Crystal structures of Aedes aegypti kynurenine aminotransferase

@article{Han2005CrystalSO,
  title={Crystal structures of Aedes aegypti kynurenine aminotransferase},
  author={Qian Han and Yi Gui Gao and Howard H Robinson and Haizhen Ding and Scott R. Wilson and Jianyong Li},
  journal={The FEBS Journal},
  year={2005},
  volume={272}
}
Aedes aegypti kynurenine aminotransferase (AeKAT) catalyzes the irreversible transamination of kynurenine to kynurenic acid, the natural antagonist of NMDA and 7‐nicotinic acetycholine receptors. Here, we report the crystal structure of AeKAT in its PMP and PLP forms at 1.90 and 1.55 Å, respectively. The structure was solved by a combination of single‐wavelength anomalous dispersion and molecular replacement approaches. The initial search model in the molecular replacement method was built with… 
Structural insight into the mechanism of substrate specificity of aedes kynurenine aminotransferase.
TLDR
The crystal structures of AeKAT in complex with its best amino acid substrates, glutamine and cysteine are reported, which 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 a Aldimine.
Crystal Structures of Aedes aegypti Alanine Glyoxylate Aminotransferase*
TLDR
Comparison of the AeAGT-alanine structure with that of the Anopheles HKT-inhibitor complex suggests that a Ser-Asn-Phe motif in the latter may be responsible for the substrate specificity of HKT enzymes for 3-HK.
Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K.
TLDR
The hKAT/IAC complex structure reveals that the binding moieties of the inhibitor are its indole ring and a carboxyl group, and the discovery of two different ligands located simultaneously in the hKKAT I active center for the first time.
Curiosity to kill the KAT (kynurenine aminotransferase): structural insights into brain kynurenic acid synthesis.
Crystal Structure of Human Kynurenine Aminotransferase II, a Drug Target for the Treatment of Schizophrenia*
TLDR
The structure of human KAT II is solved by means of the single-wavelength anomalous dispersion method at 2.3-Å resolution and reveals a novel antiparallel strand-loop-strand motif that forms an unprecedented intersubunit β-sheet in the functional hKAT II dimer.
Structure, expression, and function of kynurenine aminotransferases in human and rodent brains
TLDR
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.
Thermal stability, pH dependence and inhibition of four murine kynurenine aminotransferases
TLDR
The characteristics reported here could be used to develop specific assay methods for each of the four murine KATs and identify which KAT is affected in mouse models for research and to develop small molecule drugs for prevention and treatment of KAT-involved human diseases.
Biochemical and Structural Properties of Mouse Kynurenine Aminotransferase III
TLDR
It is established that mKAT III is able to efficiently catalyze the transamination of kynurenine to KYNA and has optimum activity at relatively basic conditions of around pH 9.0 and at relatively high temperatures of 50 to 60°C.
Cloning and molecular characterization of tick kynurenine aminotransferase (HlKAT) from Haemaphysalis longicornis (Acari: Ixodidae)
TLDR
Results suggested that a specific HlKAT is present in tick and Hl kynurenine aminotransferase may play an important physiological role in H. longicornis.
Crystal Structure of MJ0684 from Methanococcus jannaschii, a Novel Archaeal Homolog of Kynurenine Aminotransferase
TLDR
Structural observations imply that MJ0684 is a novel archaeal homolog of the subfamily Iγ kynurenine aminotransferase.
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TLDR
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TLDR
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