Cysteine-S-conjugate beta-lyase

In enzymology, a cysteine-S-conjugate beta-lyase is an enzyme that catalyzes the chemical reaction


 * RS-CH2-CH(NH3+)COO- $$\rightleftharpoons$$ RSH + NH3 + pyruvate

Hence, this enzyme has one substrate, RS-CH2-CH(NH3+)COO-, but 3 products: RSH, NH3, and pyruvate.

This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is L-cysteine-S-conjugate thiol-lyase (deaminating; pyruvate-forming). Other names in common use include cysteine conjugate beta-lyase, glutamine transaminase K/cysteine conjugate beta-lyase, and L-cysteine-S-conjugate thiol-lyase (deaminating). It employs one cofactor, pyridoxal phosphate.

Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes, , and.