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Molecular cloning of rat kynurenine aminotransferase: identity with glutamine transaminase K.
BioScience Center, Pharmacia Research Center, Nerviano, Italy.
The enzyme kynurenine aminotransferase (KAT) catalyses the conversion of L-kynurenine to kynurenic acid. A combination of polymerase chain reaction techniques and hybridization screening was used to isolate a cDNA clone encompassing the entire coding region of KAT from rat kidney. Identification of the cDNA as coding for KAT was based both on the comparison of amino acid sequences obtained from purified rat KAT and on the expression of KAT activity in COS-1 cells transfected with the cDNA. RNA blot analysis indicated that KAT mRNA is widely expressed in rat tissues. Cultured cells transfected with the cDNA for KAT also showed glutamine transaminase K activity. Based mainly on sequence data, these results demonstrate that rat kidney KAT is identical with glutamine transaminase K.
PMID: 7926014 [PubMed - indexed for MEDLINE]
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Cited by 4 PubMed Central articles
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Biochemical and phenotypic abnormalities in kynurenine aminotransferase II-deficient mice.
Yu P, Di Prospero NA, Sapko MT, Cai T, Chen A, Melendez-Ferro M, Du F, Whetsell WO Jr, Guidetti P, Schwarcz R, et al.
Mol Cell Biol. 2004 Aug; 24(16):6919-30.
[Mol Cell Biol. 2004]
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Xanthurenic acid translocates proapoptotic Bcl-2 family proteins into mitochondria and impairs mitochondrial function.
Malina HZ, Hess OM.
BMC Cell Biol. 2004 Apr 6; 5:14. Epub 2004 Apr 6.
[BMC Cell Biol. 2004]
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Kynurenine aminotransferase and glutamine transaminase K of Escherichia coli: identity with aspartate aminotransferase.
Han Q, Fang J, Li J.
Biochem J. 2001 Dec 15; 360(Pt 3):617-23.
[Biochem J. 2001]
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