Dimethylpropiothetin dethiomethylase
In enzymology, a dimethylpropiothetin dethiomethylase (EC 4.4.1.3) is an enzyme that catalyzes the chemical reaction
- S,S-dimethyl-beta-propiothetin dimethyl sulfide + acrylate
| dimethylpropiothetin dethiomethylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.4.1.3 | ||||||||
| CAS number | 9026-85-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Hence, this enzyme has one substrate, S,S-dimethyl-beta-propiothetin, and two products, dimethyl sulfide and acrylate.
This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is S,S-dimethyl-beta-propiothetin dimethyl-sulfide-lyase (acrylate-forming). Other names in common use include desulfhydrase, and S,S-dimethyl-beta-propiothetin dimethyl-sulfide-lyase.
References
- ANDERSON DG, CANTONI GL (1956). "Enzymatic cleavage of dimethylpropiothetin by Polysiphonia lanosa". J. Biol. Chem. 222 (1): 171–7. PMID 13366990.
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