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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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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
Systems-level analysis of mechanisms regulating yeast metabolic flux
Hackett S R, et al.
Science, 354(6311), aaf2786-aaf2786 (2016)
Bijayalaxmi Mohanty et al.
Annals of botany, 91 Spec No, 291-300 (2003-01-02)
Submergence tolerance of 13 doubled haploid lines of rice and their parents (submergence tolerant FR13A and submergence intolerant CT6241) was assessed using 2-week-old seedlings. Plants were scored for leaf senescence and percentage of seedlings that survived up to 15 d
Substrate activation behaviour of pyruvate decarboxylase from Pisum sativum cv. Miko
Dietrich A and Konig S
Febs Letters, 400(1), 42-44 (1997)
Danilo Meyer et al.
Journal of the American Chemical Society, 133(10), 3609-3616 (2011-02-24)
Pyruvate decarboxylase (PDC) catalyzes the decarboxylation of pyruvate into acetaldehyde and CO(2) and requires the cofactors thiamin diphosphate and Mg(2+) for activity. Owing to its catalytic promiscuity and relaxed substrate specificity, PDC catalyzes carboligation side reactions and is exploited for

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