Truncation of N- and C-terminal regions of Streptococcus mutans dextranase enhances catalytic activity = 말단부위를 절단한 후 활성이 급격하게 증가하는 구강내 존재하는 덱스트란 분해효소

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dc.contributor.authorYoung Min Kim-
dc.contributor.authorR Shimizu-
dc.contributor.authorH Nakai-
dc.contributor.authorH Mori-
dc.contributor.authorM Okuyama-
dc.contributor.authorS M Kang-
dc.contributor.authorZ Fujimoto-
dc.contributor.authorK Funane-
dc.contributor.authorD Kim-
dc.contributor.authorA Kimura-
dc.date.accessioned2017-04-19T09:24:19Z-
dc.date.available2017-04-19T09:24:19Z-
dc.date.issued2011-
dc.identifier.issn0175-7598-
dc.identifier.uri10.1007/s00253-011-3201-yko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10198-
dc.description.abstractMultiple forms of native and recombinant endo-dextranases (Dexs) of the glycoside hydrolase family (GH) 66 exist. The GH 66 Dex gene from Streptococcus mutans ATCC 25175 (SmDex) was expressed in Escherichia coli. The recombinant full-size (95.4 kDa) SmDex protein was digested to form an 89.8 kDa isoform (SmDex90). The purified SmDex90 was proteolytically degraded to more than seven polypeptides (23-70 kDa) during long storage. The protease-insensitive protein was desirable for the biochemical analysis and utilization of SmDex. GH 66 Dex was predicted to comprise four regions from the N- to C-termini: N-terminal variable region (N-VR), conserved region (CR), glucan-binding site (GBS), and C-terminal variable region (C-VR). Five truncated SmDexs were generated by deleting N-VR, GBS, and/or C-VR. Two truncation-mutant enzymes devoid of C-VR (TM-NCGΔ) or N-VR/C-VR (TM-ΔCGΔ) were catalytically active, thereby indicating that N-VR and C-VR were not essential for the catalytic activity. TM-ΔCGΔ did not accept any further protease-degradation during long storage. TM-NCGΔ and TM-ΔCGΔ enhanced substrate hydrolysis, suggesting that N-VR and C-VR induce hindered substrate binding to the active site.-
dc.publisherSpringer-
dc.titleTruncation of N- and C-terminal regions of Streptococcus mutans dextranase enhances catalytic activity = 말단부위를 절단한 후 활성이 급격하게 증가하는 구강내 존재하는 덱스트란 분해효소-
dc.title.alternativeTruncation of N- and C-terminal regions of Streptococcus mutans dextranase enhances catalytic activity-
dc.typeArticle-
dc.citation.titleApplied Microbiology and Biotechnology-
dc.citation.number2-
dc.citation.endPage339-
dc.citation.startPage329-
dc.citation.volume91-
dc.contributor.affiliatedAuthorYoung Min Kim-
dc.contributor.alternativeName김영민-
dc.contributor.alternativeNameShimizu-
dc.contributor.alternativeNameNakai-
dc.contributor.alternativeNameMori-
dc.contributor.alternativeNameOkuyama-
dc.contributor.alternativeName강민선-
dc.contributor.alternativeNameFujimoto-
dc.contributor.alternativeNameFunane-
dc.contributor.alternativeName김도만-
dc.contributor.alternativeNameKimura-
dc.identifier.bibliographicCitationApplied Microbiology and Biotechnology, vol. 91, no. 2, pp. 329-339-
dc.identifier.doi10.1007/s00253-011-3201-y-
dc.subject.keywordEndo-dextranase-
dc.subject.keywordGlycoside hydrolase family 66-
dc.subject.keywordLimited proteolysis-
dc.subject.keywordTruncation-
dc.subject.localEndo-dextranase-
dc.subject.localendo-dextranase-
dc.subject.localglycoside hydrolase family 66-
dc.subject.localGlycoside hydrolase family 66-
dc.subject.localLimited proteolysis-
dc.subject.localTruncation-
dc.description.journalClassY-
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