Literature summary extracted from
Han, Q.; Robinson, H.; Li, J.
Crystal structure of human kynurenine aminotransferase II (2008), J. Biol. Chem., 283, 3567-3573.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.6.1.7 |
expression in Escherichia coli |
Homo sapiens |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.6.1.7 |
native enzyme, diffraction to 2.16 A resolution, in complex with kynurenine, diffraction to 1.95 A. Enzyme belongs to the fold-type I pyridoxal 5'-phosphate-dependent enzymes and shows a unique folding of its first 65 N-terminal residues |
Homo sapiens |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.6.1.7 |
Homo sapiens |
Q8N5Z0 |
isoform KAT II |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.6.1.7 |
L-kynurenine + 2-oxoglutarate |
- |
Homo sapiens |
kynurenic acid + L-glutamate + H2O |
- |
? |
|
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
2.6.1.7 |
pyridoxal 5'-phosphate |
enzyme belongs to the fold-type I pyridoxal 5'-phosphate-dependent enzymes, crystallization data |
Homo sapiens |
|