Structural insights into the substrate recognition properties of beta-glucosidase
DC Field | Value | Language |
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dc.contributor.author | Nam, Ki Hyun | - |
dc.contributor.author | Sung, Min Woo | - |
dc.contributor.author | Hwang, Kwang Yeon | - |
dc.date.accessioned | 2021-09-08T05:51:36Z | - |
dc.date.available | 2021-09-08T05:51:36Z | - |
dc.date.created | 2021-06-11 | - |
dc.date.issued | 2010-01-01 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/117182 | - |
dc.description.abstract | Glucosidase enzymes (EC 3.2.1-3.2.3) hydrolyze sugars and are implicated in a wide spectrum of biological processes. Recently we reported that beta-glucosidase has varied kinetic parameters for the natural and synthetic substrates [K.H Nam. S.J. Kim, M.Y. Kim, J.H. Kim, T.S. Yeo, C.M. Lee, H.K Jun, K.Y. Hwang. Crystal structure of engineered beta-glucosidase from a soil metagenome, Proteins 73 (2009) 798-793]. However, an understanding of the kinetic values of beta-glucosidase has not yet enabled the elucidation of its molecular function. Here, we report the X-ray crystal structure of beta-glucosidase with a glucose and cellobiose fragment from uncultured soil metagenome. From the various crystals, we obtained the pre-reaction (native). intermediate (disaccharide cleavage) and post-reaction (glucose binding) states of the active site pocket. These structures provide snapshot of the catalytic processing of beta-glucosidase. In addition, the intermediate state of the crystal structure provides insight into the substrate specificity of beta-glucosidase. These structural studies will facilitate elucidation of the architctural mechanism responsible for the substrate recognition of beta-glucosidase. (C) 2009 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | CATALYTIC MACHINERY | - |
dc.subject | CRYSTAL-STRUCTURES | - |
dc.subject | GLYCOSIDASES | - |
dc.subject | SPECIFICITY | - |
dc.subject | HYDROLASES | - |
dc.subject | COMPLEXES | - |
dc.subject | MECHANISM | - |
dc.title | Structural insights into the substrate recognition properties of beta-glucosidase | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Hwang, Kwang Yeon | - |
dc.identifier.doi | 10.1016/j.bbrc.2009.12.038 | - |
dc.identifier.scopusid | 2-s2.0-72949100309 | - |
dc.identifier.wosid | 000273624500200 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.391, no.1, pp.1131 - 1135 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 391 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 1131 | - |
dc.citation.endPage | 1135 | - |
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 | CATALYTIC MACHINERY | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURES | - |
dc.subject.keywordPlus | GLYCOSIDASES | - |
dc.subject.keywordPlus | SPECIFICITY | - |
dc.subject.keywordPlus | HYDROLASES | - |
dc.subject.keywordPlus | COMPLEXES | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordAuthor | beta-Glucosidase | - |
dc.subject.keywordAuthor | Catalysis processing | - |
dc.subject.keywordAuthor | Intermediate state | - |
dc.subject.keywordAuthor | Substrate specificity | - |
dc.subject.keywordAuthor | Steric hindrance | - |
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