Application

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.

Biochem/physiol Actions

Pyruvate decarboxylase(PDC) actively participates in the anaerobic metabolismof several bacteria, yeast andplant 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 β-α-β structure, yielding parallel β-sheets.

General description

Pyruvate decarboxylase(PDC) usually appear in plant seeds at the time of germination, especially when theplant embryois totally covered by an oxygen-impermeable testa.

Packaging

500 units in glass bottle

Physical form

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.

Preparation Note

Isolated without the use of heavy metals.

Unit Definition

One unit will convert 1.0 µmole of pyruvate to acetaldehyde per min at pH 6.0 at 25 °C.