View source for Vitamin K epoxide reductase

{{Infobox protein family
| Symbol = VKOR
| Name = VKOR
| image = 
| width = 
| caption = structure of a bacterial homolog of vitamin K epoxide reductase
| Pfam = PF07884
| Pfam_clan =  
| InterPro = IPR012932
| SMART = 
| PROSITE = 
| MEROPS = 
| SCOP = 
| TCDB = 
| OPM family = 18
| OPM protein = 3kp9
| CAZy = 
| CDD = 
}}

{{infobox protein
|name=vitamin K epoxide reductase complex, subunit 1
|caption=
|image=
|width=
|HGNCid=23663
|Symbol=VKORC1
|AltSymbols=VKCFD2
|EntrezGene=79001
|OMIM=
|RefSeq=NM_024006
|UniProt=
|PDB=
|ECnumber=
|Chromosome=16
|Arm=p
|Band=11.2
|LocusSupplementaryData=
}}
'''Vitamin K epoxide reductase''' ('''VKOR''') is an [[enzyme]] ({{EC number|1.17.4.4}}) that [[reduction (chemistry)|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, [[Zinc dependent phospholipase C|bacteria]] and [[archaea]].<ref name="pmid15276181">{{cite journal |vauthors=Goodstadt L, Ponting CP | title = Vitamin K epoxide reductase: homology, active site and catalytic mechanism | journal = Trends Biochem. Sci. | volume = 29 | issue = 6 | pages = 289–92 |date=June 2004 | pmid = 15276181 | doi = 10.1016/j.tibs.2004.04.004 | url = }}</ref> Its C1 subunit ([[VKORC1]]) is the target of [[anticoagulant]] [[warfarin]].<ref>{{cite journal | last1 = Li | first1 = T | last2 = Chang | first2 = CY | last3 = Jin | first3 = DY | last4 = Lin | first4 = PJ | last5 = Khvorova | first5 = A | last6 = Stafford | first6 = DW | title = Identification of the gene for vitamin K epoxide reductase | journal = Nature | volume = 427 | issue = 6974 | pages = 541–4 | year = 2004 | pmid = 14765195 | doi = 10.1038/nature02254 }}</ref><ref>{{cite journal | doi = 10.1038/nature02214 | last1 = Rost | first1 = S | last2 = Fregin | first2 = A | last3 = Ivaskevicius | first3 = V | last4 = Conzelmann | first4 = E | last5 = Hortnagel | first5 = K | last6 = Pelz | first6 = HJ | last7 = Lappegard | first7 = K | last8 = Seifried | first8 = E | last9 = Scharrer | first9 = I ''et al.'' | last10 = Tuddenham | first10 = Edward G. D. | last11 = Müller | first11 = Clemens R. | last12 = Strom | first12 = Tim M. | last13 = Oldenburg | first13 = Johannes | year = 2004 | title = ''VKORC1'' cause warfarin resistance and multiple coagulation factor deficiency type 2 | url = | journal = Nature | volume = 427 | issue = 6974| pages = 537–41 | pmid = 14765194 | display-authors = 8 }}</ref> Four [[cysteine]] residues and one residue, which is either [[serine]] or threonine, are identified as likely active-site [[residue (chemistry)|residue]]s.<ref name="pmid15276181"/> In some [[plant]] and [[bacteria]]l [[Homology (biology)|homologues]], the VKORC1 homologous [[Domain (biology)|domain]] is fused with [[protein domain|domains]] of the [[thioredoxin]] family of [[oxidoreductases]].<ref name="pmid15276181"/>

==References==
<references/>

{{Metabolism of vitamins, coenzymes, and cofactors}}
{{Alcohol oxidoreductases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}

{{InterPro content|IPR012932}}

[[Category:EC 1.17.4]]