Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.6.1.7 extracted from

  • Han, Q.; Robinson, H.; Li, J.
    Crystal structure of human kynurenine aminotransferase II (2008), J. Biol. Chem., 283, 3567-3573.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Homo sapiens Q8N5Z0 isoform KAT II
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-kynurenine + 2-oxoglutarate
-
Homo sapiens kynurenic acid + L-glutamate + H2O
-
?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate enzyme belongs to the fold-type I pyridoxal 5'-phosphate-dependent enzymes, crystallization data Homo sapiens