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Your query returned 1 entry. Printable version
EC | 4.4.1.25 | ||
Accepted name: | L-cysteate sulfo-lyase | ||
Reaction: | L-cysteate + H2O = hydrogensulfite + pyruvate + NH3 (overall reaction) (1a) L-cysteate = hydrogensulfite + 2-aminoprop-2-enoate (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous) (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous) |
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Glossary: | L-cysteate = (2S)-2-amino-3-sulfopropanoate | ||
Other name(s): | L-cysteate sulfo-lyase (deaminating); CuyA; L-cysteate bisulfite-lyase (deaminating; pyruvate-forming) | ||
Systematic name: | L-cysteate hydrogensulfite-lyase (deaminating; pyruvate-forming) | ||
Comments: | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing hydrogensulfite 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 hydrogen sulfide, pyruvate, and ammonia. This inducible enzyme from the marine bacterium Silicibacter pomeroyi DSS-3 forms part of the cysteate-degradation pathway. | ||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||
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