DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ahn, Woo-Chan | ko |
dc.contributor.author | An, Yan | ko |
dc.contributor.author | Song, Kyung-Mo | ko |
dc.contributor.author | Park, Kwang-Hyun | ko |
dc.contributor.author | Lee, Su-jin | ko |
dc.contributor.author | Oh, Byung-Ha | ko |
dc.contributor.author | Park, Jong-Tae | ko |
dc.contributor.author | Woo, Eui-Jeon | ko |
dc.date.accessioned | 2022-04-15T06:48:10Z | - |
dc.date.available | 2022-04-15T06:48:10Z | - |
dc.date.created | 2022-04-04 | - |
dc.date.created | 2022-04-04 | - |
dc.date.created | 2022-04-04 | - |
dc.date.created | 2022-04-04 | - |
dc.date.issued | 2022-01 | - |
dc.identifier.citation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.586, pp.49 - 54 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | http://hdl.handle.net/10203/294801 | - |
dc.description.abstract | Maltodextrin glucosidase (MalZ) is a key enzyme in the maltose utilization pathway in Escherichia coli that liberates glucose from the reducing end of the short malto-oligosaccharides. Unlike other enzymes in the GH13_21 subfamily, the hydrolytic activity of MalZ is limited to maltodextrin rather than long starch substrates, forming various transglycosylation products in alpha-1,3, alpha-1,4 or alpha-1,6 linkages. The mechanism for the substrate binding and hydrolysis of this enzyme is not well understood yet. Here, we present the dimeric crystal structure of MalZ, with the N-domain generating a unique substrate binding groove. The N-domain bears CBM34 architecture and forms a part of the active site in the catalytic domain of the adjacent molecule. The groove found between the N-domain and catalytic domain from the adjacent molecule, shapes active sites suitable for short malto-oligosaccharides, but hinders long stretches of oligosaccharides. The conserved residue of E44 protrudes at subsite +2, elucidating the hydrolysis pattern of the substrate by the glucose unit from the reducing end. The structural analysis provides a molecular basis for the substrate specificity and the enzymatic property, and has potential industrial application for protein engineering. (C) 2021 The Authors. Published by Elsevier Inc. | - |
dc.language | English | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.title | Dimeric architecture of maltodextrin glucosidase (MalZ) provides insights into the substrate recognition and hydrolysis mechanism | - |
dc.type | Article | - |
dc.identifier.wosid | 000768269900006 | - |
dc.identifier.scopusid | 2-s2.0-85119510603 | - |
dc.type.rims | ART | - |
dc.citation.volume | 586 | - |
dc.citation.beginningpage | 49 | - |
dc.citation.endingpage | 54 | - |
dc.citation.publicationname | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.identifier.doi | 10.1016/j.bbrc.2021.11.070 | - |
dc.contributor.localauthor | Oh, Byung-Ha | - |
dc.contributor.nonIdAuthor | An, Yan | - |
dc.contributor.nonIdAuthor | Song, Kyung-Mo | - |
dc.contributor.nonIdAuthor | Park, Kwang-Hyun | - |
dc.contributor.nonIdAuthor | Lee, Su-jin | - |
dc.contributor.nonIdAuthor | Park, Jong-Tae | - |
dc.contributor.nonIdAuthor | Woo, Eui-Jeon | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | Maltodextrin glucosidase | - |
dc.subject.keywordAuthor | MalZ | - |
dc.subject.keywordAuthor | Dimerization | - |
dc.subject.keywordAuthor | Crystal structure | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | AMYLASE | - |
dc.subject.keywordPlus | SUBFAMILIES | - |
dc.subject.keywordPlus | METABOLISM | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordPlus | ENZYME | - |
dc.subject.keywordPlus | GENE | - |
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