3HLM
Crystal Structure of Mouse Mitochondrial Aspartate Aminotransferase/Kynurenine Aminotransferase IV
Summary for 3HLM
| Entry DOI | 10.2210/pdb3hlm/pdb |
| Descriptor | Aspartate aminotransferase, mitochondrial, GLYCEROL (3 entities in total) |
| Functional Keywords | alpha & beta protein, plp-dependent transferase, aminotransferase, multifunctional enzyme, pyridoxal phosphate, acetylation, cell membrane, lipid transport, membrane, mitochondrion, nitration, phosphoprotein, transferase, transit peptide, transport |
| Biological source | Mus musculus (mouse) |
| Cellular location | Mitochondrion matrix: P05202 |
| Total number of polymer chains | 4 |
| Total formula weight | 180016.94 |
| Authors | Han, Q.,Robinson, H.,Li, J. (deposition date: 2009-05-27, release date: 2010-06-02, Last modification date: 2023-11-22) |
| Primary citation | Han, Q.,Cai, T.,Tagle, D.A.,Li, J. Structure, expression, and function of kynurenine aminotransferases in human and rodent brains. Cell.Mol.Life Sci., 67:353-368, 2010 Cited by PubMed 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 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. PubMed: 19826765DOI: 10.1007/s00018-009-0166-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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