Enzymes
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- Name help_outline 3-hydroxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone Identifier CHEBI:18298 Charge 0 Formula C31H48O3 InChIKeyhelp_outline OOJSROHRRKVBFW-MNBFGQJISA-N SMILEShelp_outline CC(C)CCC[C@@H](C)CCC[C@@H](C)CCC\C(C)=C\CC1(O)C(C)C(=O)c2ccccc2C1=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline oxidized dithiothreitol Identifier CHEBI:41837 (Beilstein: 1280351) help_outline Charge 0 Formula C4H8O2S2 InChIKeyhelp_outline YPGMOWHXEQDBBV-QWWZWVQMSA-N SMILEShelp_outline S1SC[C@H]([C@@H](C1)O)O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1,4-dithiothreitol Identifier CHEBI:18320 (Beilstein: 8144556; CAS: 3483-12-3) help_outline Charge 0 Formula C4H10O2S2 InChIKeyhelp_outline VHJLVAABSRFDPM-UHFFFAOYSA-N SMILEShelp_outline OC(CS)C(O)CS 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2,3-epoxyphylloquinone Identifier CHEBI:15759 Charge 0 Formula C31H46O3 InChIKeyhelp_outline KUTXFBIHPWIDJQ-HBDFACPTSA-N SMILEShelp_outline CC(C)CCC[C@@H](C)CCC[C@@H](C)CCC\C(C)=C\CC12OC1(C)C(=O)c1ccccc1C2=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:21560 | RHEA:21561 | RHEA:21562 | RHEA:21563 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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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 R.B.
An enzyme from bovine liver microsomes that catalyzes the reduction of vitamin K 2,3-epoxide to 2- and 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone was purified 1152-fold to apparent homogeneity. Microsomes were solubilized with 3-[3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CH ... >> More
An enzyme from bovine liver microsomes that catalyzes the reduction of vitamin K 2,3-epoxide to 2- and 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone was purified 1152-fold to apparent homogeneity. Microsomes were solubilized with 3-[3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), and the enzyme was purified by chromatography on PBE-94 ion exchanger, hydroxylapatite, and DEAE-cellulose, and then gel filtration on Sephacryl S-200. The homogeneity of the final preparation was established by polyacrylamide slab gel electrophoresis in the presence of sodium dodecyl sulfate. The molecular weight of the native enzyme is 25,000 and that of denatured enzyme is 12,400, which suggests that the enzyme is a dimer with identical subunits. No chromophoric cofactors are associated with the enzyme. Dithiothreitol and CHAPS are essential for activity, but high concentrations of glycerol reduces the activity. The enzyme is not inhibited by warfarin, a potent inhibitor of the vitamin K epoxide reductase, which catalyzes the conversion of vitamin K 2,3-epoxide to vitamin K. Evidence is presented indicating that the purified enzyme is not simply a fragment of the warfarin-sensitive vitamin K epoxide reductase. << Less
Proc Natl Acad Sci U S A 82:2713-2717(1985) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.