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Cysteine-S-conjugate beta-lyase
From Wikipedia, the free encyclopedia
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The enzyme cysteine-S-conjugate β-lyase (EC 4.4.1.13) catalyzes the chemical reaction
- an L-cysteine-S-conjugate + H2O = a thiol + NH3 + pyruvate (overall reaction)
- (1a) an L-cysteine-S-conjugate = a thiol + 2-aminoprop-2-enoate
- (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
- (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
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 β-lyase, glutamine transaminase K/cysteine conjugate β-lyase, and L-cysteine-S-conjugate thiol-lyase (deaminating). It employs one cofactor, pyridoxal phosphate.
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Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1W7L, 1W7M, and 1W7N.
References
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