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P9474

Sigma-Aldrich

Pyruvate Decarboxylase from baker′s yeast (S. cerevisiae)

ammonium sulfate suspension, 5.0-20.0 units/mg protein (biuret)

Synonym(s):

2-Oxo-acid carboxy-lyase

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

ammonium sulfate suspension

specific activity

5.0-20.0 units/mg protein (biuret)

storage temp.

2-8°C

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General description

Pyruvate decarboxylase (PDC) usually appear in plant seeds at the time of germination, especially when the plant embryo is totally covered by an oxygen-impermeable testa.

Application

Pyruvate Decarboxylase from baker′s yeast (S. cerevisiae) has been used to evaluate the power of systematic identification of meaningful metabolic enzyme regulation (SIMMER) for finding unknown yeast regulatory interactions.
Pyruvate decarboxylase (PDC) is used to study residues involved in thiamine pyrophosphate (TPP) binding. It is used to study the regulation of fermentation pathways in plant species.

Biochem/physiol Actions

Pyruvate decarboxylase (PDC) is a homotetrameric enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde and carbon dioxide in the cytoplasm. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. PDC contains a β-α-β structure, yielding parallel β-sheets.
Pyruvate decarboxylase (PDC) actively participates in the anaerobic metabolism of several bacteria, yeast and plant seeds.

Unit Definition

One unit will convert 1.0 μmole of pyruvate to acetaldehyde per min at pH 6.0 at 25 °C.

Physical form

Suspension in 3.2 M (NH4)2SO4 pH 6.5, stabilized with 5% glycerol, 5 mM potassium phosphate, 1 mM magnesium acetate, 0.5 mM EDTA, and 25 μM cocarboxylase.

Preparation Note

Isolated without the use of heavy metals.

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Dietrich A and Konig S
Febs Letters, 400(1), 42-44 (1997)
F Dyda et al.
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The crystal structure of brewers' yeast pyruvate decarboxylase, a thiamin diphosphate dependent alpha-keto acid decarboxylase, has been determined to 2.4-A resolution. The homotetrameric assembly contains two dimers, exhibiting strong intermonomer interactions within each dimer but more limited ones between dimers.
Systems-level analysis of mechanisms regulating yeast metabolic flux
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Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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