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Aminoadipate aminotransferase

kynurenine aminotransferase II, KAT2, alpha-aminoadipate aminotransferase, 2-Aminoadipate Transaminase, AadAT
This gene encodes a protein that is highly similar to mouse and rat kynurenine aminotransferase II. The rat protein is a homodimer with two transaminase activities. One activity is the transamination of alpha-aminoadipic acid, a final step in the saccaropine pathway which is the major pathway for L-lysine catabolism. The other activity involves the transamination of kynurenine to produce kynurenine acid, the precursor of kynurenic acid which has neuroprotective properties. Two alternative transcripts encoding the same isoform have been identified, however, additional alternative transcripts and isoforms may exist. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, KAT1, HAD, CAN, V1a
Papers on kynurenine aminotransferase II
Inhibition of kynurenine aminotransferase II reduces activity of midbrain dopamine neurons.
Engberg et al., Stockholm, Sweden. In Neuropharmacology, Mar 2016
Kynurenic acid (KYNA), a neuroactive metabolite of tryptophan, is elevated in the brain of patients with psychotic disorders.
Expression, purification and crystallization of human Kynurenine Aminotransferase 2 exploiting a highly optimized codon set.
Church et al., Sydney, Australia. In Protein Expr Purif, Feb 2016
Reducing KYNA production through inhibiting kynurenine aminotransferase 2 (KAT2) would be a promising approach to understanding and treating the related neurological and mental disorders.
Efficient gene-targeting in rat embryonic stem cells by CRISPR/Cas and generation of human kynurenine aminotransferase II (KAT II) knock-in rat.
Takeyama et al., Fujisawa, Japan. In Transgenic Res, Dec 2015
The relative proportion of kynurenine aminotransferase (KAT) I-IV activities in the brain is similar between humans and rats.
Challenges and Opportunities in the Discovery of New Therapeutics Targeting the Kynurenine Pathway.
Verhoest et al., Colorado Springs, United States. In J Med Chem, Dec 2015
Recent studies have focused on three enzymes in this pathway: indoleamine dioxygenase (IDO1), kynurenine monooxygenase (KMO), and kynurenine aminotransferase II (KAT II).
Absence of aryl hydrocarbon receptors increases endogenous kynurenic acid levels and protects mouse brain against excitotoxic insult and oxidative stress.
Segovia et al., Mexico. In J Neurosci Res, Sep 2015
L-kynurenine (Kyn) is a key element of tryptophan metabolism; it is enzymatically converted by kynurenine aminotransferase II (KAT II) to kynurenic acid (KYNA), which acts as an antagonist to the NMDA receptor-glycine site.
CmWRKY15 Facilitates Alternaria tenuissima Infection of Chrysanthemum.
Chen et al., Nanjing, China. In Plos One, 2014
NCED3A, NCED3B, GTG1, AKT1, AKT2, KAT1, KAT2, and KC1were compared between transgenic plants and controls.
Knockout of the two evolutionarily conserved peroxisomal 3-ketoacyl-CoA thiolases in Arabidopsis recapitulates the abnormal inflorescence meristem 1 phenotype.
Smith et al., Potsdam, Germany. In J Exp Bot, 2014
KAT2 and KAT5 are present throughout angiosperms whereas KAT1 is a Brassicaceae-specific duplication of KAT2 expressed at low levels in Arabidopsis.
Genetic polymorphisms associated with the inflammatory response in bacterial meningitis.
Agnez-Lima et al., Natal, Brazil. In Bmc Med Genet, 2014
In recent papers published by our group, we described the associations between the single nucleotide polymorphisms (SNPs) AADAT +401C > T, APEX1 Asn148Glu, OGG1 Ser326Cys and PARP1 Val762Ala and BM.
CPK13, a noncanonical Ca2+-dependent protein kinase, specifically inhibits KAT2 and KAT1 shaker K+ channels and reduces stomatal opening.
Xiong et al., Cambodia. In Plant Physiol, 2014
We provide evidence that CPK13 (1) specifically phosphorylates peptide arrays featuring Arabidopsis K(+) Channel KAT2 and KAT1 polypeptides, (2) inhibits KAT2 and/or KAT1 when expressed in Xenopus laevis oocytes, and (3) closely interacts in plant cells with KAT2 channels (Förster resonance energy transfer-fluorescence lifetime imaging microscopy).
