Structural and biochemical characterization of the broad substrate specificity of Bacteroides thetaiotaomicron commensal sialidase
DC Field | Value | Language |
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dc.contributor.author | Park, Kwang-Hyun | - |
dc.contributor.author | Kim, Min-Gyu | - |
dc.contributor.author | Ahn, Hee-Jeong | - |
dc.contributor.author | Lee, Dae-Han | - |
dc.contributor.author | Kim, Jin-Hyo | - |
dc.contributor.author | Kim, Young-Wan | - |
dc.contributor.author | Woo, Eui-Jeon | - |
dc.date.accessioned | 2021-09-05T23:11:41Z | - |
dc.date.available | 2021-09-05T23:11:41Z | - |
dc.date.created | 2021-06-14 | - |
dc.date.issued | 2013-08 | - |
dc.identifier.issn | 1570-9639 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/102550 | - |
dc.description.abstract | 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 K-i value of 35 mu M. The structure of BSTA was determined at a resolution of 2.3 angstrom. 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. (C) 2013 Elsevier B.V. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.subject | STRUCTURE-BASED DESIGN | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | NEURAMINIDASE INHIBITORS | - |
dc.subject | STREPTOCOCCUS-PNEUMONIAE | - |
dc.subject | VIRUS NEURAMINIDASE | - |
dc.subject | BACTERIAL SIALIDASE | - |
dc.subject | MICROBIAL ECOLOGY | - |
dc.subject | TRANS-SIALIDASE | - |
dc.subject | HIGH-RESOLUTION | - |
dc.subject | GUT SYMBIONT | - |
dc.title | Structural and biochemical characterization of the broad substrate specificity of Bacteroides thetaiotaomicron commensal sialidase | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Young-Wan | - |
dc.identifier.doi | 10.1016/j.bbapap.2013.04.028 | - |
dc.identifier.scopusid | 2-s2.0-84882267201 | - |
dc.identifier.wosid | 000321802200007 | - |
dc.identifier.bibliographicCitation | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v.1834, no.8, pp.1510 - 1519 | - |
dc.relation.isPartOf | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | - |
dc.citation.title | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | - |
dc.citation.volume | 1834 | - |
dc.citation.number | 8 | - |
dc.citation.startPage | 1510 | - |
dc.citation.endPage | 1519 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | STRUCTURE-BASED DESIGN | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | NEURAMINIDASE INHIBITORS | - |
dc.subject.keywordPlus | STREPTOCOCCUS-PNEUMONIAE | - |
dc.subject.keywordPlus | VIRUS NEURAMINIDASE | - |
dc.subject.keywordPlus | BACTERIAL SIALIDASE | - |
dc.subject.keywordPlus | MICROBIAL ECOLOGY | - |
dc.subject.keywordPlus | TRANS-SIALIDASE | - |
dc.subject.keywordPlus | HIGH-RESOLUTION | - |
dc.subject.keywordPlus | GUT SYMBIONT | - |
dc.subject.keywordAuthor | Bacteroides thetaiotaomicron | - |
dc.subject.keywordAuthor | Sialidase | - |
dc.subject.keywordAuthor | Substrate specificity | - |
dc.subject.keywordAuthor | Protein structure | - |
dc.subject.keywordAuthor | Carbohydrate-binding domain | - |
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