Abstract
High affinity lipid binding sites on the peripheral membrane enzyme pyruvate oxidase. Specific ligand effects on detergent binding.
Highlights
Pyruvate oxidase is a peripheral membrane enzyme which has been purified to homogeneity from Escherichia coli
Lipids and detergents clearly have a substantial effect on the V, of the enzymatic reaction and modulate the binding interactions between the enzyme and the ligands involved in catalysis, pyruvate and thiamin pyrophosphate [7]
This paper presents the characterization of the interaction between SDS4 and pyruvate oxidase as studied by equilibrium dialysis
Summary
The simultaneous presence of both the substrate, pyruvate, and the cofactor, thiamin pyrophosphate, results in a large increase of the affinity of the oxidase for SDS at detergent concentrations which elicit activation. Fluoropyruvate, a competitive inhibitor of pyruvate oxidase, can be substituted for pyruvate and has a similar effect on the SDS-binding isotherm in the presence of thiamin pyrophosphate. It is clear that there is a ligandinduced conformational change in pyruvate oxidase which has dramatic effects on the properties of the enzyme This conformational change results in a great enhancement of the detergent-protein interactions which are observed. Lipids and detergents clearly have a substantial effect on the V,,,,, of the enzymatic reaction and modulate the binding interactions between the enzyme and the ligands involved in catalysis, pyruvate and thiamin pyrophosphate [7]. This paper presents the characterization of the interaction between SDS4 and pyruvate oxidase as studied by equilibrium dialysis
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