PDBsum entry 2r5e

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protein ligands Protein-protein interface(s) links
Transferase PDB id
Protein chains
419 a.a. *
QLP ×2
Waters ×584
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Aedes kynurenine aminotransferase in complex with glutamine
Structure: Kynurenine aminotransferase. Chain: a, b. Engineered: yes
Source: Aedes aegypti. Yellow fever mosquito. Organism_taxid: 7159. Strain: liverpool. Gene: kat. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
1.84Å     R-factor:   0.203     R-free:   0.243
Authors: Q.Han,Y.G.Gao,H.Robinson,J.Li
Key ref: Q.Han et al. (2008). Structural insight into the mechanism of substrate specificity of aedes kynurenine aminotransferase. Biochemistry, 47, 1622-1630. PubMed id: 18186649
03-Sep-07     Release date:   18-Mar-08    
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Protein chains
Pfam   ArchSchema ?
Q95VY4  (Q95VY4_AEDAE) -  Kynurenine aminotransferase
477 a.a.
419 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     biosynthetic process   1 term 
  Biochemical function     catalytic activity     4 terms  


Biochemistry 47:1622-1630 (2008)
PubMed id: 18186649  
Structural insight into the mechanism of substrate specificity of aedes kynurenine aminotransferase.
Q.Han, Y.G.Gao, H.Robinson, J.Li.
Aedes aegypti kynurenine aminotransferase (AeKAT) is a multifunctional aminotransferase. It catalyzes the transamination of a number of amino acids and uses many biologically relevant alpha-keto acids as amino group acceptors. AeKAT also is a cysteine S-conjugate beta-lyase. The most important function of AeKAT is the biosynthesis of kynurenic acid, a natural antagonist of NMDA and alpha7-nicotinic acetylcholine receptors. Here, we report the crystal structures of AeKAT in complex with its best amino acid substrates, glutamine and cysteine. Glutamine is found in both subunits of the biological dimer, and cysteine is found in one of the two subunits. Both substrates form external aldemines with pyridoxal 5-phosphate in the structures. This is the first instance in which one pyridoxal 5-phosphate enzyme has been crystallized with cysteine or glutamine forming external aldimine complexes, cysteinyl aldimine and glutaminyl aldimine. All the units with substrate are in the closed conformation form, and the unit without substrate is in the open form, which suggests that the binding of substrate induces the conformation change of AeKAT. By comparing the active site residues of the AeKAT-cysteine structure with those of the human KAT I-phenylalanine structure, we determined that Tyr286 in AeKAT is changed to Phe278 in human KAT I, which may explain why AeKAT transaminates hydrophilic amino acids more efficiently than human KAT I does.

Literature references that cite this PDB file's key reference

  PubMed id Reference
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
19826765 Q.Han, T.Cai, D.A.Tagle, and J.Li (2010).
Structure, expression, and function of kynurenine aminotransferases in human and rodent brains.
  Cell Mol Life Sci, 67, 353-368.
PDB code: 3hlm
19029248 Q.Han, H.Robinson, T.Cai, D.A.Tagle, and J.Li (2009).
Biochemical and structural properties of mouse kynurenine aminotransferase III.
  Mol Cell Biol, 29, 784-793.
PDB codes: 3e2f 3e2y 3e2z
19338303 Q.Han, H.Robinson, T.Cai, D.A.Tagle, and J.Li (2009).
Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K.
  J Med Chem, 52, 2786-2793.
PDB codes: 3fvs 3fvu 3fvx
18950711 F.Rossi, R.Schwarcz, and M.Rizzi (2008).
Curiosity to kill the KAT (kynurenine aminotransferase): structural insights into brain kynurenic acid synthesis.
  Curr Opin Struct Biol, 18, 748-755.  
18620547 Q.Han, T.Cai, D.A.Tagle, H.Robinson, and J.Li (2008).
Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II.
  Biosci Rep, 28, 205-215.
PDB code: 3dc1
18537204 R.Pellicciari, F.Venturoni, D.Bellocchi, A.Carotti, M.Marinozzi, A.Macchiarulo, L.Amori, and R.Schwarcz (2008).
Sequence variants in kynurenine aminotransferase II (KAT II) orthologs determine different potencies of the inhibitor S-ESBA.
  ChemMedChem, 3, 1199-1202.  
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.