Prenylcysteine oxidase
From Wikipedia, the free encyclopedia
In enzymology, a prenylcysteine oxidase (EC 1.8.3.5) is an enzyme that catalyzes the chemical reaction
- an S-prenyl-L-cysteine + O2 + H2O
a prenal + L-cysteine + H2O2
The 3 substrates of this enzyme are S-prenyl-L-cysteine, O2, and H2O, whereas its 3 products are prenal, L-cysteine, and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is S-prenyl-L-cysteine:oxygen oxidoreductase. This enzyme is also called prenylcysteine lyase.
[edit] References
- IUBMB entry for 1.8.3.5
- BRENDA references for 1.8.3.5 (Recommended.)
- PubMed references for 1.8.3.5
- PubMed Central references for 1.8.3.5
- Google Scholar references for 1.8.3.5
- Zhang L, Tschantz WR, Casey PJ (1997). "Isolation and characterization of a prenylcysteine lyase from bovine brain". J. Biol. Chem. 272: 23354–9. doi:. PMID 9287348.
- Tschantz WR, Digits JA, Pyun HJ, Coates RM, Casey PJ (2001). "Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase". J. Biol. Chem. 276: 2321–4. doi:. PMID 11078725.