Reduction of brain kynurenic acid improves cognitive function.
Castner et al., New Haven, United States. In J Neurosci, 2014
To address this issue, we identified PF-04859989, a brain-penetrable inhibitor of kynurenine aminotransferase II (KAT II), the enzyme responsible for most brain KYNA synthesis.
Modulation by kynurenine of extracellular kynurenate and glutamate in cerebral cortex of rats with acute liver failure.
Albrecht et al., Warsaw, Poland. In Pharmacol Rep, 2014
The expression of mRNA coding for kynurenine aminotransferase II (KAT-II), the astrocytic enzyme converting KYN to KYNA, was assayed by real-time PCR.
The kynurenine pathway is involved in bacterial meningitis.
Agnez-Lima et al., In J Neuroinflammation, 2013
Previously, the KP was shown to be activated in animal models of BM, and the association of the SNP AADAT + 401C/T (kynurenine aminotransferase II - KAT II) with the host immune response to BM has been described.
AtKC1 is a general modulator of Arabidopsis inward Shaker channel activity.
Véry et al., Montpellier, France. In Plant J, 2011
KAT2 was able to re-locate AtKC1 fused to GFP from endomembranes to the plasma membrane, indicating that heteromeric AtKC1-KAT2 channels are efficiently targeted to the plasma membrane.
Arabidopsis 3-ketoacyl-CoA thiolase-2 (KAT2), an enzyme of fatty acid β-oxidation, is involved in ABA signal transduction.
Zhang et al., Beijing, China. In Plant Cell Physiol, 2011
KAT2 may function downstream of an important WRKY transcription repressor WRKY40, which may link KAT2 with the ABA receptor ABAR/CHLH-mediated signaling.
Association of kynurenine aminotransferase II gene C401T polymorphism with immune response in patients with meningitis.
Agnez-Lima et al., Natal, Brazil. In Bmc Med Genet, 2010
association of SNP AADAT+401C/T with the host immune response to bacterial meningitis, suggesting that this SNP may affect the host ability in recruitment of leukocytes to the infection site
Somatization, but not depression, is characterized by disorders in the tryptophan catabolite (TRYCAT) pathway, indicating increased indoleamine 2,3-dioxygenase and lowered kynurenine aminotransferase activity.
Rief et al., Bangkok, Thailand. In Neuro Endocrinol Lett, 2010
Somatization is characterized by disorders in kynurenine aminotransferase activity and an increased neurotoxic potential
Thermal stability, pH dependence and inhibition of four murine kynurenine aminotransferases.
Li et al., Blacksburg, United States. In Bmc Biochem, 2009
The activity of mouse KAT II was not significantly inhibited by any proteinogenic amino acids at equimolar concentrations and half-life was 27.4 minutes at 65 degree C.
The guard cell as a single-cell model towards understanding drought tolerance and abscisic acid action.
Leung et al., Gif-sur-Yvette, France. In J Exp Bot, 2008
In Arabidopsis, the reference for guard cell genetics, stomatal opening driven by K(+) entry is mainly through KAT1 and KAT2, two voltage-gated K(+) inward-rectifying channels that are activated on hyperpolarization of the plasma membrane principally by the OST2 H(+)-ATPase (proton pump coupled to ATP hydrolysis).
Pharmacological manipulation of kynurenic acid: potential in the treatment of psychiatric disorders.
Engberg et al., Stockholm, Sweden. In Cns Drugs, 2008
Thus, decreased endogenous levels of rat brain KYNA have been found to reduce firing of these neurons, and mice with a targeted deletion of kynurenine aminotransferase II display low endogenous brain KYNA levels concomitant with an increased performance in cognitive tests.
The role of glutamine transaminase K (GTK) in sulfur and alpha-keto acid metabolism in the brain, and in the possible bioactivation of neurotoxicants.
Cooper, White Plains, United States. In Neurochem Int, 2004
KAT I and KAT II are identical to GTK and alpha-aminoadipate aminotransferase, respectively.
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