Linked Life Data

7737423

Source:http://linkedlifedata.com/resource/pubmed/id/7737423

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-6-8
pubmed:abstractText
Incubation of D-amino acid oxidase from the yeast Rhodotorula gracilis with excess dansyl chloride at pH 6.6 and 18 degrees C caused an irreversible inactivation of D-amino acid oxidase. Benzoate, a competitive inhibitor of the enzyme, completely protected the enzyme from inactivation. The dansylated-enzyme, isolated by gel-filtration, was in part still active while the substrate specificity was altered substantially. It was completely reduced by D-alanine in anaerobiosic conditions and did stabilize the red anion semiquinone upon photochemical reduction with EDTA. The results provide evidence for the presence of essential histidyl residue(s) in the active center of the yeast enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
363
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
307-10
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Reactivity of histidyl residues in D-amino acid oxidase from Rhodotorula gracilis.
pubmed:affiliation
Department of General Physiology and Biochemistry, University of Milano, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't