Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 67, Issue 3, Pages 353-368Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-009-0166-4
Keywords
Kynurenic acid; Pyridoxal 5 '-phosphate; Kynurenine; Kynurenine aminotransferase; Aminotransferase; Tryptophan metabolism; Cysteine conjugate beta-lyase; Neurodegeneration
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Funding
- NIDCR and NINDS at NIH [NS063836]
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Kynurenine aminotransferases (KATs) catalyze the synthesis of kynurenic acid (KYNA), an endogenous antagonist of N-methyl-d-aspartate and alpha 7-nicotinic acetylcholine receptors. Abnormal KYNA levels in human brains are implicated in the pathophysiology of schizophrenia, Alzheimer's disease, and other neurological disorders. Four KATs have been reported in mammalian brains, KAT I/glutamine transaminase K/cysteine conjugate beta-lyase 1, KAT II/aminoadipate aminotransferase, KAT III/cysteine conjugate beta-lyase 2, and KAT IV/glutamic-oxaloacetic transaminase 2/mitochondrial aspartate aminotransferase. KAT II has a striking tertiary structure in N-terminal part and forms a new subgroup in fold type I aminotransferases, which has been classified as subgroup I epsilon. Knowledge regarding KATs is vast and complex; therefore, this review is focused on recent important progress of their gene characterization, physiological and biochemical function, and structural properties. The biochemical differences of four KATs, specific enzyme activity assays, and the structural insights into the mechanism of catalysis and inhibition of these enzymes are discussed.
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