Cyclohexylamine oxidase
| cyclohexylamine oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.3.12 | ||||||||
| CAS no. | 63116-97-2 | ||||||||
| 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, cyclohexylamine oxidase (EC 1.4.3.12) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are cyclohexylamine, water, and oxygen. Its products are cyclohexanone, hydrogen peroxide, and ammonia.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is cyclohexylamine:oxygen oxidoreductase (deaminating). This enzyme participates in caprolactam degradation. It employs one cofactor, FAD.
References
- ^ Enzyme 1.4.3.12 at KEGG Pathway Database.
- ^ Tokieda T, Niimura T, Takamura F, Yamaha T (April 1977). "Purification and some properties of cyclohexylamine oxidase from a Pseudomonas sp". J. Biochem. 81 (4). Tokyo: 851–8. doi:10.1093/oxfordjournals.jbchem.a131549. PMID 18451.