Enzymes
| UniProtKB help_outline | 5 proteins |
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- Name help_outline 2-oxobutanoate Identifier CHEBI:16763 (Beilstein: 3601760) help_outline Charge -1 Formula C4H5O3 InChIKeyhelp_outline TYEYBOSBBBHJIV-UHFFFAOYSA-M SMILEShelp_outline CCC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 33 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-kynurenine Identifier CHEBI:57959 Charge 0 Formula C10H12N2O3 InChIKeyhelp_outline YGPSJZOEDVAXAB-QMMMGPOBSA-N SMILEShelp_outline Nc1ccccc1C(=O)C[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 34 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2S)-2-aminobutanoate Identifier CHEBI:74359 Charge 0 Formula C4H9NO2 InChIKeyhelp_outline QWCKQJZIFLGMSD-VKHMYHEASA-N SMILEShelp_outline CC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 15 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline kynurenate Identifier CHEBI:58454 Charge -1 Formula C10H6NO3 InChIKeyhelp_outline HCZHHEIFKROPDY-UHFFFAOYSA-M SMILEShelp_outline Oc1cc(nc2ccccc12)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 19 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:66044 | RHEA:66045 | RHEA:66046 | RHEA:66047 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Cloning and functional expression of a soluble form of kynurenine/alpha-aminoadipate aminotransferase from rat kidney.
Buchli R., Alberati-Giani D., Malherbe P., Koehler C., Broger C., Cesura A.M.
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 ... >> More
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. << Less
J. Biol. Chem. 270:29330-29335(1995) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.
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Cysteine and keto acids modulate mosquito kynurenine aminotransferase catalyzed kynurenic acid production.
Han Q., Li J.
Kynurenine aminotransferase (KAT) catalyzes the formation of kynurenic acid (KYNA), the natural antagonist of ionotropic glutamate receptors. This study tests potential substrates and assesses the effects of amino acids and keto acids on the activity of mosquito KAT. Various keto acids, when simul ... >> More
Kynurenine aminotransferase (KAT) catalyzes the formation of kynurenic acid (KYNA), the natural antagonist of ionotropic glutamate receptors. This study tests potential substrates and assesses the effects of amino acids and keto acids on the activity of mosquito KAT. Various keto acids, when simultaneously present in the same reaction mixture, display a combined effect on KAT catalyzed KYNA production. Moreover, methionine and glutamine show inhibitory effects on KAT activity, while cysteine functions as either an antagonist or an inhibitor depending on the concentration. Therefore, the overall level of keto acids and cysteine might modulate the KYNA synthesis. Results from this study will be useful in the study of KAT regulation in other animals. << Less
FEBS Lett. 577:381-385(2004) [PubMed] [EuropePMC]
This publication is cited by 28 other entries.
Comments
Mutli-step reaction: RHEA:66048 + RHEA:42452