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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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F Dyda et al.
Biochemistry, 32(24), 6165-6170 (1993-06-22)
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.
Clara C Posthuma et al.
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
Liangliang Zhao et al.
Wei sheng wu xue bao = Acta microbiologica Sinica, 51(1), 50-58 (2011-04-07)
We developed an engineered Sacchromyces cerevisiae strain to produce L-lactic acid efficiently by using glucose as carbon source. For construction of the strain CEN. PK2-1C [LDH], we integrated an LDH gene coding L-lactic acid dehydrogenase from bovine into the genome
Vishal Chugh et al.
Indian journal of biochemistry & biophysics, 48(5), 346-352 (2011-12-15)
The present investigation was undertaken to identify the possible mode of mechanism that could provide tolerance to maize (Zea mays L.) seedlings under waterlogging. Using cup method, a number of maize genotypes were screened on the basis of survival of
Kyung Ok Yu et al.
Applied biochemistry and biotechnology, 166(4), 856-865 (2011-12-14)
The conversion of low-priced glycerol to higher value products has been proposed as a way to improve the economic viability of the biofuels industry. In a previous study, the conversion of glycerol to ethanol in a metabolically engineered strain of

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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