EC Number   |
General Information |
Reference |
|---|
    1.17.4.4 | evolution |
clear difference in VKOR activity and Ki for warfarin among bird species |
724796 |
| 1.17.4.4 | evolution |
the enzyme belongs to the thiol-disulfide oxidoreductases. VKORL1, EC 1.1.4.2, is more highly conserved among vertebrates than its evolutionary relative VKOR, EC 1.1.4.1. The human paralogous proteins are 42% identical with 60% similarity |
724800 |
| 1.17.4.4 | malfunction |
depletion of the protein disulfide formation activity of the enzyme in the endoplasmic reticulum results in cell death. Knockdown of the enzyme results in no detectable increase in expression of the ER Hsp70 chaperone BiP nor evidence of Xbp-1 splicing when measured on the final day of knockdown, indicating that an unfolded protein response is not being induced |
725921 |
| 1.17.4.4 | malfunction |
some naturally occuring mutations of the enzyme, e.g. at residues mutations at Leu120, Leu128 and Tyr139, confer resistance against anti-coagulants, sodium warfarin, difenacoum and brodifacoum, to rats |
724119 |
| 1.17.4.4 | malfunction |
warfarin interfers with the vitamin K cycle by inhibiting VKOR thus limiting the available activated hydroquinone cofactor and functionally impeding various blood clotting proteins that are dependent on gamma-carboxyglutamate residues |
724800 |
| 1.17.4.4 | metabolism |
a key enzyme in the vitamin K cycle |
745946 |
| 1.17.4.4 | metabolism |
in vivo VKORC1L1 reduces vitamin K epoxide to support vitamin K-dependent carboxylation as efficiently as does VKORC1 |
745318 |
| 1.17.4.4 | metabolism |
one of the key enzymes in the vitamin K cycle, which is essential for posttranslational modification of vitamin K-dependent proteins. Essential enzyme for vitamin K-dependent carboxylation |
746471 |
| 1.17.4.4 | metabolism |
posttranslocational protein folding in the Gram-positive biofilm-forming actinobacterium Actinomyces oris is mediated by a membrane-bound thiol-disulfide oxidoreductase named MdbA, which catalyzes oxidative folding of nascent polypeptides transported by the Sec translocon. Reoxidation of MdbA involves a bacterial vitamin K epoxide reductase (VKOR)-like protein |
745224 |
| 1.17.4.4 | metabolism |
the enzyme plays important roles in redox regulation. The enzyme is involved in resistance to salt or drought stress. Down- and up-regulation of the enzyme in vivo changes the activities of antioxidant enzymes and results in differential accumulation of reactive oxygen species |
745995 |
