EC |
1.8.3.5 |
Accepted name: |
prenylcysteine oxidase |
Reaction: |
an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2 |
Other name(s): |
prenylcysteine lyase |
Systematic name: |
S-prenyl-L-cysteine:oxygen oxidoreductase |
Comments: |
A flavoprotein (FAD). Cleaves the thioether bond of S-prenyl-L-cysteines, such as S-farnesylcysteine and S-geranylgeranylcysteine. N-Acetyl-prenylcysteine and prenylcysteinyl peptides are not substrates. May represent the final step in the degradation of prenylated proteins in mammalian tissues. Originally thought to be a simple lyase so it had been classified as EC 4.4.1.18. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 196717-99-4 |
References: |
1. |
Zhang, L., Tschantz, W.R. and Casey, P.J. Isolation and characterization of a prenylcysteine lyase from bovine brain. J. Biol. Chem. 272 (1997) 23354–23359. [DOI] [PMID: 9287348] |
2. |
Tschantz, W.R., Digits, J.A., Pyun, H.J., Coates, R.M. and Casey, P.J. Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase. J. Biol. Chem. 276 (2001) 2321–2324. [DOI] [PMID: 11078725] |
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[EC 1.8.3.5 created 2000 as EC 4.4.1.18, transferred 2002 to EC 1.8.3.5] |
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