Structure, expression, and function of kynurenine aminotransferases in human and rodent brains |
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| Authors: | Qian Han Tao Cai Danilo A Tagle Jianyong Li |
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| Institution: | (1) Department of Biochemistry, Virginia Tech, Blacksburg, VA 24061, USA;(2) OIIB, NIDCR, National Institutes of Health, Bethesda MD, 20892-4322, USA;(3) Neuroscience Center, NINDS, National Institutes of Health, Bethesda, MD 2089-29525, USA; |
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| Abstract: | 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 Iε. 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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