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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Yeast-like Candida utilis has been metabolically engineered by pyruvate decarboxylase deletion and L-lactate dehydrogenase expression to produce lactic acid from glucose with yield of 95% [4].
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.
These findings were demonstrated by Lam-Himlin et al, (5) who designed 2 sets of primers using sequence data from GenBank to target proximal, mid, and terminal regions of the 16S rRNA gene (AF110272.1) and the pyruvate decarboxylase gene (AF354297.1) of S ventriculi.
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.e.
In a two-step pathway, pyruvate is converted to acetaldehyde by the enzyme pyruvate decarboxylase (PDC, EC
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.
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).
PDH E1[alpha] subunit (pyruvate decarboxylase; EC deficiency (McKusick 312170) is an X-linked error of metabolism, and diagnosis is usually based on measurement of enzyme activity.
The corn kernels contain a multi-enzyme complex, called the pyruvate decarboxylase system, which lops off carbon dioxide molecules from certain compounds, including pyruvate.