| http://purl.uniprot.org/citations/23665536 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23665536 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23665536 | http://www.w3.org/2000/01/rdf-schema#comment | "Sialidases release the terminal sialic acid residue from a wide range of sialic acid-containing polysaccharides. Bacteroides thetaiotaomicron, a symbiotic commensal microbe, resides in and dominates the human intestinal tract. We characterized the recombinant sialidase from B. thetaiotaomicron (BTSA) and demonstrated that it has broad substrate specificity with a relative activity of 97, 100 and 64 for 2,3-, 2,6- and 2,8-linked sialic substrates, respectively. The hydrolysis activity of BTSA was inhibited by a transition state analogue, 2-deoxy-2,3-dehydro-N-acetyl neuraminic acid, by competitive inhibition with a Ki value of 35μM. The structure of BSTA was determined at a resolution of 2.3Å. This structure exhibited a unique carbohydrate-binding domain (CBM) at its N-terminus (a.a. 23-190) that is adjacent to the catalytic domain (a.a. 191-535). The catalytic domain has a conserved arginine triad with a wide-open entrance for the substrate that exposes the catalytic residue to the surface. Unlike other pathogenic sialidases, the polysaccharide-binding site in the CBM is near the active site and possibly holds and positions the polysaccharide substrate directly at the active site. The structural feature of a wide substrate-binding groove and closer proximity of the polysaccharide-binding site to the active site could be a unique signature of the commensal sialidase BTSA and provide a molecular basis for its pharmaceutical application."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.org/dc/terms/identifier | "doi:10.1016/J.BBAPAP.2013.04.028"xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbapap.2013.04.028"xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Kim J.H."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Kim J.H."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Kim Y.W."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Kim Y.W."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Lee D.H."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Lee D.H."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Park K.H."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Park K.H."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Ahn H.J."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Ahn H.J."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Woo E.J."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Woo E.J."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Kim M.G."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/author | "Kim M.G."xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/name | "Biochim. Biophys. Acta"xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta"xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/pages | "1510-1519"xsd:string |
| http://purl.uniprot.org/citations/23665536 | http://purl.uniprot.org/core/pages | "1510-1519"xsd:string |