-15-1-0054] ; U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences[DE-AC02-76SF00515] ; DOE Office of Biological and Environmental Research ; National Institutes of Health, National Institute of General Medical Sciences[P41GM103393] ; United State Defense Threat Reduction Agency[HDTRA1-15-1-0054] ; U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences[DE-AC02-76SF00515] ; DOE Office of Biological and Environmental Research ; National Institutes of Health, National Institute of General Medical Sciences[P41GM103393] |
| WOS Research Area | Biochemistry & Molecular Biology ; Biophysics ; Cell Biology |
| WOS Subject | Biochemistry & Molecular Biology ; Biophysics ; Cell Biology |
| WOS ID | WOS:000533959400004 |
| Publisher | WILEY |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.qdio.ac.cn/handle/337002/163349 |
| Collection | 实验海洋生物学重点实验室 |
| Corresponding Author | Chen, Xi |
| Affiliation | 1.Univ Calif Davis, Dept Chem, Davis, CA 95616 USA 2.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao, Peoples R China 3.Univ Calif Davis, Dept Mol & Cellular Biol, Davis, CA 95616 USA |
| Recommended Citation GB/T 7714 | Li, Yanhong,Li, Riyao,Yu, Hai,et al. Enterococcus faecalis alpha 1-2-mannosidase (EfMan-I): an efficient catalyst for glycoprotein N-glycan modification[J]. FEBS LETTERS,2020,594(3):439-451. |
| APA | Li, Yanhong.,Li, Riyao.,Yu, Hai.,Sheng, Xue.,Wang, Jing.,...&Chen, Xi.(2020).Enterococcus faecalis alpha 1-2-mannosidase (EfMan-I): an efficient catalyst for glycoprotein N-glycan modification.FEBS LETTERS,594(3),439-451. |
| MLA | Li, Yanhong,et al."Enterococcus faecalis alpha 1-2-mannosidase (EfMan-I): an efficient catalyst for glycoprotein N-glycan modification".FEBS LETTERS 594.3(2020):439-451. |
| Files in This Item: | ||||||
| File Name/Size | DocType | Version | Access | License | ||
| 1873-3468.13618.pdf（1273KB） | 期刊论文 | 出版稿 | 限制开放 | CC BY-NC-SA | View | |
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