Title |
Structure and Kinetic Investigation of Streptococcus pyogenes Family GH38 α-Mannosidase
|
---|---|
Published in |
PLOS ONE, February 2010
|
DOI | 10.1371/journal.pone.0009006 |
Pubmed ID | |
Authors |
Michael D. L. Suits, Yanping Zhu, Edward J. Taylor, Julia Walton, David L. Zechel, Harry J. Gilbert, Gideon J. Davies |
Abstract |
The enzymatic hydrolysis of alpha-mannosides is catalyzed by glycoside hydrolases (GH), termed alpha-mannosidases. These enzymes are found in different GH sequence-based families. Considerable research has probed the role of higher eukaryotic "GH38" alpha-mannosides that play a key role in the modification and diversification of hybrid N-glycans; processes with strong cellular links to cancer and autoimmune disease. The most extensively studied of these enzymes is the Drosophila GH38 alpha-mannosidase II, which has been shown to be a retaining alpha-mannosidase that targets both alpha-1,3 and alpha-1,6 mannosyl linkages, an activity that enables the enzyme to process GlcNAc(Man)(5)(GlcNAc)(2) hybrid N-glycans to GlcNAc(Man)(3)(GlcNAc)(2). Far less well understood is the observation that many bacterial species, predominantly but not exclusively pathogens and symbionts, also possess putative GH38 alpha-mannosidases whose activity and specificity is unknown. |
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Geographical breakdown
Country | Count | As % |
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Unknown | 75 | 95% |
Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 27 | 34% |
Student > Ph. D. Student | 18 | 23% |
Student > Bachelor | 8 | 10% |
Other | 5 | 6% |
Professor > Associate Professor | 5 | 6% |
Other | 9 | 11% |
Unknown | 7 | 9% |
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Pharmacology, Toxicology and Pharmaceutical Science | 2 | 3% |
Other | 4 | 5% |
Unknown | 7 | 9% |