Vitamin K epoxide reductase

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Vitamin K epoxide reductase
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Symbol VKOR
Pfam PF07884
InterPro IPR012932
OPM superfamily 232
OPM protein 3kp9
vitamin K epoxide reductase complex, subunit 1
Symbol VKORC1
Alt. symbols VKCFD2
Entrez 79001
HUGO 23663
RefSeq NM_024006
Other data
Locus Chr. 16 p11.2

Vitamin K epoxide reductase (VKOR) is an enzyme (EC that reduces vitamin K after it has been oxidised in the carboxylation of glutamic acid residues in blood coagulation enzymes. VKORC is a member of a large family of predicted enzymes that are present in vertebrates, Drosophila, plants, bacteria and archaea.[1] Its C1 subunit (VKORC1) is the target of anticoagulant warfarin.[2][3] Four cysteine residues and one residue, which is either serine or threonine, are identified as likely active-site residues.[1] In some plant and bacterial homologues, the VKORC1 homologous domain is fused with domains of the thioredoxin family of oxidoreductases.[1]


  1. ^ a b c Goodstadt L, Ponting CP (June 2004). "Vitamin K epoxide reductase: homology, active site and catalytic mechanism". Trends Biochem. Sci. 29 (6): 289–92. doi:10.1016/j.tibs.2004.04.004. PMID 15276181. 
  2. ^ Li, T; Chang, CY; Jin, DY; Lin, PJ; Khvorova, A; Stafford, DW (2004). "Identification of the gene for vitamin K epoxide reductase". Nature. 427 (6974): 541–4. doi:10.1038/nature02254. PMID 14765195. 
  3. ^ Rost, S; Fregin, A; Ivaskevicius, V; Conzelmann, E; Hortnagel, K; Pelz, HJ; Lappegard, K; Seifried, E; et al. (2004). "VKORC1 cause warfarin resistance and multiple coagulation factor deficiency type 2". Nature. 427 (6974): 537–41. doi:10.1038/nature02214. PMID 14765194. 

See also[edit]

This article incorporates text from the public domain Pfam and InterPro IPR012932