In enzymology, a phylloquinone monooxygenase (2,3-epoxidizing) (EC 1.14.99.20) is an enzyme that catalyzes the chemical reaction
phylloquinone monooxygenase (2,3-epoxidizing) | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.99.20 | ||||||||
CAS no. | 54596-37-1 | ||||||||
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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- phylloquinone + AH2 + O2 2,3-epoxyphylloquinone + A + H2O
The three substrates of this enzyme are phylloquinone, an electron acceptor AH2, and O2, whereas its three products are 2,3-epoxyphylloquinone, the reduction product A, 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 derive from O miscellaneous. The systematic name of this enzyme class is phylloquinone,hydrogen-donor:oxygen oxidoreductase (2,3-epoxidizing). Other names in common use include phylloquinone epoxidase, vitamin K 2,3-epoxidase, vitamin K epoxidase, and vitamin K1 epoxidase.
References
edit- Willingham AK, Matschiner JT (1974). "Changes in phylloquinone epoxidase activity related to prothrombin synthesis and microsomal clotting activity in the rat". Biochem. J. 140 (3): 435–41. PMC 1168020. PMID 4155625.