CATH Classification

Domain Context

CATH Clusters

Superfamily Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Functional Family Aspartate aminotransferase

Enzyme Information

2.6.1.1
Aspartate transaminase.
based on mapping to UniProt P00508
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
-!- Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. -!- This activity can be formed from EC 2.6.1.57 by controlled proteolysis.
2.6.1.7
Kynurenine--oxoglutarate transaminase.
based on mapping to UniProt P00508
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
-!- Also acts on 3-hydroxykynurenine. -!- The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.

UniProtKB Entries (1)

P00508
AATM_CHICK
Gallus gallus
Aspartate aminotransferase, mitochondrial

PDB Structure

PDB 1AKC
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue.
Malashkevich, V.N., Jager, J., Ziak, M., Sauder, U., Gehring, H., Christen, P., Jansonius, J.N.
Biochemistry