Pyruvate Decarboxylase


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The following article is from The Great Soviet Encyclopedia (1979). It might be outdated or ideologically biased.

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:

CH3COCOOH → CH3CHO + CO2

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—).

L. S. KHAILOVA

The Great Soviet Encyclopedia, 3rd Edition (1970-1979). © 2010 The Gale Group, Inc. All rights reserved.
References in periodicals archive ?
Acetoin and phenylacetylcarbinol formation by the pyruvate decarboxylase of Zymomonas mobilis and Saccharomyces carlsbergensis.
Pyruvate decarboxylase activity (PDC) was determined by measuring the rate of acetaldehyde production as described previously [6] with some modifications.
However, the absence of the commonly known pyruvate decarboxylase (PDC) is a perplexing feature of hyperthermophiles [15].
Zeikus, "Purification and characterization of pyruvate decarboxylase from Sarcina ventriculi," Journal of General Microbiology, vol.
Doelle, "Purification and kinetic characteristics of pyruvate decarboxylase and ethanol dehydrogenase from Zymomonas mobilis in relation to ethanol production," European Journal of Applied Microbiology and Biotechnology, vol.
Schneider, "A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase," Structure, vol.
Maupin-Furlow, "Pyruvate decarboxylase: a key enzyme for the oxidative metabolism of lactic acid by Acetobacter pasteurianus," Archives of Microbiology, vol.
Maupin-Furlow, "Cloning and characterization of the Zymobacter palmae pyruvate decarboxylase gene (PDC) and comparison to bacterial homologues," Applied and Environmental Microbiology, vol.
Guo et al., "Catalytic acid--base groups in yeast pyruvate decarboxylase. 1: site-directed mutagenesis and steady-state kinetic studies on the enzyme with the D28A, H114F, H115F, and E477Q substitutions," Biochemistry, vol.
Pyruvate decarboxylase, the target for omeprazole in metronidazole resistant and iron restricted Tritrichomonas foetus in vitro.
[5] Nonstandard abbreviations: PDHc, pyruvate dehydrogenase complex; E1, pyruvate decarboxylase; E2, dihydrolipoic transacetylase; E3, dihydrolipoyl dehydrogenase; TPP, thiamine pyrophosphate; PMS, phenazine methosulfate; INT, p-iodonitrotetrazolium violet; BSA, bovine serum albumin; DCA, dichloroacetic acid; DTT, dithiothreitol; PBS, phosphate-buffered saline; SMP, submitochondrial particle from bovine heart; MEF, mitochondria-enriched fraction; DQA, 2-n-decylquinazolin-4-yl-amine; and LD, lactate dehydrogenase.