Linked Life Data

21479716

Source:http://linkedlifedata.com/resource/pubmed/id/21479716

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2011-6-29
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1432-0614
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
329-39
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Truncation of N- and C-terminal regions of Streptococcus mutans dextranase enhances catalytic activity.
pubmed:affiliation
Research Faculty of Agriculture, Hokkaido University, Kita-9 Nishi-9, Kita-ku, Sapporo 060-8589, Japan. u9897854@kribb.re.kr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't