1.17.4.4: vitamin-K-epoxide reductase (warfarin-sensitive)

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For detailed information about vitamin-K-epoxide reductase (warfarin-sensitive), go to the full flat file.

Reaction

Synonyms

EC 1.1.4.1, phylloquinone epoxide reductase, reductase, phylloquinone epoxide, vitamin K 2,3-epoxide reductase, vitamin K 2,3-epoxide reductase complex subunit 1, vitamin K 2,3-epoxide reductase complex subunit-1, vitamin K epoxid reductase, vitamin K epoxide reductase, vitamin K epoxide reductase complex subunit 1, vitamin K oxidoreductase, Vitamin K reductase, vitamin K-2,3-epoxide reductase, vitamin K-2,3-epoxide reductase subunit 1, vitamin K-epoxide reductase, vitamin K1 epoxide reductase, vitaminK epoxide reductase, VKOR, VKOR complex, VKORC1, VKORC1 variant 2, VKORC1-like 1, VKORC1L1, VKORC1v2, warfarin sensitive vitamin K 2,3-epoxide reductase, warfarin-sensitive vitamin K1 2,3-epoxide reductase

ECTree

     1 Oxidoreductases

         1.17 Acting on CH or CH₂ groups

             1.17.4 With a disulfide as acceptor

                1.17.4.4 vitamin-K-epoxide reductase (warfarin-sensitive)

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Results	in table
25	Activating Compound
2046	AA Sequence
13	Application
1	CAS Registry Number
43	Cloned(Commentary)
7	Cofactor
1	Crystallization (Commentary)
646	Disease/ Diagnostics
7	Expression
42	General Information
7	General Stability
52	IC50 Value
121	Inhibitors
68	Ki Value [mM]
43	KM Value [mM]
80	Localization
7	Metals/Ions
4	Molecular Weight [Da]
70	Natural Substrates/ Products (Substrates)
4	Organic Solvent Stability
490	Organism
1	Oxidation Stability
6	Pathway
22	PDB ID
20	pH Optimum
1	pH Range
1	pI Value
2	Posttranslational Modification
151	Protein Variants
20	Purification (Commentary)
9	Reaction
3	Reaction Type
125	Reference
1	Renatured (Commentary)
99	Source Tissue
16	Specific Activity [micromol/min/mg]
1	Storage Stability
144	Substrates and Products (Substrate)
8	Subunits
195	Synonyms
1	Systematic Name
18	Temperature Optimum [°C]
2	Temperature Range [°C]
4	Temperature Stability [°C]
6	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.17.4.4 - vitamin-K-epoxide reductase (warfarin-sensitive)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

sitting-drop vapor-diffusion method, the structure of the mutant enzyme Cys50Ala at 2.8 A resolution allows a detailed analysis of an intramembrane enzyme that generates disulfide bonds. In the active site, a continuous electron density connects the thiol group of Cys133 with the C1 atom of the quinone ring. The Cys212Ala structure suggests that the transfer of electrons to the active site is an one-electron process

Synechococcus sp. JA-2-3B'a(2-13)

Q2JJF6

745849