Due to scheduled maintenance work, this service may not be available on Monday January 22nd between 08.00 am and 9.00 am CEST.
To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https

ENZYME entry: EC

Accepted Name
L-cysteate sulfo-lyase.
Reaction catalysed
L-cysteate + H(2)O <=> hydrogensulfite + pyruvate + NH(3)
Pyridoxal 5'-phosphate.
  • 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
  • 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 profiles4.4.1.25
KEGG Ligand Database for Enzyme Nomenclature4.4.1.25
IUBMB Enzyme Nomenclature4.4.1.25
MEDLINEFind literature relating to

View entry in original ENZYME format
View entry in raw text format (no links)

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.-.-.-