From Wikipedia, the free encyclopedia

S-carboxymethylcysteine synthase
Identifiers
EC no. 4.5.1.5
CAS no. 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 / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme S-carboxymethylcysteine synthase (EC 4.5.1.5) catalyzes the reaction

3-chloro-L-alanine + thioglycolate S-carboxymethyl-L-cysteine + 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 (9): 2481–2487. doi: 10.1271/bbb1961.53.2481.


From Wikipedia, the free encyclopedia

S-carboxymethylcysteine synthase
Identifiers
EC no. 4.5.1.5
CAS no. 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 / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme S-carboxymethylcysteine synthase (EC 4.5.1.5) catalyzes the reaction

3-chloro-L-alanine + thioglycolate S-carboxymethyl-L-cysteine + 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 (9): 2481–2487. doi: 10.1271/bbb1961.53.2481.



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