| pubmed-article:21479716 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21479716 | lifeskim:mentions | umls-concept:C0038409 | lld:lifeskim |
| pubmed-article:21479716 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:21479716 | lifeskim:mentions | umls-concept:C0011805 | lld:lifeskim |
| pubmed-article:21479716 | lifeskim:mentions | umls-concept:C1706395 | lld:lifeskim |
| pubmed-article:21479716 | lifeskim:mentions | umls-concept:C1264638 | lld:lifeskim |
| pubmed-article:21479716 | lifeskim:mentions | umls-concept:C0243102 | lld:lifeskim |
| pubmed-article:21479716 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:21479716 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:21479716 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:21479716 | pubmed:dateCreated | 2011-6-29 | lld:pubmed |
| pubmed-article:21479716 | pubmed:abstractText | 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-NCG?) or N-VR/C-VR (TM-?CG?) were catalytically active, thereby indicating that N-VR and C-VR were not essential for the catalytic activity. TM-?CG? did not accept any further protease-degradation during long storage. TM-NCG? and TM-?CG? enhanced substrate hydrolysis, suggesting that N-VR and C-VR induce hindered substrate binding to the active site. | lld:pubmed |
| pubmed-article:21479716 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21479716 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21479716 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21479716 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21479716 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21479716 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21479716 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21479716 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:21479716 | pubmed:issn | 1432-0614 | lld:pubmed |
| pubmed-article:21479716 | pubmed:author | pubmed-author:FujimotoZuiZ | lld:pubmed |
| pubmed-article:21479716 | pubmed:author | pubmed-author:KimuraAtsuoA | lld:pubmed |
| pubmed-article:21479716 | pubmed:author | pubmed-author:KimYoung-MinY... | lld:pubmed |
| pubmed-article:21479716 | pubmed:author | pubmed-author:OkuyamaMasayu... | lld:pubmed |
| pubmed-article:21479716 | pubmed:author | pubmed-author:MoriHaruhideH | lld:pubmed |
| pubmed-article:21479716 | pubmed:author | pubmed-author:NakaiHiroyuki... | lld:pubmed |
| pubmed-article:21479716 | pubmed:author | pubmed-author:KimDomanD | lld:pubmed |
| pubmed-article:21479716 | pubmed:author | pubmed-author:FunaneKazumiK | lld:pubmed |
| pubmed-article:21479716 | pubmed:author | pubmed-author:ShimizuRyokoR | lld:pubmed |
| pubmed-article:21479716 | pubmed:author | pubmed-author:KangMin-SunMS | lld:pubmed |
| pubmed-article:21479716 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21479716 | pubmed:volume | 91 | lld:pubmed |
| pubmed-article:21479716 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21479716 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21479716 | pubmed:pagination | 329-39 | lld:pubmed |
| pubmed-article:21479716 | pubmed:meshHeading | pubmed-meshheading:21479716... | lld:pubmed |
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| pubmed-article:21479716 | pubmed:meshHeading | pubmed-meshheading:21479716... | lld:pubmed |
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| pubmed-article:21479716 | pubmed:meshHeading | pubmed-meshheading:21479716... | lld:pubmed |
| pubmed-article:21479716 | pubmed:meshHeading | pubmed-meshheading:21479716... | lld:pubmed |
| pubmed-article:21479716 | pubmed:meshHeading | pubmed-meshheading:21479716... | lld:pubmed |
| pubmed-article:21479716 | pubmed:meshHeading | pubmed-meshheading:21479716... | lld:pubmed |
| pubmed-article:21479716 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21479716 | pubmed:articleTitle | Truncation of N- and C-terminal regions of Streptococcus mutans dextranase enhances catalytic activity. | lld:pubmed |
| pubmed-article:21479716 | pubmed:affiliation | Research Faculty of Agriculture, Hokkaido University, Kita-9 Nishi-9, Kita-ku, Sapporo 060-8589, Japan. u9897854@kribb.re.kr | lld:pubmed |
| pubmed-article:21479716 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21479716 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
