Linked Life Data

7987263

Source:http://linkedlifedata.com/resource/pubmed/id/7987263

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-1-12
pubmed:abstractText
D-amino acid oxidase from the yeast Rhodotorula gracilis is irreversibly inactivated by reaction with TNBS with complete inactivation accompanied by covalent modification of lysine residues of the protein. The inactivation was biphasic, the fast phase being dependent on TNBS concentration and completed in less than 1 minute. The competitive inhibitor benzoate afforded partial protection against inactivation during the fast phase of the process, with no effect on the slow phase. The pH curve of inactivation (slow phase) indicates the involvement of a residue(s) with a pK of 8.2. Amino acid analyses showed that in the fast phase of inactivation 1.6 lysine residues were modified, whereas up to 13 lysine residues were modified in the slow phase of inactivation. Our data show that TNBS behaves as an active site-directed reagent in yeast D-amino acid oxidase and they suggest the presence of at least one essential lysyl residue at or near the active site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
947-55
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Chemical modification of lysyl residues of Rhodotorula gracilis D-amino acid oxidase.
pubmed:affiliation
Department of General Physiology and Biochemistry, University of Milano, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't