CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.640 | Aspartate Aminotransferase; domain 2 |
|
3.40.640.10 | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
Domain Context
CATH Clusters
| Superfamily | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
| Functional Family | Kynurenine--oxoglutarate transaminase 1 |
Enzyme Information
| 2.6.1.64 |
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 2.6.1.15).
|
| 4.4.1.13 |
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 4.4.1.6 and EC 4.4.1.8.
|
| 2.6.1.7 |
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)
| Q16773 |
KAT1_HUMAN
Homo sapiens
Kynurenine--oxoglutarate transaminase 1
|
PDB Structure
| PDB | 4WP0 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of human kynurenine aminotransferase-I in a novel space group
To be published
|