Studies on the Mechanism of the Pyruvate Oxidase Flavoprotein of Escherichia Coli (Rapid Kinetics, Biochemical Software, Lipid-Activated Enzyme)
The pyruvate oxidase flavoprotein catalyzes the oxidative decarboxylation of pyruvate to acetate and carbon dioxide. Flavin adenine dinucleotide and thiamin pyrophosphate are cofactors. The enzymatic activity of the purfied flavoprotein is very low in the absence of lipids. Following reduction by substrate, lipids and many other other amphiphilic substances bind to a high affinity site on the flavoenzyme and stimulate the activity about 25 fold. The enzyme can also be activated by controlled proteolysis of the reduced flavoenzyme, which destroys the high affinity lipid site.
University of Illinois - Urbana-Champaign
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University of Illinois at Urbana-Champaign