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 | Cystathionine gamma-synthase |
Enzyme Information
| 4.4.1.1 |
Cystathionine gamma-lyase.
based on mapping to UniProt P32929
L-cystathionine + H(2)O = L-cysteine + NH(3) + 2-oxobutanoate.
-!- The enzyme cleaves a carbon-sulfur bond, releasing L-cysteine 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. -!- Also catalyzes the conversion of L-homoserine to 2-oxobutanoate and ammonia, of L-cystine to thiocysteine, pyruvate and ammonia, and of L-cysteine to pyruvate, hydrogen sulfide and ammonia. -!- Formerly EC 4.2.1.15.
|
UniProtKB Entries (1)
| P32929 |
CGL_HUMAN
Homo sapiens
Cystathionine gamma-lyase
|
PDB Structure
| PDB | 2NMP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S
J.Biol.Chem.
|
