CATH Classification

Domain Context

CATH Clusters

Superfamily Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Functional Family Kynurenine--oxoglutarate transaminase 3

Enzyme Information

4.4.1.13
Cysteine-S-conjugate beta-lyase.
based on mapping to UniProt Q71RI9
An L-cysteine-S-conjugate + H(2)O = RSH + NH(3) + pyruvate.
-!- A pyridoxal 5'-phosphate protein. -!- The enzyme is promiscuous regarding the moiety conjugated to L-cysteine, and can accept both aliphatic and aromatic substitutions. -!- The enzyme cleaves a carbon-sulfur bond, releasing a thiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- While bacteria and plants have dedicated enzymes, all of the animal enzymes discovered thus far are bifunctional, most of which also act as aminotransferases. -!- Formerly EC 4.4.1.6 and EC 4.4.1.8.
2.6.1.7
Kynurenine--oxoglutarate transaminase.
based on mapping to UniProt Q71RI9
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.
2.6.1.63
Kynurenine--glyoxylate transaminase.
based on mapping to UniProt Q71RI9
L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine.
-!- Acts, more slowly, on L-phenylalanine, L-histidine and L-tyrosine.

UniProtKB Entries (1)

Q71RI9
KAT3_MOUSE
Mus musculus
Kynurenine--oxoglutarate transaminase 3

PDB Structure

PDB 5VEP
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Detect, correct, retract: How to manage incorrect structural models.
Wlodawer, A., Dauter, Z., Porebski, P.J., Minor, W., Stanfield, R., Jaskolski, M., Pozharski, E., Weichenberger, C.X., Rupp, B.
FEBS J.