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The Regulation of HMG-CoA Reductase by Enzyme-Lipid Interactions

The temperature-dependent catalytic activity of rat liver 3-hydroxy-3 -methylglutaryl coenzyme A reductase (HMG-CoA reductase) displays the nonlinear Arrhenius behavior characteristic of many membrane-bound enzymes. A two-conformer equilibrium model has been developed to characterize this behavior. In the model, HMG-CoA reductase undergoes a conformational change from a low specific activity to a high specific activity form. This conformation change is apparently driven by a temperature-dependent phase transition of the membrane lipids. It has been found that this model accurately describes the data from diets including rat chow, low-fat, high-carbohydrate, and diets supplemented with fat, cholesterol or cholestyramine. The effects characterized by the model are consistent with the regulation of HMG-CoA reductase by enzyme-lipid interactions.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc504046
Date05 1900
CreatorsSmith, Vana L.
ContributorsThompson, Richard E., Norton, S. J., Russell, Benny
PublisherNorth Texas State University
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
Formatiii, 84 leaves: ill., Text
RightsPublic, Smith, Vana L., Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved.

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