EC 4.4.1.25 - L-cysteate sulfo-lyase

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IntEnz Enzyme Nomenclature
EC 4.4.1.25

Names

Accepted name:
L-cysteate sulfo-lyase
Other names:
L-cysteate sulfo-lyase (deaminating)
CuyA
L-cysteate bisulfite-lyase (deaminating; pyruvate-forming)
Systematic name:
L-cysteate hydrogensulfite-lyase (deaminating; pyruvate-forming)

Reaction

Cofactor

Comments:

A pyridoxal-phosphate protein. 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 catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. D-Cysteine can also act as a substrate, but more slowly. It is converted into pyruvate, sulfide and ammonia. This inducible enzyme from the marine bacterium Silicibacter pomeroyi DSS-3 forms part of the cysteate-degradation pathway.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0034011
UniProtKB/Swiss-Prot:

References

  1. Denger, K., Smits, T.H.M. and Cook, A.M.
    L-cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3T.
    Biochem. J. 394 : 657-664 (2006). [PMID: 16302849]

[EC 4.4.1.25 created 2006]