Linked Life Data

2189788

Source:http://linkedlifedata.com/resource/pubmed/id/2189788

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1990-7-12
pubmed:abstractText
Adenoviruses (Ad) synthesize serine-center endoproteinases (AdEPs) responsible for maturation cleavages within the virus particle. Many questions regarding these enzymes remain unanswered because previous studies utilized crude cells or viral lysates as the enzyme source. Here, we report on the comparison of the amino acid (aa) sequences of several AdEPs and on the expression of the cDNA of the Ad2Ep in Escherichia coli. The AdEPs consist of about 200 aa and their size is around 23 kDa. Among the seven sequences known, 60% of aa were strictly conserved. The usual serine proteinase active site sequence, GDSGG, is absent. The recombinant Ad2EP, produced by an inducible vector as a protein-A fusion product is capable of autocatalytic cleavage, and of cleaving its natural viral substrates as well as foreign proteins. Therefore, other viral proteins or mammalian specific post-translational modifications are not required for enzyme activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
88
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
269-73
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Adenovirus proteinases: comparison of amino acid sequences and expression of the cloned cDNA in Escherichia coli.
pubmed:affiliation
Department of Microbiology, Faculty of Medicine, University of Sherbrooke, Québec, Canada.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't