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TitleCharacterization of kynurenine aminotransferase from hyperthermophilic archaeon: enzymatic activity for conversion to kynurenic acid is allosterically regulated by alpha-ketoglutaric acid cooperatively with kynurenine
Journal, issue, pagesTo be Published
Publish dateOct 7, 2010 (structure data deposition date)
AuthorsOkada, K. / Angkawidjaja, C. / Koga, Y. / Takano, K. / Kanaya, Y.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.56 - 1.72 Å
Structure data

PDB-3aov:
Crystal structure of Pyrococcus horikoshii kynurenine aminotransferase in complex with PLP
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

PDB-3aow:
Crystal structure of Pyrococcus horikoshii kynurenine aminotransferase in complex with AKG
Method: X-RAY DIFFRACTION / Resolution: 1.56 Å

PDB-3ath:
Crystal structure of Pyrococcus horikoshii kynurenine aminotransferase in complex with four AKGs as substrates and allosteric effectors
Method: X-RAY DIFFRACTION / Resolution: 1.69 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-HOH:
WATER

ChemComp-AKG:
2-OXOGLUTARIC ACID

Source
  • pyrococcus horikoshii (archaea)
KeywordsTRANSFERASE / Protein-PLP complex / Schiff-base linkage / Kynurenin aminotransferase / Cofactor complex / aminotransferase / PLP binding / Transamination / Protein-PLP-AKG triple complex / Kynurenine aminotransferase / Cofactor and substrate complex / cofactor-substrate-allosteric effector complex / 2OG binding / cytosol

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