Pyruvate decarboxylase  (Synonyms: PDC)

Pyruvate decarboxylase (PDC) is an enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde. Pyruvate decarboxylase catalyses the non-oxidative conversion of pyruvate (or other 2-oxo acids) to acetaldehyde and CO₂^[1].

Pyruvate decarboxylase is a key enzyme in alcoholic fermentation. Pyruvate decarboxylase is found in yeast, some bacteria and a number of plants. All the Pyruvate decarboxylases from yeast and bacteria studied so far are tetramers in the native state and built up of identical or almost identical subunits with molecular masses of about 60 kDa. Plant Pyruvate decarboxylases are organised in higher oligomers although the subunit masses are similar to those from yeast and bacteria^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

9001-04-1

Solid

White to off-white

[Pyruvate decarboxylase]

4.1.1.1

≥1 U/mg soild

One unit is defined as the amount of enzyme that will can converts 1 μmol of pyruvic acid to acetaldehyde per minute at pH 6.0, 25°C.

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. König S. Subunit structure, function and organisation of pyruvate decarboxylases from various organisms. Biochim Biophys Acta. 1998 Jun 29;1385(2):271-86.  [Content Brief]