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  3. Pyruvate decarboxylase

Pyruvate decarboxylase (PDC) is an enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde. Pyruvate decarboxylase catalyses the non-oxidative conversion of pyruvate (or other 2-oxo acids) to acetaldehyde and CO2.

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Pyruvate decarboxylase Chemical Structure

Pyruvate decarboxylase Chemical Structure

CAS No. : 9001-04-1

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Description

Pyruvate decarboxylase (PDC) is an enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde. Pyruvate decarboxylase catalyses the non-oxidative conversion of pyruvate (or other 2-oxo acids) to acetaldehyde and CO2[1].

In Vitro

Pyruvate decarboxylase is a key enzyme in alcoholic fermentation. Pyruvate decarboxylase is found in yeast, some bacteria and a number of plants. All the Pyruvate decarboxylases from yeast and bacteria studied so far are tetramers in the native state and built up of identical or almost identical subunits with molecular masses of about 60 kDa. Plant Pyruvate decarboxylases are organised in higher oligomers although the subunit masses are similar to those from yeast and bacteria[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

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[Pyruvate decarboxylase]

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Pyruvate decarboxylase Related Classifications

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  • Do most proteins show cross-species activity?

    Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

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Pyruvate decarboxylase
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HY-P2796
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