3hlm

Crystal Structure of Mouse Mitochondrial Aspartate Aminotransferase/Kynurenine Aminotransferase IVCrystal Structure of Mouse Mitochondrial Aspartate Aminotransferase/Kynurenine Aminotransferase IV

Structural highlights

3hlm is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AATM_MOUSE Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structure, expression, and function of kynurenine aminotransferases in human and rodent brains.,Han Q, Cai T, Tagle DA, Li J Cell Mol Life Sci. 2010 Feb;67(3):353-68. Epub 2009 Oct 15. PMID:19826765^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Han Q, Robinson H, Cai T, Tagle DA, Li J. Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV. Biosci Rep. 2010 Oct 26. PMID:20977429 doi:10.1042/BSR20100117
↑ Zhou SL, Stump D, Kiang CL, Isola LM, Berk PD. Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-L1 adipocytes mediates saturable fatty acid uptake. Proc Soc Exp Biol Med. 1995 Mar;208(3):263-70. PMID:7878064
↑ Han Q, Cai T, Tagle DA, Li J. Structure, expression, and function of kynurenine aminotransferases in human and rodent brains. Cell Mol Life Sci. 2010 Feb;67(3):353-68. Epub 2009 Oct 15. PMID:19826765 doi:10.1007/s00018-009-0166-4

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Han Q, Robinson H, Cai T, Tagle DA, Li J. Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV. Biosci Rep. 2010 Oct 26. PMID:20977429 doi:10.1042/BSR20100117

[2] Zhou SL, Stump D, Kiang CL, Isola LM, Berk PD. Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-L1 adipocytes mediates saturable fatty acid uptake. Proc Soc Exp Biol Med. 1995 Mar;208(3):263-70. PMID:7878064

[3] Han Q, Cai T, Tagle DA, Li J. Structure, expression, and function of kynurenine aminotransferases in human and rodent brains. Cell Mol Life Sci. 2010 Feb;67(3):353-68. Epub 2009 Oct 15. PMID:19826765 doi:10.1007/s00018-009-0166-4

[1]

[2]

[3]