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Key Documents

P4591

Sigma-Aldrich

Pyruvate Oxidase from microorganisms

lyophilized powder, ≥1.5 U/mg

Synonyme(s) :

Pyruvate:oxygen oxidoreductase (phosphorylating)

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Forme

lyophilized powder

Niveau de qualité

Activité spécifique

≥1.5 U/mg

Poids mol.

~260 kDa

Température de stockage

−20°C

Application

Pyruvate Oxidase (PoxB) converts pyruvate directly to acetate and CO2. It is used to study pyruvate metabolism. It is used to study aerobic metabolism of bacterium, such as Lactobacillus plantarumand Streptococcus pneumoniae. Pyruvate Oxidase is used for enzymatic determination of pyruvate, GOT, and GPT in clinical analysis.
Pyruvate Oxidase from microorganisms has been used in the Amplex Red-based fluorescence assay for pyruvate. It has also been used in developing near real-time continuous detection system for pyruvate.

Actions biochimiques/physiologiques

Pyruvate Oxidase consists of four subunits with identical molecular weights. PoxB reacts with certain aldehydes and phosphate can be replaced by arsenate. Oxygen as well as several artificial compounds can function as electron acceptors. Pyruvate Oxidase is activated by phospholipids as well as monomeric and micellar amphiphiles.
Pyruvate Oxidase oxidises pyruvate to form acetate, hydrogen peroxide and carbondioxide. Pyruvate oxidase requires flavin adenine dinucleotide (FAD), thiamine pyrophosphate (TPP) and magnesium as cofactors for its catalytic activity. Pyruvate oxidase is activated by the cofactor thiamine.

Propriétés physiques

Isoelectric point : 4.3
Michaelis constant : 3.4 X 10-4M (Pyruvate)
Inhibitors : Fe++,Zn++,Cu++,Ag+,Hg++
Optimum pH : 5.7
Optimum temperature : 65oC
pH Stability : pH 5.7 - 6.5 (25oC, 20hr)
Thermal stability : below 45oC (pH 6.0, 15min)

Définition de l'unité

One unit will produce 1.0 μmole of H2O2 per min during the conversion of pyruvate and phosphate to acetylphosphate and CO2 at pH 5.7 at 37 °C.

Forme physique

Lyophilized powder containing FAD and sugar as stabilizer

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Multiplexed and fully automated detection of metabolic biomarkers using microdialysis probe
Das C, et al.
Sensors and Actuators B, Chemical, 238, 633-640 (2017)
A sensitive fluorimetric assay for pyruvate
Zhu A, et al.
Analytical Biochemistry, 396(1), 146-151 (2010)
Lan-yan Zheng et al.
International journal of oral science, 3(2), 82-89 (2011-04-13)
The objective of this study was to characterize the oxygen dependent regulation of pyruvate oxidase (SpxB) gene expression and protein production in Streptococcus sanguinis (S. sanguinis). SpxB is responsible for the generation of growth-inhibiting amounts of hydrogen peroxide (H2O2) able
Amit Priyadarshi et al.
Biochemical and biophysical research communications, 380(4), 797-801 (2009-04-03)
MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate) synthase belongs to the superfamily of thiamin diphosphate-dependent decarboxylases, which converts isochorismate and 2-oxoglutarate to SHCHC, pyruvate, and carbon dioxide. Here, we report the first crystal structure of apo-MenD from Escherichia coli determined in tetragonal crystal form. The
Rachel Benisty et al.
Biochimica et biophysica acta, 1801(9), 1098-1104 (2010-07-06)
FabF elongation condensing enzyme is a critical factor in determining the spectrum of products produced by the FASII pathway. Its active site contains a critical cysteine-thiol residue, which is a plausible target for oxidation by H2O2. Streptococcus pneumoniae produces exceptionally

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