CATH Classification

Domain Context

CATH Clusters

Superfamily Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Functional Family Kynurenine--oxoglutarate transaminase 1

Enzyme Information
Glutamine--phenylpyruvate transaminase.
based on mapping to UniProt Q16773
L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine.
-!- L-methionine, L-histidine and L-tyrosine can act as donors. -!- Has little activity on pyruvate and glyoxylate (cf. EC
Cysteine-S-conjugate beta-lyase.
based on mapping to UniProt Q16773
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 and EC
Kynurenine--oxoglutarate transaminase.
based on mapping to UniProt Q16773
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)

Homo sapiens
Kynurenine--oxoglutarate transaminase 1

PDB Structure

External Links
Primary Citation
Crystal structure of human kynurenine aminotransferase-I in a novel space group
Nadvi, N.A., Salam, N.K., Park, J., Akladios, F.N., Kapoor, V., Collyer, C.A., Gorrell, M.D., Church, W.B.
To be published