Linked Life Data

21439022

Source:http://linkedlifedata.com/resource/pubmed/id/21439022

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2011-5-18
pubmed:abstractText
Kynurenine aminotransferase (KAT) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the conversion of kynurenine, an intermediate of the tryptophan degradation pathway, into kynurenic acid, an endogenous antagonist of ionotropic excitatory amino acid receptors in the central nervous system. KATII is the prevalent isoform in mammalian brain and a drug target for the treatment of schizophrenia. We have carried out a spectroscopic and functional characterization of both the human wild-type KATII and a variant carrying the active site mutation Tyr142?Phe. The transamination and the ?-lytic activity of KATII towards the substrates kynurenine and ?-aminoadipate, the substrate analog ?-chloroalanine and the inhibitors (R)-2-amino-4-(4-(ethylsulfonyl))-4-oxobutanoic acid and cysteine sulfinate were investigated with both conventional assays and a novel continuous spectrophotometric assay. Furthermore, for high-throughput KATII inhibitor screenings, an endpoint assay suitable for 96-well plates was also developed and tested. The availability of these assays and spectroscopic analyses demonstrated that (R)-2-amino-4-(4-(ethylsulfonyl))-4-oxobutanoic acid and cysteine sulfinate, reported to be KATII inhibitors, are poor substrates that undergo slow transamination.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1742-4658
pubmed:author
pubmed:copyrightInfo
© 2011 The Authors Journal compilation © 2011 FEBS.
pubmed:issnType
Electronic
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1882-900
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Human kynurenine aminotransferase II--reactivity with substrates and inhibitors.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, University of Parma, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't