S-carboxymethylcysteine synthase
| S-carboxymethylcysteine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 4.5.1.5 | ||||||||
| CAS number | 124671-39-2 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a S-carboxymethylcysteine synthase (EC 4.5.1.5) is an enzyme that catalyzes the chemical reaction
- 3-chloro-L-alanine + thioglycolate S-carboxymethyl-L-cysteine + chloride
Thus, the two substrates of this enzyme are 3-chloro-L-alanine and thioglycolate, whereas its two products are S-carboxymethyl-L-cysteine and chloride.
This enzyme belongs to the family of lyases, specifically the class of carbon-halide lyases. The systematic name of this enzyme class is 3-chloro-L-alanine chloride-lyase (adding thioglycolate S-carboxymethyl-L-cysteine-forming). This enzyme is also called S-carboxymethyl-L-cysteine synthase. It employs one cofactor, pyridoxal phosphate.
References
- Kumagai H, Suzuki H, Shigematsu H, Tuchikura T (1989). "S-Carboxymethylcysteine synthase from Escherichia coli". Agric. Biol. Chem. 53: 2481–2487. doi:10.1271/bbb1961.53.2481.
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