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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. |
