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ENZYME entry: EC 4.4.1.25

Accepted Name
L-cysteate sulfo-lyase.
Reaction catalysed
L-cysteate + H(2)O <=> hydrogensulfite + pyruvate + NH(3)
Cofactor(s)
Pyridoxal 5'-phosphate.
Comment(s)
  • 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 3.5.99.10.
  • 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.
Cross-references
BRENDA4.4.1.25
EC2PDB4.4.1.25
ExplorEnz4.4.1.25
PRIAM enzyme-specific profiles4.4.1.25
KEGG Ligand Database for Enzyme Nomenclature4.4.1.25
IUBMB Enzyme Nomenclature4.4.1.25
IntEnz4.4.1.25
MEDLINEFind literature relating to 4.4.1.25
MetaCyc4.4.1.25
UniProtKB/Swiss-Prot
Q5LL69, CUYA_RUEPO

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot 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.-.-.-