Cysteine-S-conjugate beta-lyase
From Wikipedia, the free encyclopedia
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
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.
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[edit] Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1W7L, 1W7M, and 1W7N.
[edit] References
- IUBMB entry for 4.4.1.13
- BRENDA references for 4.4.1.13 (Recommended.)
- PubMed references for 4.4.1.13
- PubMed Central references for 4.4.1.13
- Google Scholar references for 4.4.1.13
- 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: 8854–9. PMID 721818.
[edit] External links
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- The CAS registry number for this enzyme class is 68652-57-3.