ENZYME entry: EC 220.127.116.11
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|L-cysteate + H(2)O <=> hydrogensulfite + pyruvate + NH(3)|
- The enzyme cleaves a carbon-sulfur bond, releasing bisulfite 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 18.104.22.168.
- D-cysteine can also act as a substrate, but more slowly.
- It is converted into pyruvate, sulfide and ammonia.
- The inducible enzyme from Silicibacter pomeroyi DSS-3 forms part of
the cysteate-degradation pathway.
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
|Rhea expert-curated reactions||220.127.116.11|
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.-.-.-