Pyruvate oxidase is a peripheral membrane enzyme isolated from Escherichia coli. Pyruvate oxidase catalyzes the oxidative carboxylation of pyruvate to yield the phosphoryl donor, acetyl phosphate releasing CO2 and H2O2. Most bacterial pyruvate oxidases require Mg(II) to bind the thiamine pyrophosphate cofactor in the active site.
Activity: 40 units/mg powder. One unit is defined as amount of enzyme required to generate 1umol of H202 per minute at 37C, pH 6.5. Contaminate info: Glutamate oxalacetate transaminase (GOT) 002% by activity; Glutamate pyruvate transaminase (GPT) 006% by activity; Lactate Oxidase 002% by activity; Catalase not detectable.
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