Pyruvate Decarboxylase from baker's yeast (S. cerevisiae) has been used to evaluate the power of systematic identification of meaningful metabolic enzyme regulation (SIMMER) for finding unknown yeast regulatory interactions.
Pyruvate decarboxylase (PDC) is used to study residues involved in thiamine pyrophosphate (TPP) binding. It is used to study the regulation of fermentation pathways in plant species.
Pyruvate decarboxylase (PDC) actively participates in the anaerobic metabolism of several bacteria, yeast and plant seeds.
Pyruvate decarboxylase (PDC) is a homotetrameric enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde and carbon dioxide in the cytoplasm. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. PDC contains a ß-a-ß structure, yielding parallel ß-sheets.
Pyruvate decarboxylase (PDC) usually appear in plant seeds at the time of germination, especially when the plant embryo is totally covered by an oxygen-impermeable testa.
500 units in glass bottle
Suspension in 3.2 M (NH4)2SO4 pH 6.5, stabilized with 5% glycerol, 5 mM potassium phosphate, 1 mM magnesium acetate, 0.5 mM EDTA, and 25 µM cocarboxylase.
Isolated without the use of heavy metals.
One unit will convert 1.0 µmole of pyruvate to acetaldehyde per min at pH 6.0 at 25 °C.