From Wikipedia, the free encyclopedia
dimethylpropiothetin dethiomethylase
Identifiers
EC no. 4.4.1.3
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme dimethylpropiothetin dethiomethylase (EC 4.4.1.3) catalyzes the chemical reaction

S,S-dimethyl-β-propiothetin dimethyl sulfide + acrylate

The enzyme breaks S,S-dimethyl-β-propiothetin into 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-β-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.


From Wikipedia, the free encyclopedia
dimethylpropiothetin dethiomethylase
Identifiers
EC no. 4.4.1.3
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme dimethylpropiothetin dethiomethylase (EC 4.4.1.3) catalyzes the chemical reaction

S,S-dimethyl-β-propiothetin dimethyl sulfide + acrylate

The enzyme breaks S,S-dimethyl-β-propiothetin into 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-β-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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