ENZYME entry: EC 4.4.1.8
| Accepted Name |
|---|
| Cystathionine beta-lyase.
|
| Alternative Name(s) |
|---|
| Beta C-S lyase. |
| Beta-cystathionase. |
| Cysteine lyase. |
| Cystine lyase. |
| Reaction catalysed |
|---|
| L-cystathionine + H(2)O <=> L-homocysteine + NH(3) + pyruvate |
| Cofactor(s) |
|---|
| Pyridoxal 5'-phosphate.
|
| Comment(s) |
|---|
- The enzyme cleaves a carbon-sulfur bond, releasing L-homocysteine and
an unstable enamine product that tautomerizes to an imine form, which
undergoes a hydrolytic deamination to form pyruvate and ammonia.
- The latter reaction, which can occur spontaneously, can also be
catalyzed by EC 3.5.99.10.
- The enzyme from some sources also acts on L-cystine, forming
pyruvate, ammonia and cysteine persulfide, and a number of related
compounds.
- Possibly identical, in Saccharomyces cerevisiae, with EC 4.4.1.6.
|
| Cross-references |
|---|
| PROSITE | PDOC00518 ; PDOC00677 |
| BRENDA | 4.4.1.8 |
| EC2PDB | 4.4.1.8 |
| ExplorEnz | 4.4.1.8 |
| PRIAM enzyme-specific profiles | 4.4.1.8 |
| KEGG Ligand Database for Enzyme Nomenclature | 4.4.1.8 |
| IUBMB Enzyme Nomenclature | 4.4.1.8 |
| IntEnz | 4.4.1.8 |
| MEDLINE | Find literature relating to 4.4.1.8 |
| MetaCyc | 4.4.1.8 |
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 4.4.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-