Results 141 to 150 of about 8,906,109 (167)

Tissue distribution and warfarin sensitivity of vitamin K epoxide reductase

Biochemical Pharmacology, 1988
The distribution of vitamin K epoxide reductase activity and its sensitivity to warfarin have been examined in whole microsomes from tissues of both control and warfarin-resistant strain rats. The distribution of activity roughly paralleled that previously shown for the vitamin K-dependent carboxylase. Activity on a per gram tissue basis was highest in
S E, Hazelett, P C, Preusch
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Two enzymes catalyze vitamin K 2,3-epoxide reductase activity in mouse: VKORC1 is highly expressed in exocrine tissues while VKORC1L1 is highly expressed in brain [PDF]

Thrombosis Research, 2015
VKORC1 and VKORC1L1 are enzymes that both catalyze the reduction of vitamin K2,3-epoxide via vitamin K quinone to vitamin K hydroquinone. VKORC1 is the key enzyme of the classical vitamin K cycle by which vitamin K-dependent (VKD) proteins are γ ...
, Johannes Oldenburg, Matthias Watzka
exaly   +2 more sources

Substituted vitamin K epoxide analogs. New competitive inhibitors and substrates of vitamin K1 epoxide reductase

Journal of Medicinal Chemistry, 1990
2- and 3-substituted vitamin K 2,3-epoxide analogues were synthesized and tested as inactivators, inhibitors, and substrates for beef liver microsomal vitamin K1 epoxide reductase. 2-(X)-3-phytyl-1,4-naphthoquinone 2,3-epoxides, where X is hydroxymethyl, chloromethyl, fluoromethyl, difluoromethyl, and formyl were all competitive inhibitors, but none ...
R P, Ryall, D L, Nandi, R B, Silverman
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Substrate specificity of vitamin K epoxide reductase C1

Hämostaseologie, 2009
Substratspezifitat der Vitamin-K-Epoxid reduktase C1 Hamostaseologie 2009; 29 (Suppl 1): S116 Vitamin K epoxide reductase C1 (VKORC1) acts in vitamin K recycling in order to enable its reutilisation. Vitamin K is a co-factor of γ-carboxylase, an enzyme responsible for functional active blood coagulation factors and other vitamin K dependent proteins ...
J. Oldenburg, D. Lütjohann, M. Hass, P. Westhofen, M. Watzka, M. Marinova   +5 more
openaire   +1 more source

A chemical model for the mechanism of vitamin K epoxide reductase

The Journal of Organic Chemistry, 1983
Etude des reactions de l'epoxyde de la vitamine K 1 et de l'epoxyde de la dimethyl-2,3 naphtoquinone-1,4 avec le dithiothreitol et le mercapto-2 ...
Peter C. Preusch, J. W. Suttie
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Comparison of vitamin K1 and K2 kinetics of vitamin K epoxide reductase C1

Hämostaseologie, 2008
Vitamin K is a co-factor of γ-carboxylase, an enzyme responsible for functional active blood coagulation factors. Carboxylation requires hydroquinone and results in its conversion to vitamin K epoxide. The vitamin K epoxide is recycled to vitamin K before it can be reutilised. This reaction is catalyzed by the enzyme vitamin K epoxide reductase (VKORC1)
J. Oldenburg, D. Lütjohann, C. Müller-Reible, M. Hass, M. Watzka, P. Westhofen, M. Marinova   +6 more
openaire   +1 more source

Solubilization of vitamin K epoxide reductase and vitamin K-dependent carboxylase from rat liver microsomes

Biochemical and Biophysical Research Communications, 1978
Abstract Vitamin K epoxide reductase and vitamin K-dependent carboxylase have been solubilized by treatment of rat liver microsomes with potassium cholate. Both reactions required dithiothreitol, and were inhibited by warfarin. NADH did not replace the dithiothreitol requirement.
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Vitamin-K-epoxide reductase (warfarin sensitive)

1995
Dietmar Schomburg, Dörte Stephan
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Purification of vitamin K 2,3 epoxide reductase

Biochemical Society Transactions, 1999
Anthony Hill, C. Pallister, D. Cowell, G. Steventon   +3 more
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Kinetics of vitamin K 2,3 epoxide reductase

Biochemical Society Transactions, 1999
L.A. Begent, S.T. Chan, G.B. Steventon
openaire   +1 more source