A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus

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dc.contributor.authorJ T Park-
dc.contributor.authorHyung-Nam Song-
dc.contributor.authorTae-Yang Jung-
dc.contributor.authorM H Lee-
dc.contributor.authorSung Goo Park-
dc.contributor.authorEui-Jeon Woo-
dc.contributor.authorK H Park-
dc.date.accessioned2017-04-19T09:44:08Z-
dc.date.available2017-04-19T09:44:08Z-
dc.date.issued2013-
dc.identifier.issn1570-9639-
dc.identifier.uri10.1016/j.bbapap.2012.08.001ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/11570-
dc.description.abstractPFTA (Pyrococcus furiosus thermostable amylase) is a hyperthermophilic amylase isolated from the archaeon Pyrococcus furiosus. This enzyme possesses characteristics of both α-amylase- and cyclodextrin (CD)-hydrolyzing enzymes, allowing it to degrade pullulan, CD and acarbose - activities that are absent in most α-amylases - without the transferring activity that is common in CD-hydrolyzing enzymes. The crystal structure of PFTA revealed a unique monomeric subunit with an extended N-terminal region and an N′-domain folded into its own active site - a significantly altered domain configuration relative to that of the conventional dimeric CD-hydrolyzing amylases in glycoside hydrolase family 13. The active site is formed by the interface of the N'-domain and the catalytic domain and exhibits a broad and wide-open geometry without the concave pocket that is commonly found in the active sites of maltogenic amylases. The mutation of a residue (Gly415 to Glu) located at the domain interface between the N'- and catalytic domains yielded an enzyme that produced a significantly higher purity maltoheptaose (G7) from β-CD, supporting the involvement of this interface in substrate recognition and indicating that this mutant enzyme is a suitable candidate for the production of pure G7. The unique configuration of the active site distinguishes this archaic monomeric enzyme from classical bacterial CD-hydrolyzing amylases and provides a molecular basis for its enzymatic characteristics and for its potential use in industrial applications.-
dc.publisherElsevier-
dc.titleA novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus-
dc.title.alternativeA novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus-
dc.typeArticle-
dc.citation.titleBiochimica et Biophysica Acta-Proteins and Proteomics-
dc.citation.number1-
dc.citation.endPage386-
dc.citation.startPage380-
dc.citation.volume1834-
dc.contributor.affiliatedAuthorHyung-Nam Song-
dc.contributor.affiliatedAuthorTae-Yang Jung-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.affiliatedAuthorEui-Jeon Woo-
dc.contributor.alternativeName박종태-
dc.contributor.alternativeName송형남-
dc.contributor.alternativeName정태양-
dc.contributor.alternativeName이명희-
dc.contributor.alternativeName박성구-
dc.contributor.alternativeName우의전-
dc.contributor.alternativeName박관화-
dc.identifier.bibliographicCitationBiochimica et Biophysica Acta-Proteins and Proteomics, vol. 1834, no. 1, pp. 380-386-
dc.identifier.doi10.1016/j.bbapap.2012.08.001-
dc.subject.keywordGH13 family-
dc.subject.keywordHyperthermophilic enzyme-
dc.subject.keywordMaltoheptaose production-
dc.subject.keywordMonomer-
dc.subject.keywordSubstrate specificity-
dc.subject.localGH13 family-
dc.subject.localHyperthermophilic enzyme-
dc.subject.localMaltoheptaose production-
dc.subject.localmonomer-
dc.subject.localMonomer-
dc.subject.localSubstrate specificity-
dc.subject.localsubstrate specificity-
dc.description.journalClassY-
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Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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