Structural and functional analysis of substrate recognition by the 250s loop in amylomaltase from Thermus brockianus

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dc.contributor.authorJ H Jung-
dc.contributor.authorTae Yang Jung-
dc.contributor.authorD H Seo-
dc.contributor.authorS M Yoon-
dc.contributor.authorH C Choi-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorC S Park-
dc.contributor.authorEui-Jeon Woo-
dc.date.accessioned2017-04-19T09:21:13Z-
dc.date.available2017-04-19T09:21:13Z-
dc.date.issued2011-
dc.identifier.issn0887-3585-
dc.identifier.uri10.1002/prot.22911ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9940-
dc.description.abstractAmylomaltase, or 4-α-glucanotransferase (EC 2.4.1.25), is involved in glycogen and maltooligosaccharide metabolism in microorganisms, catalyzing both the hydrolysis and transfer of an α-1,4-oligosacchraride to other sugar molecules. In this study, we determined the crystal structure of amylomaltase from Thermus brockianus at a resolution of 2.3 A and conducted a biochemical study to understand the detailed mechanism for its activity. Careful comparison with previous amylomaltase structures showed a pattern of conformational flexibility in the 250s loop with higher B-factor. Amylomaltase from T. brockianus exhibited a high transglycosylation factor for glucose and a lower value for maltose. Mutation of Gln256 resulted in increased Km for maltotriose and a sharp decrease of the transglycosylation factor for maltose, suggesting the involvement of Gln 256 in substrate binding between subsites +1 and +2. Mutation of Phe251 resulted in significantly lower glucose production but increased maltose production from maltopentose substrates, showing an altered substrate-binding affinity. The mutational data suggest the conformational flexibility of the loop may be involved in substrate binding in the GH77 family. Here, we present an action model of the 250s loop providing the molecular basis for the involvement of residues Phe251, Gln256, and Trp258 in the hydrolysis and transglycosylation activities in amylomaltase.-
dc.publisherWiley-
dc.titleStructural and functional analysis of substrate recognition by the 250s loop in amylomaltase from Thermus brockianus-
dc.title.alternativeStructural and functional analysis of substrate recognition by the 250s loop in amylomaltase from Thermus brockianus-
dc.typeArticle-
dc.citation.titleProteins-Structure Function and Bioinformatics-
dc.citation.number2-
dc.citation.endPage644-
dc.citation.startPage633-
dc.citation.volume79-
dc.contributor.affiliatedAuthorTae Yang Jung-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorEui-Jeon Woo-
dc.contributor.alternativeName정종현-
dc.contributor.alternativeName정태양-
dc.contributor.alternativeName서동호-
dc.contributor.alternativeName윤세미-
dc.contributor.alternativeName최현창-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName박천석-
dc.contributor.alternativeName우의전-
dc.identifier.bibliographicCitationProteins-Structure Function and Bioinformatics, vol. 79, no. 2, pp. 633-644-
dc.identifier.doi10.1002/prot.22911-
dc.subject.keyword250s loop-
dc.subject.keywordAmylomaltase-
dc.subject.keywordSubstrate binding sites-
dc.subject.keywordThermus brockianus-
dc.subject.local250s loop-
dc.subject.localAmylomaltase-
dc.subject.localSubstrate binding site-
dc.subject.localSubstrate binding sites-
dc.subject.localThermus brockianus-
dc.description.journalClassY-
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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