Linked Life Data

9832617

Source:http://linkedlifedata.com/resource/pubmed/id/9832617

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1999-3-9
pubmed:abstractText
Saccharomyces cerevisiae bearing a lipase cDNA from Fusarium heterosporum produced two lipases, A and B. Lipase B was significantly more stable to temperature than lipase A, but their optimum temperatures were similar. Lipase B was composed of one polypeptide (301 amino acids), and lipase A was composed of two polypeptides (275 and 26 amino acids) generated by the cleavage between Arg275 and Asp276 with a trypsin-like protease. It was suggested that the C-terminal peptide (26 amino acids) tightened the lipase structure when bound to the catalytic domain (275 amino acids) through a peptide bond. The tight structure was loosened by cleavage of the C-terminal peptide, even though the peptide interacted noncovalently with the catalytic domain, possibly through charged amino acids, in which it is rich. Deletion of the C-terminal peptide greatly decreased the lipase production by the recombinant S. cerevisiae, although its transcriptional level was the same as that of cells carrying the wild-type gene. These facts suggested that the C-terminal peptide affected the lipase production in the post-transcriptional step.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
124
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1124-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
C-terminal peptide of fusarium heterosporum lipase is necessary for its increasing thermostability.
pubmed:affiliation
Osaka Municipal Technical Research Institute, Joto-ku, Osaka, 536-8553, Japan. nagao@omtri.osaka.city.jp
pubmed:publicationType
Journal Article