||Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).
|Gene References into Functions
- Immunohistochemical analysis revealed the presence of KAT I, II, and III in all examined corneal sections. PMID: 28706436
- he optimised method of protein production provides a fast and reliable technique to generate large quantities of active human KAT2 suitable for future small-molecule lead compound screening and structural design work. PMID: 26773745
- Participants with major depression had lower levels of kynurenine compared to controls, with intermediate concentrations in somatoform patients. PMID: 24140252
- Somatization is characterized by disorders in kynurenine aminotransferase activity and an increased neurotoxic potential PMID: 21712776
- 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 PMID: 21473761
- analysis of the crystal structure of kynurenine aminotransferase II PMID: 18056995
- analysis of the crystal structure of human kynurenine aminotransferase II PMID: 18056996
- A human cDNA encodes a 425-residue protein with a mitochondrial cleavage signal and a pyridoxal-phosphate binding site, ~70% identical to the mouse and rat AADAT orthologs. Bacterial expression studies confirm that the gene encodes AADAT activity. PMID: 12126930
||Class-I pyridoxal-phosphate-dependent aminotransferase family
||Higher expression in the liver. Also found in heart, brain, kidney, pancreas, prostate, testis and ovary.