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 | Cystathionine gamma-lyase |
Enzyme Information
| 4.4.1.2 |
Homocysteine desulfhydrase.
based on mapping to UniProt P13254
L-homocysteine + H(2)O = H(2)S + NH(3) + 2-oxobutanoate.
-!- The enzyme cleaves a carbon-sulfur bond, releasing hydrogen sulfide and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10.
|
| 4.4.1.11 |
Methionine gamma-lyase.
based on mapping to UniProt P13254
L-methionine + H(2)O = methanethiol + NH(3) + 2-oxobutanoate.
-!- The enzyme cleaves a carbon-sulfur bond, releasing methanethiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10. -!- The enzyme is involved in L-methionine catabolism.
|
UniProtKB Entries (1)
| P13254 |
MEGL_PSEPU
Pseudomonas putida
L-methionine gamma-lyase
|
PDB Structure
| PDB | 3VK3 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The role of amino acid residues in the active site of L-methionine gamma-lyase from Pseudomonas putida.
Biosci.Biotechnol.Biochem.
|