Pyruvate decarboxylase

<p>Pyruvate decarboxylase is an <a href="/facts/Enzyme/DSI1Fh7y">enzyme</a> (<a href="/facts/Enzyme_Commission_number/Y5GNLRKX">EC</a> <a href="https://www.enzyme-database.org/query.php?ec=4.1.1.1">4.1.1.1</a>) that <a href="/facts/Catalysis/LPBS7TQC">catalyses</a> the decarboxylation of <a href="/facts/Pyruvic_acid/qJTgl4J9">pyruvic acid</a> to <a href="/facts/Acetaldehyde/QllLbSUe">acetaldehyde</a>. It is also called 2-oxo-acid carboxylase, alpha-ketoacid carboxylase, and pyruvic decarboxylase.  In anaerobic conditions, this enzyme participates in the fermentation process that occurs in yeast, especially of the genus <i><a href="/facts/Saccharomyces/uvqNvGje">Saccharomyces</a></i>, to produce <a href="/facts/Ethanol/3lCLfBSP">ethanol</a> by fermentation. It is also present in some species of fish (including <a href="/facts/Goldfish/Wdkw4kIL">goldfish</a> and <a href="/facts/Carp/8VFzFsYk">carp</a>) where it permits the fish to perform ethanol fermentation (along with lactic acid fermentation) when oxygen is scarce. Pyruvate decarboxylase starts this process by converting pyruvate into acetaldehyde and carbon dioxide.  Pyruvate decarboxylase depends on <a href="/facts/Cofactor_(biochemistry)/AGo0PCUU">cofactors</a> <a href="/facts/Thiamine_pyrophosphate/xGQAGmhC">thiamine pyrophosphate</a> (TPP) and magnesium. This enzyme should not be mistaken for the unrelated enzyme <a href="/facts/Pyruvate_dehydrogenase/VpJt0RLA">pyruvate dehydrogenase</a>, an oxidoreductase (<a href="/facts/Enzyme_Commission_number/Y5GNLRKX">EC</a> <a href="https://enzyme.expasy.org/EC/1.2.4.1">1.2.4.1</a>), that catalyzes the oxidative decarboxylation of pyruvate to <a href="/facts/Acetyl-CoA/XyxFfC84">acetyl-CoA</a>.
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Pyruvate decarboxylase open-in-new

Pyruvate decarboxylase