Linked Life Data

14565460

Source:http://linkedlifedata.com/resource/pubmed/id/14565460

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5-8
pubmed:dateCreated
2003-10-20
pubmed:abstractText
In order to design new efficient cytidine based drugs, an intersubunit interactions study related to the active site has been performed on the wild-type cytidine deaminase (CDA) and on the mutant enzyme F137W/W113F. F137 is the homologous to the Bacillus subtilis CDA F125 involved in the subunit interactions. In presence of the dissociating agent SDS, wild-type human CDA dissociate into enzymatically inactive monomers without intermediate forms via a non-cooperative transition. Extensive dialysis or dilution of the inactivated monomers restores completely the activity. The presence of the strong human CDA competitive inhibitor 5-fluorozebularine disfavour dissociation of the tetramer into subunits in the wild-type CDA but not in mutant enzyme F137W/W113F.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1525-7770
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1535-8
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:articleTitle
Intersubunit interactions in human cytidine deaminase.
pubmed:affiliation
Dipartimento di Scienze Veterinarie, University of Camerino, Matelica (MC), Italy.
pubmed:publicationType
Journal Article