| 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 | ||||||||
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In enzymology, a cyclohexylamine oxidase (EC 1.4.3.12) is an enzyme that catalyzes the chemical reaction
- cyclohexylamine + O2 + H2O cyclohexanone + NH3 + H2O2
cyclohexanone + NH3 + H2O2The 3 substrates of this enzyme are cyclohexylamine, O2, and H2O, whereas its 3 products are cyclohexanone, NH3, and H2O2.
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
- 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. PMID 18451.
| CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases | |
|---|---|
| 1.4.1: NAD/NADP acceptor | |
| 1.4.3: oxygen acceptor | |
| 1.4.4: disulfide acceptor | |
| 1.4.99: other acceptors | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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