Linked Life Data

6764538

Source:http://linkedlifedata.com/resource/pubmed/id/6764538

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1983-10-8
pubmed:abstractText
The active species of aspartase from Escherichia coli is further 3-5 fold activated upon limited proteolysis with trypsin releasing carboxy-terminal peptides as reported previously (N. Yumoto, M. Tokushige, and R. Hayashi. Biochim. Biophys. Acta, 616, 319 (1980) ). Survey of the protease specificity for the activation revealed that subtilisin BPN' and several other proteases having far broader substrate specificity than trypsin also activated the enzyme. The results of sequence analyses revealed that subtilisin BPN' cleaved mainly the serylarginine bond near the carboxy-terminal and released an octapeptide, while trypsin cleaved mainly the arginyltyrosine bond which is just next to the subtilisin cleavage site. These results suggest that the protease-mediated activation does not necessarily require a site-specific peptidyl cleavage, but the cleavage of any bond within a certain region centered at arginine, the eighth residue from the carboxy-terminal, is sufficient.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0031-9325
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
391-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Studies on aspartase VIII. Protease-mediated activation: comparative survey of protease specificity for activation and peptide cleavage.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't