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PDBsum entry 3pdb

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3pdb
Jmol
Contents
Protein chains
401 a.a. *
Ligands
BME ×7
GOL ×5
OAA
PMP ×2
Waters ×706
* Residue conservation analysis
PDB id:
3pdb
Name: Transferase
Title: Crystal structure of mouse mitochondrial aspartate aminotran complex with oxaloacetic acid
Structure: Aspartate aminotransferase, mitochondrial. Chain: a, c. Synonym: maspat, fatty acid-binding protein, fabp-1, glutam oxaloacetate transaminase 2, plasma membrane-associated fat binding protein, fabppm, transaminase a. Engineered: yes. Aspartate aminotransferase, mitochondrial. Chain: b, d. Synonym: maspat, fatty acid-binding protein, fabp-1, glutam
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: got2. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.40Å     R-factor:   0.178     R-free:   0.190
Authors: Q.Han,H.Robinson,T.Cai,D.A.Tagle,J.Li
Key ref: Q.Han et al. (2011). Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV. Biosci Rep, 31, 323-332. PubMed id: 20977429
Date:
22-Oct-10     Release date:   10-Nov-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 = OAA)
corresponds exactly
+ L-glutamate
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = PMP) matches with 88.24% similarity
   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   7 terms 
  Biological process     L-kynurenine metabolic process   15 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
    reference    
 
 
Biosci Rep 31:323-332 (2011)
PubMed id: 20977429  
 
 
Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV.
Q.Han, H.Robinson, T.Cai, D.A.Tagle, J.Li.
 
  ABSTRACT  
 
Mammalian mAspAT (mitochondrial aspartate aminotransferase) is recently reported to have KAT (kynurenine aminotransferase) activity and plays a role in the biosynthesis of KYNA (kynurenic acid) in rat, mouse and human brains. This study concerns the biochemical and structural characterization of mouse mAspAT. In this study, mouse mAspAT cDNA was amplified from mouse brain first stand cDNA and its recombinant protein was expressed in an Escherichia coli expression system. Sixteen oxo acids were tested for the co-substrate specificity of mouse mAspAT and 14 of them were shown to be capable of serving as co-substrates for the enzyme. Structural analysis of mAspAT by macromolecular crystallography revealed that the cofactor-binding residues of mAspAT are similar to those of other KATs. The substrate-binding residues of mAspAT are slightly different from those of other KATs. Our results provide a biochemical and structural basis towards understanding the overall physiological role of mAspAT in vivo and insight into controlling the levels of endogenous KYNA through modulation of the enzyme in the mouse brain.