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DOI	10.1073/pnas.1615141114
	Recognition of protein-linked glycans as a determinant of peptidase activity
	Noach I.; Ficko-Blean E.; Pluvinage B.; Stuart C.; Jenkins M.L.; Brochu D.; Buenbrazo N.; Wakarchuk W.; Burke J.E.; Gilbert M.; Boraston A.B.
发表日期	2017
ISSN	0027-8424
起始页码	E679
结束页码	E688
卷号	114 期号:5
英文摘要	The vast majority of proteins are posttranslationally altered, with the addition of covalently linked sugars (glycosylation) being one of the most abundant modifications. However, despite the hydrolysis of protein peptide bonds by peptidases being a process essential to all life on Earth, the fundamental details of how peptidases accommodate posttranslational modifications, including glycosylation, has not been addressed. Through biochemical analyses and X-ray crystallographic structures we show that to hydrolyze their substrates, three structurally related metallopeptidases require the specific recognition of O-linked glycan modifications via carbohydrate-specific subsites immediately adjacent to their peptidase catalytic machinery. The three peptidases showed selectivity for different glycans, revealing protein-specific adaptations to particular glycan modifications, yet always cleaved the peptide bond immediately preceding the glycosylated residue. This insight builds upon the paradigm of how peptidases recognize substrates and provides a molecular understanding of glycoprotein degradation.
英文关键词	Glycoprotein; Metallopeptidase; O-glycopeptidase; O-glycosylation
语种	英语
scopus关键词	amino acid; carbohydrate; disaccharide; fetuin; glycan; glycopeptide; glycoprotein; glycosylated protein; glycosyltransferase; metalloproteinase; monosaccharide; peptidase; peptide fragment; serine; synthetic peptide; thermolysin; threonine; Tn antigen; mucin; peptide hydrolase; polysaccharide; catalysis; Conference Paper; enzyme active site; enzyme activity; enzyme specificity; glycosylation; nonhuman; priority journal; protein analysis; protein degradation; protein expression; protein processing; protein structure; X ray crystallography; chemistry; Escherichia coli; genetics; glycosylation; metabolism; protein conformation; protein processing; Escherichia coli; Fetuins; Glycopeptides; Glycosylation; Mucins; Peptide Hydrolases; Polysaccharides; Protein Conformation; Protein Processing, Post-Translational
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/160666
作者单位	Noach, I., Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8W 3P6, Canada; Ficko-Blean, E., Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8W 3P6, Canada; Pluvinage, B., Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8W 3P6, Canada; Stuart, C., Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8W 3P6, Canada; Jenkins, M.L., Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8W 3P6, Canada; Brochu, D., Human Health Therapeutics, National Research Council Canada, Ottawa, ON K1A 0R6, Canada; Buenbrazo, N., Department of Chemistry and Biology, Ryerson University, Toronto, ON M5B 2K3, Canada; Wakarchuk, W., Department of Chemistry and Biology, Ryerson University, Toronto, ON M5B 2K3, Canada; Burke, J.E., Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8W 3P6, Canada; Gilbert, M., Human Health Thera...
推荐引用方式 GB/T 7714	Noach I.,Ficko-Blean E.,Pluvinage B.,et al. Recognition of protein-linked glycans as a determinant of peptidase activity[J],2017,114(5).
APA	Noach I..,Ficko-Blean E..,Pluvinage B..,Stuart C..,Jenkins M.L..,...&Boraston A.B..(2017).Recognition of protein-linked glycans as a determinant of peptidase activity.Proceedings of the National Academy of Sciences of the United States of America,114(5).
MLA	Noach I.,et al."Recognition of protein-linked glycans as a determinant of peptidase activity".Proceedings of the National Academy of Sciences of the United States of America 114.5(2017).