Vitamin K epoxide reductase

Vitamin K epoxide reductase (VKOR) is an enzyme (EC 1.1.4.1) 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]

References

1. ↑ 1.0 1.1 1.2 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.  CS1 maint: Explicit use of et al. (link)

See also

• Oxidoreductase

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