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Membrane Enzymes: Artifacts in Arrhenius Plots Due to Temperature Dependence of Substrate-Binding Affinity

John R. Silvius, Brian D. Read, Ronald N. McElhaney

Open publisher page 132 citations

Abstract

For the membrane sodium-stimulated magnesium-adenosinetriphosphatase of Acholeplasma laidlawii B both the Vmax and Km values in the Michaelis equation very strongly with temperature. Simulations of Arrhenius plots show that an enzyme with a temperature-dependent Km can yield a variety of Arrhenius plot artifacts, most notably erroneous "breaks," if activity is assayed at a fixed substrate concentration.

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What this paper is about

For the membrane sodium-stimulated magnesium-adenosinetriphosphatase of Acholeplasma laidlawii B both the Vmax and Km values in the Michaelis equation very strongly with temperature. Simulations of Arrhenius plots show that an enzyme with a temperature-dependent Km can yield a variety of Arrhenius plot artifacts, most notably erroneous "breaks," if activity is assayed at a fixed substrate concentration.

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OpenAlex reports 132 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

For the membrane sodium-stimulated magnesium-adenosinetriphosphatase of Acholeplasma laidlawii B both the Vmax and Km values in the Michaelis equation very strongly with temperature. Simulations of Arrhenius plots show that an enzyme with a temperature-dependent Km can yield a variety of Arrhenius plot artifacts, most notably erroneous "breaks," if activity is assayed at a fixed substrate concentration.

Key concepts: Arrhenius plot, Arrhenius equation, Substrate (aquarium), Enzyme, Chemistry, Yield (engineering), Membrane, Michaelis–Menten kinetics

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Membrane Enzymes: Artifacts in Arrhenius Plots Due to Temperature Dependence of Substrate-Binding Affinity — Research Paper | ScholarLens