CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1150 | Aspartate Aminotransferase, domain 1 |
|
3.90.1150.10 | Aspartate Aminotransferase, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Aspartate Aminotransferase, domain 1 |
| 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 | 3E2F |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Correction for Han et al., "Biochemical and Structural Properties of Mouse Kynurenine Aminotransferase III".
Mol. Cell. Biol.
|
