What does pyruvate decarboxylase produce?

Pyruvate decarboxylase is an enzyme that catalyzes the reaction of decarboxylating pyruvate into acetaldehyde, releasing carbon dioxide in the process. This enzyme is primarily involved in alcoholic fermentation in yeasts and certain bacteria. The production of carbon dioxide and acetaldehyde is a crucial step in the conversion of pyruvate under anaerobic conditions.

Acetaldehyde can subsequently be converted into ethanol, but the direct output of pyruvate decarboxylase itself is indeed carbon dioxide and acetaldehyde, not Acetyl CoA. Acetyl CoA is formed in aerobic pathways (such as the TCA cycle) from pyruvate via the pyruvate dehydrogenase complex.

Therefore, while the understanding of pyruvate metabolism is broad and contains many pathways and products, the specific activity of pyruvate decarboxylase distinctly results in the release of carbon dioxide.