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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)

Synonyme(s) :

2-Oxo-acid carboxy-lyase

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About This Item

Numéro CAS:
9001-04-1
Numéro de classification (Commission des enzymes):
4.1.1.1 (BRENDA, IUBMB)
Numéro MDL:
MFCD00132144
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Forme

ammonium sulfate suspension

Activité spécifique

5.0-20.0 units/mg protein (biuret)

Température de stockage

2-8°C

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Description générale

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.

Actions biochimiques/physiologiques

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.

Définition de l'unité

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

Forme physique

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.

Notes préparatoires

Isolated without the use of heavy metals.

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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Applied and environmental microbiology, 68(2), 831-837 (2002-02-02)
Purification of xylulose 5-phosphate phosphoketolase (XpkA), the central enzyme of the phosphoketolase pathway (PKP) in lactic acid bacteria, and cloning and sequence analysis of the encoding gene, xpkA, from Lactobacillus pentosus MD363 are described. xpkA encodes a 788-amino-acid protein with
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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.
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