Vitamin K epoxide reductase: Difference between revisions
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| SCOP = | | SCOP = | ||
| TCDB = | | TCDB = | ||
| OPM family = | | OPM family = 18 | ||
| OPM protein = 3kp9 | | OPM protein = 3kp9 | ||
| CAZy = | | CAZy = | ||
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'''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]] | '''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== | ||
<references/> | <references/> | ||
{{Metabolism of vitamins, coenzymes, and cofactors}} | {{Metabolism of vitamins, coenzymes, and cofactors}} | ||
Latest revision as of 09:10, 10 January 2019
| VKOR | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | VKOR | ||||||||
| Pfam | PF07884 | ||||||||
| InterPro | IPR012932 | ||||||||
| OPM superfamily | 18 | ||||||||
| OPM protein | 3kp9 | ||||||||
| |||||||||
| vitamin K epoxide reductase complex, subunit 1 | |
|---|---|
| Identifiers | |
| 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 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.