Vitamin K epoxide reductase
| Vitamin K epoxide reductase (warfarin-sensitive) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
ExPASy NiceZyme view | | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Vitamin K epoxide reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
TCDB 9.B.265 | | ||||||||
| OPM superfamily | 18 | ||||||||
| OPM protein | 3kp9 | ||||||||
| |||||||||
Vitamin K epoxide reductase (VKOR) is an
oxidoreductases.[1]
Four
DsbB active site. Two other cysteines to the N-terminal are located in a loop outside of the transmembrane region; they relay electrons with a redox protein (or in the case of the bacterial homolog, its own fused domain).[2][3]
The human gene for VKOR is called VKORC1 (VKOR complex subunit 1). It is the target of anticoagulant warfarin. Its partner is a redox protein with an unknown identity,[4][5] probably a thioredoxin-like protein located in the ER lumen such as TMX1.[6]
There is also a similar gene called VKORC1L1. The VKORL1 complex it forms is much less efficient at reducing the epoxide, but it has the ability to reduce the quinone form of vitamin K to a diol form (KH2). Although EC 1.17.4.4 notes both paralogs as having both activities, the precise division of labor in vitro is debated.[7]
