| prenylcysteine oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.3.5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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.
Human protein and gene
- Prenylcysteine oxidase 1, symbol PCYOX1, gene on chromosome 2
See also
- Hemithioacetals in nature, for mechanism of action
- Flavin adenine dinucleotide, cofactor of the enzyme
- Prenylation, a process forming S-prenyl-L-cysteine
References
- Zhang L, Tschantz WR, Casey PJ (1997). "Isolation and characterization of a prenylcysteine lyase from bovine brain". J. Biol. Chem. 272 (37): 23354–9. doi:10.1074/jbc.272.37.23354. 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 (4): 2321–4. doi:10.1074/jbc.C000616200. PMID 11078725.
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