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Cysteine-S-conjugate beta-lyase

The enzyme cysteine-S-conjugate β-lyase (EC 4.4.1.13) catalyzes the chemical reaction

an <small>L</small>-cysteine-S-conjugate + H<sub>2</sub>O = a thiol + NH<sub>3</sub> + pyruvate (overall reaction)
:(1a) an <small>L</small>-cysteine-S-conjugate = a thiol + 2-aminoprop-2-enoate
:(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
:(1c) 2-iminopropanoate + H<sub>2</sub>O = pyruvate + NH<sub>3</sub> (spontaneous)

This enzyme belongs to the family of lyases, specifically the class of carbon-sulfur lyases. The systematic name of this enzyme class is <small>L</small>-cysteine-S-conjugate thiol-lyase (deaminating; pyruvate-forming). Other names in common use include cysteine conjugate β-lyase, glutamine transaminase K/cysteine conjugate β-lyase, and <small>L</small>-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 .

References