| vitamin-K-epoxide reductase (warfarin-sensitive) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.17.4.4 | ||||||||
| CAS no. | 55963-40-1 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a vitamin-K-epoxide reductase (warfarin-sensitive) ( EC 1.17.4.4) is an enzyme that catalyzes the chemical reaction
- 2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
Thus, the two substrates of this enzyme are 2-methyl-3-phytyl-1,4-naphthoquinone and oxidized dithiothreitol, whereas its two products are 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone and 1,4-dithiothreitol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH or CH2 groups of donor with a disulfide as acceptor. The systematic name of this enzyme class is 2-methyl-3-phytyl-1,4-naphthoquinone:oxidized-dithiothreitol oxidoreductase. This enzyme participates in biosynthesis of steroids. At least one compound, Warfarin is known to inhibit this enzyme.
References
- Lee JJ, Fasco MJ (1984). "Metabolism of vitamin K and vitamin K 2,3-epoxide via interaction with a common disulfide". Biochemistry. 23 (10): 2246–52. doi: 10.1021/bi00305a024. PMID 6733086.
- Mukharji I, Silverman RB (1985). "Purification of a vitamin K epoxide reductase that catalyzes conversion of vitamin K 2,3-epoxide to 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone". Proc. Natl. Acad. Sci. U.S.A. 82 (9): 2713–7. Bibcode: 1985PNAS...82.2713M. doi: 10.1073/pnas.82.9.2713. PMC 397635. PMID 3857611.
- Whitlon DS, Sadowski JA, Suttie JW (1978). "Mechanism of coumarin action: significance of vitamin K epoxide reductase inhibition". Biochemistry. 17 (8): 1371–7. doi: 10.1021/bi00601a003. PMID 646989.
| vitamin-K-epoxide reductase (warfarin-sensitive) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.17.4.4 | ||||||||
| CAS no. | 55963-40-1 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a vitamin-K-epoxide reductase (warfarin-sensitive) ( EC 1.17.4.4) is an enzyme that catalyzes the chemical reaction
- 2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
Thus, the two substrates of this enzyme are 2-methyl-3-phytyl-1,4-naphthoquinone and oxidized dithiothreitol, whereas its two products are 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone and 1,4-dithiothreitol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH or CH2 groups of donor with a disulfide as acceptor. The systematic name of this enzyme class is 2-methyl-3-phytyl-1,4-naphthoquinone:oxidized-dithiothreitol oxidoreductase. This enzyme participates in biosynthesis of steroids. At least one compound, Warfarin is known to inhibit this enzyme.
References
- Lee JJ, Fasco MJ (1984). "Metabolism of vitamin K and vitamin K 2,3-epoxide via interaction with a common disulfide". Biochemistry. 23 (10): 2246–52. doi: 10.1021/bi00305a024. PMID 6733086.
- Mukharji I, Silverman RB (1985). "Purification of a vitamin K epoxide reductase that catalyzes conversion of vitamin K 2,3-epoxide to 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone". Proc. Natl. Acad. Sci. U.S.A. 82 (9): 2713–7. Bibcode: 1985PNAS...82.2713M. doi: 10.1073/pnas.82.9.2713. PMC 397635. PMID 3857611.
- Whitlon DS, Sadowski JA, Suttie JW (1978). "Mechanism of coumarin action: significance of vitamin K epoxide reductase inhibition". Biochemistry. 17 (8): 1371–7. doi: 10.1021/bi00601a003. PMID 646989.