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 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.
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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.
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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.
FEBS J.
|