Association of bi-functional activity in the N-terminal domain of glycogen debranching enzyme

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dc.contributor.authorMinho Lee-
dc.contributor.authorHyeong Nam Song-
dc.contributor.authorJ E Cho-
dc.contributor.authorP L Tran-
dc.contributor.authorS Park-
dc.contributor.authorJ T Park-
dc.contributor.authorEui-jeon Woo-
dc.date.accessioned2017-04-19T09:51:43Z-
dc.date.available2017-04-19T09:51:43Z-
dc.date.issued2014-
dc.identifier.issn0006291X-
dc.identifier.uri10.1016/j.bbrc.2014.01.134ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/11886-
dc.description.abstractGlycogen debranching enzyme (GDE) in mammals and yeast exhibits α-1,4-transferase and α-1,6-glucosidase activities within a single polypeptide chain and facilitates the breakdown of glycogen by a bi-functional mechanism. Each enzymatic activity of GDE is suggested to be associated with distinct domains; α-1,4-glycosyltransferase activity with the N-terminal domain and α-1,6-glucosidase activity with the C-terminal domain. Here, we present the biochemical features of the GDE from Saccharomyces cerevisiae using the substrate glucose(n)-β-cyclodextrin (Gn-β-CD). The bacterially expressed and purified GDE N-terminal domain (aa 1-644) showed α-1,4-transferase activity on maltotetraose (G4) and G4-β-CD, yielding various lengths of (G)n. Surprisingly, the N-terminal domain also exhibited α-1,6-glucosidase activity against G1-β-CD and G4-β-CD, producing G1 and β-CD. Mutational analysis showed that residues D535 and E564 in the N-terminal domain are essential for the transferase activity but not for the glucosidase activity. These results indicate that the N-terminal domain (1-644) alone has both α-1,4- transferase and the α-1,6-glucosidase activities and suggest that the bi-functional activity in the N-domain may occur via one active site, as observed in some archaeal debranching enzymes.-
dc.publisherElsevier-
dc.titleAssociation of bi-functional activity in the N-terminal domain of glycogen debranching enzyme-
dc.title.alternativeAssociation of bi-functional activity in the N-terminal domain of glycogen debranching enzyme-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number1-
dc.citation.endPage112-
dc.citation.startPage107-
dc.citation.volume445-
dc.contributor.affiliatedAuthorEui-jeon Woo-
dc.contributor.alternativeName이민호-
dc.contributor.alternativeName송형남-
dc.contributor.alternativeName조지은-
dc.contributor.alternativeNameTran-
dc.contributor.alternativeName박성훈-
dc.contributor.alternativeName박종태-
dc.contributor.alternativeName우의전-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 445, no. 1, pp. 107-112-
dc.identifier.doi10.1016/j.bbrc.2014.01.134-
dc.subject.keywordα-1,4-Transferase activity-
dc.subject.keywordα-1,6-Glucosidase activity-
dc.subject.keywordBi-functional-
dc.subject.keywordGlycogen debranching enzyme (GDE)-
dc.subject.keywordSaccharomyces cerevisiae-
dc.subject.localα-1,4-Transferase activity-
dc.subject.localα-1,6-Glucosidase activity-
dc.subject.localBi-functional-
dc.subject.localGlycogen debranching enzyme (GDE)-
dc.subject.localSaccharomyces cerevisiae-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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