pyruvate decarboxylase


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py·ru·vate de·car·box·yl·ase

α-carboxylase; α-ketoacid carboxylase; a thiamin-pyrophosphate-dependent carboxylase of yeast catalyzing decarboxylation of a 2-oxoacid (for example, pyruvate) to an aldehyde (for example, acetaldehyde) without oxidoreduction and without lipoamide, in contrast to pyruvate dehydrogenase (lipoamide).
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This alteration leads to the accumulation of malate, reduces pyruvate dehydrogenase activity and increases the activity of malic and pyruvate decarboxylase enzymes, thus increasing the formation of acetaldehyde.
However, the organism can also be confirmed at a molecular level by polymerase chain reaction and sequencing of the 16S ribosomal RNA (rRNA) gene and pyruvate decarboxylase gene.
The production of the 1-hydroxy-1-phenyl-2-propanoneis carried out by pyruvate decarboxylase (PDC) and is accompanied with the formation of by-productsi.
In anaerobic metabolism (alcohol fermentation), pyruvate, primarily produced in glycolysis, is transformed into acetaldehyde by pyruvate decarboxylase enzyme and the acetaldehyde is reduced to ethanol by ADH.