DC Field | Value | Language |
---|---|---|
dc.contributor.author | Young Min Kim | - |
dc.contributor.author | R Shimizu | - |
dc.contributor.author | H Nakai | - |
dc.contributor.author | H Mori | - |
dc.contributor.author | M Okuyama | - |
dc.contributor.author | S M Kang | - |
dc.contributor.author | Z Fujimoto | - |
dc.contributor.author | K Funane | - |
dc.contributor.author | D Kim | - |
dc.contributor.author | A Kimura | - |
dc.date.accessioned | 2017-04-19T09:24:19Z | - |
dc.date.available | 2017-04-19T09:24:19Z | - |
dc.date.issued | 2011 | - |
dc.identifier.issn | 0175-7598 | - |
dc.identifier.uri | 10.1007/s00253-011-3201-y | ko |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/10198 | - |
dc.description.abstract | Multiple 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.publisher | Springer | - |
dc.title | Truncation 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.alternative | Truncation of N- and C-terminal regions of Streptococcus mutans dextranase enhances catalytic activity | - |
dc.type | Article | - |
dc.citation.title | Applied Microbiology and Biotechnology | - |
dc.citation.number | 2 | - |
dc.citation.endPage | 339 | - |
dc.citation.startPage | 329 | - |
dc.citation.volume | 91 | - |
dc.contributor.affiliatedAuthor | Young Min Kim | - |
dc.contributor.alternativeName | 김영민 | - |
dc.contributor.alternativeName | Shimizu | - |
dc.contributor.alternativeName | Nakai | - |
dc.contributor.alternativeName | Mori | - |
dc.contributor.alternativeName | Okuyama | - |
dc.contributor.alternativeName | 강민선 | - |
dc.contributor.alternativeName | Fujimoto | - |
dc.contributor.alternativeName | Funane | - |
dc.contributor.alternativeName | 김도만 | - |
dc.contributor.alternativeName | Kimura | - |
dc.identifier.bibliographicCitation | Applied Microbiology and Biotechnology, vol. 91, no. 2, pp. 329-339 | - |
dc.identifier.doi | 10.1007/s00253-011-3201-y | - |
dc.subject.keyword | Endo-dextranase | - |
dc.subject.keyword | Glycoside hydrolase family 66 | - |
dc.subject.keyword | Limited proteolysis | - |
dc.subject.keyword | Truncation | - |
dc.subject.local | Endo-dextranase | - |
dc.subject.local | endo-dextranase | - |
dc.subject.local | glycoside hydrolase family 66 | - |
dc.subject.local | Glycoside hydrolase family 66 | - |
dc.subject.local | Limited proteolysis | - |
dc.subject.local | Truncation | - |
dc.description.journalClass | Y | - |
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