| http://purl.uniprot.org/citations/25487964 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25487964 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25487964 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/25487964 | http://www.w3.org/2000/01/rdf-schema#comment | "Glycoside hydrolase family 99 (GH99) was created to categorize sequence-related glycosidases possessing endo-α-mannosidase activity: the cleavage of mannosidic linkages within eukaryotic N-glycan precursors (Glc1-3 Man9 GlcNAc2 ), releasing mono-, di- and triglucosylated-mannose (Glc1-3 -1,3-Man). GH99 family members have recently been implicated in the ability of Bacteroides spp., present within the gut microbiota, to metabolize fungal cell wall α-mannans, releasing α-1,3-mannobiose by hydrolysing αMan-1,3-αMan→1,2-αMan-1,2-αMan sequences within branches off the main α-1,6-mannan backbone. We report the development of a series of substrates and inhibitors, which we use to kinetically and structurally characterise this novel endo-α-1,2-mannanase activity of bacterial GH99 enzymes from Bacteroides thetaiotaomicron and xylanisolvens. These data reveal an approximate 5 kJ mol(-1) preference for mannose-configured substrates in the -2 subsite (relative to glucose), which inspired the development of a new inhibitor, α-mannopyranosyl-1,3-isofagomine (ManIFG), the most potent (bacterial) GH99 inhibitor reported to date. X-ray structures of ManIFG or a substrate in complex with wild-type or inactive mutants, respectively, of B. xylanisolvens GH99 reveal the structural basis for binding to D-mannose- rather than D-glucose-configured substrates."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.org/dc/terms/identifier | "doi:10.1002/CHEM.201405539"xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.org/dc/terms/identifier | "doi:10.1002/chem.201405539"xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/author | "Davies G.J."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/author | "Davies G.J."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/author | "Williams S.J."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/author | "Williams S.J."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/author | "Thompson A.J."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/author | "Thompson A.J."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/author | "Speciale G."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/author | "Speciale G."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/author | "Bellmaine S."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/author | "Bellmaine S."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/author | "Hakki Z."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/author | "Hakki Z."xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/name | "Chemistry"xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/name | "Chemistry"xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/pages | "1966-1977"xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/pages | "1966-1977"xsd:string |
| http://purl.uniprot.org/citations/25487964 | http://purl.uniprot.org/core/title | "Structural and kinetic dissection of the endo-alpha-1,2-mannanase activity of bacterial GH99 glycoside hydrolases from Bacteroidesspp."xsd:string |