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PDBsum entry 3hlm

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3hlm
Jmol
Contents
Protein chains
401 a.a. *
Ligands
GOL ×6
Waters ×653
* Residue conservation analysis
PDB id:
3hlm
Name: Transferase
Title: Crystal structure of mouse mitochondrial aspartate aminotransferase/kynurenine aminotransferase iv
Structure: Aspartate aminotransferase, mitochondrial. Chain: a, b, c, d. Synonym: maspat, transaminase a, glutamate oxaloacetate tra 2, fatty acid-binding protein, fabp-1, fabppm. Engineered: yes
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: got-2, got2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.184     R-free:   0.234
Authors: Q.Han,H.Robinson,J.Li
Key ref: Q.Han et al. (2010). Structure, expression, and function of kynurenine aminotransferases in human and rodent brains. Cell Mol Life Sci, 67, 353-368. PubMed id: 19826765
Date:
27-May-09     Release date:   02-Jun-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P05202  (AATM_MOUSE) -  Aspartate aminotransferase, mitochondrial
Seq:
Struc:
430 a.a.
401 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 1: E.C.2.6.1.1  - Aspartate transaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
L-aspartate
+ 2-oxoglutarate
=
oxaloacetate
Bound ligand (Het Group name = GOL)
matches with 50.00% similarity
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
   Enzyme class 2: E.C.2.6.1.7  - Kynurenine--oxoglutarate transaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
      Reaction: L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
L-kynurenine
+ 2-oxoglutarate
= 4-(2-aminophenyl)-2,4-dioxobutanoate
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   6 terms 
  Biological process     L-kynurenine metabolic process   15 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
    reference    
 
 
Cell Mol Life Sci 67:353-368 (2010)
PubMed id: 19826765  
 
 
Structure, expression, and function of kynurenine aminotransferases in human and rodent brains.
Q.Han, T.Cai, D.A.Tagle, J.Li.
 
  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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21155972 D.Zádori, P.Klivényi, I.Plangár, J.Toldi, and L.Vécsei (2011).
Endogenous neuroprotection in chronic neurodegenerative disorders: with particular regard to the kynurenines.
  J Cell Mol Med, 15, 701-717.  
  21439022 E.Passera, B.Campanini, F.Rossi, V.Casazza, M.Rizzi, R.Pellicciari, and A.Mozzarelli (2011).
Human kynurenine aminotransferase II - reactivity with substrates and inhibitors.
  FEBS J, 278, 1882-1900.  
20811799 G.F.Oxenkrug (2011).
Interferon-gamma-inducible kynurenines/pteridines inflammation cascade: implications for aging and aging-associated psychiatric and medical disorders.
  J Neural Transm, 118, 75-85.  
20977429 Q.Han, H.Robinson, T.Cai, D.A.Tagle, and J.Li (2011).
Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV.
  Biosci Rep, 31, 323-332.
PDB codes: 3pd6 3pdb
  21153519 P.Mehere, Q.Han, J.A.Lemkul, C.J.Vavricka, H.Robinson, D.R.Bevan, and J.Li (2010).
Tyrosine aminotransferase: biochemical and structural properties and molecular dynamics simulations.
  Protein Cell, 1, 1023-1032.
PDB code: 3pdx
20482848 Q.Han, T.Cai, D.A.Tagle, and J.Li (2010).
Thermal stability, pH dependence and inhibition of four murine kynurenine aminotransferases.
  BMC Biochem, 11, 19.  
20629991 Z.T.Kincses, J.Toldi, and L.Vécsei (2010).
Kynurenines, neurodegeneration and Alzheimer's disease.
  J Cell Mol Med, 14, 2045-2054.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.