Enzyme

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     1. Oxidoreductases
        1.17 Acting on CH or CH2 groups
            1.17.4 With a disulfide as acceptor
ID:1.17.4.4
Description:Vitamin-K-epoxide reductase (warfarin-sensitive).
Alternative Name: Vitamin K1 epoxide reductase.
Phylloquinone epoxide reductase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.17.4.4
BRENDA Enzyme Link: BRENDA 1.17.4.4
KEGG Enzyme Link: KEGG1.17.4.4
BioCyc Enzyme Link: BioCyc 1.17.4.4
ExPASy Enzyme Link: ExPASy1.17.4.4
EC2PDB Enzyme Link: EC2PDB 1.17.4.4
ExplorEnz Enzyme Link: ExplorEnz 1.17.4.4
PRIAM enzyme-specific profiles Link: PRIAM 1.17.4.4
IntEnz Enzyme Link: IntEnz 1.17.4.4
MEDLINE Enzyme Link: MEDLINE 1.17.4.4
MSA:

1.17.4.4;

Phylogenetic Tree:

1.17.4.4;

Uniprot:
M-CSA:
RHEA:13817 H2O + oxidized dithiothreitol + phylloquinone = 1,4-dithiothreitol + 2,3-epoxyphylloquinone
RULE(radius=1) [*:1]-[C;H0;+0:2]1(-[*:3])-[O;H0;+0:4]-[C;H0;+0:5]-1(-[*:6])-[*:7].([*:8]-[SH;+0:9].[*:10]-[SH;+0:11])>>[*:1]-[C;H0;+0:2](-[*:3])=[C;H0;+0:5](-[*:6])-[*:7].[*:8]-[S;H0;+0:9]-[S;H0;+0:11]-[*:10].[OH2;+0:4]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Metabolism of vitamin K and vitamin K 2,3-epoxide via interaction with a common disulfide.Lee JJ, Fasco MJ1984 May 86733086
Mechanism of coumarin action: significance of vitamin K epoxide reductase inhibition.Whitlon DS, Sadowski JA, Suttie JW1978 Apr 18646989
Purification of a vitamin K epoxide reductase that catalyzes conversion of vitamin K 2,3-epoxide to 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone.Mukharji I, Silverman RB1985 May3857611
Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regeneration.Tie JK, Jin DY, Stafford DW2014 Mar 2824532791
VKORC1L1, an enzyme rescuing the vitamin K 2,3-epoxide reductase activity in some extrahepatic tissues during anticoagulation therapy.Hammed A, Matagrin B, Spohn G, Prouillac C, Benoit E, Lattard V2013 Oct 423928358
New insights into the catalytic mechanism of vitamin K epoxide reductase (VKORC1) - The catalytic properties of the major mutations of rVKORC1 explain the biological cost associated to mutations.Matagrin B, Hodroge A, Montagut-Romans A, Andru J, Fourel I, Besse S, Benoit E, Lattard V201323772386
Determination of the warfarin inhibition constant Ki for vitamin K 2,3-epoxide reductase complex subunit-1 (VKORC1) using an in vitro DTT-driven assay.Bevans CG, Krettler C, Reinhart C, Tran H, Koßmann K, Watzka M, Oldenburg J2013 Aug23618698
Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanisms.Tie JK, Jin DY, Stafford DW2012 Oct 522923610
Novel insight into the mechanism of the vitamin K oxidoreductase (VKOR): electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylation.Rishavy MA, Usubalieva A, Hallgren KW, Berkner KL2011 Mar 420978134
A quantum chemical study of the mechanism of action of Vitamin K epoxide reductase (VKOR) II. Transition states.Davis CH, Deerfield D 2nd, Wymore T, Stafford DW, Pedersen LG2007 Sep17182266
Vitamin K epoxide reductase complex subunit 1 (VKORC1): the key protein of the vitamin K cycle.Oldenburg J, Bevans CG, Müller CR, Watzka M2006 Mar-Apr16677080
Site-directed mutagenesis of coumarin-type anticoagulant-sensitive VKORC1: evidence that highly conserved amino acids define structural requirements for enzymatic activity and inhibition by warfarin.Rost S, Fregin A, Hünerberg M, Bevans CG, Müller CR, Oldenburg J2005 Oct16270630
The genetic basis of resistance to anticoagulants in rodents.Pelz HJ, Rost S, Hünerberg M, Fregin A, Heiberg AC, Baert K, MacNicoll AD, Prescott CV, Walker AS, Oldenburg J, Müller CR2005 Aug15879509
Engineering of a recombinant vitamin K-dependent gamma-carboxylation system with enhanced gamma-carboxyglutamic acid forming capacity: evidence for a functional CXXC redox center in the system.Wajih N, Sane DC, Hutson SM, Wallin R2005 Mar 1815640149