Results 121 to 130 of about 8,906,109 (167)

Phosphite inhibits <i>Phytophthora cinnamomi</i> by downregulating oxidoreductases and disrupting energy metabolism. [PDF]

Front Microbiol
Prabhu SA, Naicker P, Duong TA, Govender IS, Engelbrecht J, Backer R, Stoychev SH, van den Berg N.   +7 more
europepmc   +1 more source

Warfarin analogs target disulfide bond-forming enzymes and suggest a residue important for quinone and coumarin binding. [PDF]

J Biol Chem
Chavez D, Amarquaye GN, Mejia-Santana A, Dyotima, Ryan K, Zeng L, Landeta C.   +6 more
europepmc   +1 more source

Disulfide bonds are critical for stabilizing cell division, cell envelope biogenesis, and antibiotic resistance proteins in mycobacteria. [PDF]

mBio
Mejia-Santana A, Collins R, Doud EH, Landeta C.   +3 more
europepmc   +1 more source

Structural Investigation of the Vitamin K Epoxide Reductase (VKORC1) Binding Site with Vitamin K

Biochemistry, 2020
The vitamin K epoxide reductase (VKORC1) enzyme is of primary importance in many physiological processes, i.e., blood coagulation, energy metabolism, and arterial calcification prevention, due to its role in the vitamin K cycle. Indeed, VKORC1 catalyzes reduction of vitamin K epoxide to quinone and then to hydroquinone.
Chatron, Nolan, Abi Khalil, Rami, Benoit, Etienne, Lattard, Virginie   +3 more
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Structural and functional insights into human vitamin K epoxide reductase and vitamin K epoxide reductase-like1

Critical Reviews in Biochemistry and Molecular Biology, 2013
Human vitamin K epoxide reductase (hVKOR) is a small integral membrane protein involved in recycling vitamin K. hVKOR produces vitamin K hydroquinone, a crucial cofactor for γ-glutamyl carboxylation of vitamin K dependent proteins, which are necessary for blood coagulation.
Wade Van Horn
exaly   +3 more sources

Relationship of dithiothreitol-dependent microsomal vitamin K quinone and vitamin K epoxide reductases Inhibition of epoxide reduction by vitamin K quinone

Biochimica Et Biophysica Acta - General Subjects, 1984
Vitamin K quinone was shown to be an effective inhibitor of vitamin K epoxide reduction by whole rat liver microsomes. Observation of inhibition was dependent upon the mode of addition of the substrate and inhibitor suggesting segregation of the compounds into different microsomal vesicles under certain conditions.
J W Suttie, John W Suttie, P C Preusch
exaly   +3 more sources

Effect of n-methyl-thiotetrazole on vitamin k epoxide reductase

Thrombosis Research, 1986
Clinical use of antibiotics containing a N-methyl-thiotetrazole (NMTT) side chain has been reported to be associated with an increased incidence of a vitamin K-responsive hypoprothrombinemia. Administration of NMTT to rats decreased the activity of the liver microsomal vitamin K epoxide reductase, increased the liver ratio of vitamin K epoxide to ...
J W Suttie, J W Suttie
exaly   +3 more sources

Vitamin K 2,3-epoxide reductase and the vitamin K-dependent γ-carboxylation system

Thrombosis Research, 2002
Vitamin K is an essential cofactor for post translational gamma-carboxylation of vitamin K-dependent coagulation factors. The modification is carried out by a system of integral proteins of the endoplasmic reticulum (ER) membrane where the warfarin sensitive vitamin K 2,3-epoxide reductase (VKOR) produces the reduced hydroquinone form of vitamin K (vit.
Reidar Wallin, Susan M Hutson
exaly   +3 more sources

Vitamin K Epoxide Reductase Complex Subunit 1 (VKORC1): The Key Protein of the Vitamin K Cycle

Antioxidants & Redox Signaling, 2006
Vitamin K epoxide, a by-product of the carboxylation of blood coagulation factors, is reduced to vitamin K by an enzymatic system possessing vitamin K epoxide reductase (VKOR) activity. This system is the target of coumarin-derived drugs widely used in thrombosis therapy and prophylaxis. Recently, the key protein of the VKOR system has been identified.
Oldenburg, J., Bevans, C., Müller, C., Watzka, M.   +3 more
openaire   +4 more sources

Vitamin K epoxide reductase activity in the metabolism of epoxides

Biochemical Pharmacology, 1985
The importance of vitamin K epoxide reductase for the metabolism of a range of structurally diverse epoxides has been investigated. Vitamin K1 epoxide is reduced by rat liver microsomes at a rate of 0.47 nmoles/g liver/min. The rate of menadione oxide reduction is not significantly higher than the non-enzymatic reduction rate.
I, Liptay-Reuter, K, Dose, T, Guenthner, W, Wörner, F, Oesch   +4 more
openaire   +2 more sources