Camphor 1,2-monooxygenase
| camphor 1,2-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.15.2 | ||||||||
| CAS number | 37256-81-8 | ||||||||
| 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 / EGO | ||||||||
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In enzymology, a camphor 1,2-monooxygenase (EC 1.14.15.2) is an enzyme that catalyzes the chemical reaction
- (+)-bornane-2,5-dione + reduced rubredoxin + O2 5-oxo-1,2-campholide + oxidized rubredoxin + H2O
The 3 substrates of this enzyme are (+)-bornane-2,5-dione, reduced rubredoxin, and O2, whereas its 3 products are 5-oxo-1,2-campholide, oxidized rubredoxin, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation o one atom of oxygen into the other donor. The systematic name of this enzyme class is (+)-camphor,reduced-rubredoxin:oxygen oxidoreductase (1,2-lactonizing). Other names in common use include 2,5-diketocamphane lactonizing enzyme, camphor ketolactonase I, oxygenase, camphor 1,2-mono, and ketolactonase I. It employs one cofactor, iron.
References
- CONRAD HE, DUBUS R, NAMTVEDT MJ, GUNSALUS IC (1965). "MIXED FUNCTION OXIDATION. II. SEPARATION AND PROPERTIES OF THE ENZYMES CATALYZING CAMPHOR LACTONIZATION". J. Biol. Chem. 240: 495–503. PMID 14253460.
- Trudgill PW, DuBus R, Gunsalus IC (1966). "Mixed function oxidation. VI. Purification of a tightly coupled electron transport complex in camphor lactonization". J. Biol. Chem. 241 (18): 4288–90. PMID 4288652.
- Yu CA, Gunsalus IC (1969). "Monoxygenases. VII. Camphor ketolactonase I and the role of three protein components". J. Biol. Chem. 244 (22): 6149–52. PMID 4310834.