DC Field | Value | Language |
---|---|---|
dc.contributor.author | J T Park | - |
dc.contributor.author | Hyung-Nam Song | - |
dc.contributor.author | Tae-Yang Jung | - |
dc.contributor.author | M H Lee | - |
dc.contributor.author | Sung Goo Park | - |
dc.contributor.author | Eui-Jeon Woo | - |
dc.contributor.author | K H Park | - |
dc.date.accessioned | 2017-04-19T09:44:08Z | - |
dc.date.available | 2017-04-19T09:44:08Z | - |
dc.date.issued | 2013 | - |
dc.identifier.issn | 1570-9639 | - |
dc.identifier.uri | 10.1016/j.bbapap.2012.08.001 | ko |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/11570 | - |
dc.description.abstract | PFTA (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.publisher | Elsevier | - |
dc.title | A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus | - |
dc.title.alternative | A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus | - |
dc.type | Article | - |
dc.citation.title | Biochimica et Biophysica Acta-Proteins and Proteomics | - |
dc.citation.number | 1 | - |
dc.citation.endPage | 386 | - |
dc.citation.startPage | 380 | - |
dc.citation.volume | 1834 | - |
dc.contributor.affiliatedAuthor | Hyung-Nam Song | - |
dc.contributor.affiliatedAuthor | Tae-Yang Jung | - |
dc.contributor.affiliatedAuthor | Sung Goo Park | - |
dc.contributor.affiliatedAuthor | Eui-Jeon Woo | - |
dc.contributor.alternativeName | 박종태 | - |
dc.contributor.alternativeName | 송형남 | - |
dc.contributor.alternativeName | 정태양 | - |
dc.contributor.alternativeName | 이명희 | - |
dc.contributor.alternativeName | 박성구 | - |
dc.contributor.alternativeName | 우의전 | - |
dc.contributor.alternativeName | 박관화 | - |
dc.identifier.bibliographicCitation | Biochimica et Biophysica Acta-Proteins and Proteomics, vol. 1834, no. 1, pp. 380-386 | - |
dc.identifier.doi | 10.1016/j.bbapap.2012.08.001 | - |
dc.subject.keyword | GH13 family | - |
dc.subject.keyword | Hyperthermophilic enzyme | - |
dc.subject.keyword | Maltoheptaose production | - |
dc.subject.keyword | Monomer | - |
dc.subject.keyword | Substrate specificity | - |
dc.subject.local | GH13 family | - |
dc.subject.local | Hyperthermophilic enzyme | - |
dc.subject.local | Maltoheptaose production | - |
dc.subject.local | monomer | - |
dc.subject.local | Monomer | - |
dc.subject.local | Substrate specificity | - |
dc.subject.local | substrate specificity | - |
dc.description.journalClass | Y | - |
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