Pyruvate Decarboxylase

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Pyruvate Decarboxylase


an enzyme of the lyase class that takes part in the anaerobic decomposition of carbohydrates in the cells of certain microorganisms, for example, brewer’s yeast, and in the tissues of higher plants. Pyruvate decarboxylase catalyzes the nonoxidative decarboxylation of pyruvic acid, resulting in the formation of acetaldehyde:


The reaction proceeds in the presence of thiamine pyrophosphate, which acts as a coenzyme, and of Mg2+ ions, which act as cofactors. Pyruvate decarboxylase also decarboxylates other alpha keto acids, for example, α-ketobutyric and α-ketovaleric acids. The activity of the enzyme decreases in proportion to the length of the carbon chain in the substrate.

Pyruvate decarboxylase was discovered in yeast in 1911 by the German biochemist C. Neuberg. It is isolated in pure form from plant tissues, for example, brewer’s yeast and wheat germ; the molecular weight of the wheat-germ variety is about 1,000,000. The term “pyruvate decarboxylase” is also used to designate one of the components of pyruvate dehydrogenase, which catalyzes the oxidative decarboxylation of pyruvic acid with the resultant formation of an acetyl group (CH3CO—).


References in periodicals archive ?
Acetoin and phenylacetylcarbinol formation by the pyruvate decarboxylase of Zymomonas mobilis and Saccharomyces carlsbergensis.
An in vitro study demonstrated that omeprazole inhibits the growth of metronidazole resistant bovine pathogen Tritrichomonas foetus by inhibiting the enzyme Pyruvate decarboxylase of the parasite (14).
In this process, specialized strains of yeast (typically a variety of Candida utilis or Saccharomyces cerevisiae) are added to large vats containing water, dextrose and the enzyme pyruvate decarboxylase (such as found in beets and other plants, inter alia).
It consists of six different components: pyruvate decarboxylase (E1; EC 1.