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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
49
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pubmed:dateCreated |
1996-1-11
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pubmed:databankReference | |
pubmed:abstractText |
Several aminotransferases with kynurenine aminotransferase (KAT) activity are able to convert L-kynurenine into kynurenic acid, a putative endogenous modulator of glutamatergic neurotransmission. In the rat, one of the described KAT isoforms has been found to correspond to glutamine transaminase K. In addition, rat kidney alpha-aminoadipate aminotransferase (AadAT) also shows KAT activity. In this report, we describe the isolation of a cDNA clone encoding the soluble form of this aminotransferase isoenzyme from rat (KAT/AadAT). Degenerate oligonucleotides were designed from the amino acid sequences of rat kidney KAT/AadAT tryptic peptides for use as primers for reverse transcription-polymerase chain reaction of rat kidney RNA. The resulting polymerase chain reaction fragment was used to screen a rat kidney cDNA library and to isolate a cDNA clone encoding KAT/AadAT. Analysis of the combined DNA sequences indicated the presence of a single 1275-base pair open reading frame coding for a soluble protein of 425 amino acid residues. KAT/AadAT appears to be structurally homologous to aspartate aminotransferase in the pyridoxal 5'-phosphate binding domain. RNA blot analysis of rat tissues, including brain, revealed a single species of KAT/AadAT mRNA of approximately 2.1 kilobases. HEK-293 cells transfected with the KAT/AadAT cDNA exhibited both KAT and AadAT activities with enzymatic properties similar to those reported for the rat native protein.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-Aminoadipate Transaminase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transaminases,
http://linkedlifedata.com/resource/pubmed/chemical/glutamine - phenylpyruvate...,
http://linkedlifedata.com/resource/pubmed/chemical/kynurenine-oxoglutarate transaminase
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
29330-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7493966-2-Aminoadipate Transaminase,
pubmed-meshheading:7493966-Amino Acid Sequence,
pubmed-meshheading:7493966-Animals,
pubmed-meshheading:7493966-Base Sequence,
pubmed-meshheading:7493966-Blotting, Northern,
pubmed-meshheading:7493966-Cloning, Molecular,
pubmed-meshheading:7493966-DNA, Complementary,
pubmed-meshheading:7493966-Kidney,
pubmed-meshheading:7493966-Lyases,
pubmed-meshheading:7493966-Molecular Sequence Data,
pubmed-meshheading:7493966-Rats,
pubmed-meshheading:7493966-Recombinant Proteins,
pubmed-meshheading:7493966-Transaminases
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pubmed:year |
1995
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pubmed:articleTitle |
Cloning and functional expression of a soluble form of kynurenine/alpha-aminoadipate aminotransferase from rat kidney.
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pubmed:affiliation |
Pharma Division, F. Hoffmann-La Roche Ltd., Basel, Switzerland.
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pubmed:publicationType |
Journal Article
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