Description
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.
Abbr
PDC, Native (Baker's Yeast (S. cerevisiae))
Source
Baker's yeast (S. cerevisiae)
Applications
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.
Form
ammonium sulfate suspension; 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 c ocarboxylase.
Enzyme Commission Number
EC 4.1.1.1
Activity
5.0-20.0 units/mg protein (biuret)
Unit Definition
One unit will convert 1.0 μmole of pyruvate to acetaldehyde per min at pH 6.0 at 25°C.
Warnings
Isolated without the use of heavy metals.
Synonyms
Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC
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