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Vitamin K epoxide reductase
Introduction
Vitamin K epoxide reductase (VKOR) is an enzyme (EC 1.17.4.4) 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
- ↑ 1.0 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.
- ↑ 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.
- ↑ 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.