Cysteine-S-conjugate beta-lyase

In enzymology, a cysteine-S-conjugate beta-lyase (EC 4.4.1.13) is an enzyme that catalyzes the chemical reaction

RS-CH2-CH(NH3+)COO- RSH + NH3 + pyruvate
cysteine-S-conjugate beta-lyase
Identifiers
EC number4.4.1.13
CAS number68652-57-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Hence, this enzyme has one substrate, [[RS-CH<sub>2</sub>-CH(NH<sub>3</sub>+)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 1W7L, 1W7M, and 1W7N.

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References
    • Tateishi M, Suzuki S, Shimizu H (1978). "Cysteine conjugate beta-lyase in rat liver. A novel enzyme catalyzing formation of thiol-containing metabolites of drugs". J. Biol. Chem. 253 (24): 8854–9. PMID 721818.


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