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P4105

Sigma-Aldrich

Pyruvate Oxidase from Aerococcus sp.

lyophilized powder, ≥35 units/mg protein (biuret)

Synonym(s):

Pyruvate: oxygen oxidoreductase (phosphorylating)

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About This Item

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

biological source

bacterial (Aerococcus spp.)

Quality Level

form

lyophilized powder

specific activity

≥35 units/mg protein (biuret)

storage temp.

−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 from Aerococcus sp. has been used in the amplex Red-based fluorescence assay for pyruvate. It is suitable for use in the preparation of biosensor for determination of thiamine (vitamin B1), and as a component in the constant part of the multi-enzyme biocatalytic cascade for the determination of biomarkers for traumatic brain injury (TBI) and soft tissue injury (STI).

Biochem/physiol Actions

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 carbon dioxide. Pyruvate oxidase requires flavin adenine dinucleotide (FAD), thiamine pyrophosphate (TPP) and magnesium as cofactors for its catalytic activity. Thiamine activates pyruvate oxidase activity.

Unit Definition

One unit will produce 1.0 μmole of H2O2 per min during the conversion of pyruvate and phosphate to acetylphosphate and CO2 at pH 6.7 at 37 °C.

Physical form

Lyophilized powder containing buffer salt and sugar

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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B Sedewitz et al.
Journal of bacteriology, 160(1), 273-278 (1984-10-01)
Pyruvate oxidase (EC 1.2.3.3) was isolated and characterized from Lactobacillus plantarum. The enzyme catalyzes the oxidative decarboxylation of pyruvate in the presence of phosphate and oxygen, yielding acetyl phosphate, carbon dioxide, and hydrogen peroxide. This pyruvate oxidase is a flavoprotein
Hiroaki Taniai et al.
Journal of bacteriology, 190(10), 3572-3579 (2008-03-18)
Streptococcus pneumoniae was shown to possess lactate oxidase in addition to well-documented pyruvate oxidase. The activities of both H(2)O(2)-forming oxidases in wild-type cultures were detectable even in the early exponential phase of growth and attained the highest levels in the
Alice Dawson et al.
Journal of molecular biology, 401(2), 253-264 (2010-07-06)
The first committed step in the classical biosynthetic route to menaquinone (vitamin K(2)) is a Stetter-like conjugate addition of alpha-ketoglutarate with isochorismate. This reaction is catalyzed by the thiamine diphosphate and metal-ion-dependent 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD). The medium-resolution (2.35 A) crystal
Amit Priyadarshi et al.
Biochemical and biophysical research communications, 388(4), 748-751 (2009-08-26)
Here we describe in detail the crystal structures of the Vitamin K(2) synthesis protein MenD, from Escherichia coli, in complex with thiamine diphosphate (ThDP) and oxoglutarate, and the effects of cofactor and substrate on its structural stability. This is the
Yihui Zhu et al.
Journal of industrial microbiology & biotechnology, 37(3), 307-312 (2009-12-17)
We report the conversion of glycerol to pyruvate by E. coli ALS929 containing knockouts in the genes encoding for phosphoenolpyruvate synthase, lactate dehydrogenase, pyruvate formate lyase, the pyruvate dehydrogenase complex, and pyruvate oxidase. As a result of these knockouts, ALS929

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