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PDBsum entry 3hlm
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References listed in PDB file
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Key reference
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Title
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Structure, Expression, And function of kynurenine aminotransferases in human and rodent brains.
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Authors
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Q.Han,
T.Cai,
D.A.Tagle,
J.Li.
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Ref.
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Cell Mol Life Sci, 2010,
67,
353-368.
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PubMed id
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Abstract
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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
Iepsilon. 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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