P4105
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
Recommended Products
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
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)
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B Sedewitz et al.
Journal of bacteriology, 160(1), 462-465 (1984-10-01)
Under aerobic growth conditions Lactobacillus plantarum produced acetic acid in addition to lactic acid. It was found that lactic acid was predominantly produced at first, and then when the carbohydrate was nearly exhausted, lactic acid was metabolized further to acetic
Multi-enzyme logic network architectures for assessing injuries: digital processing of biomarkers
Halamek J, et al.
Molecular Biosystems, 6(12), 2554-2560 (2010)
Activation of pyruvate oxidase by monomeric and micellar amphiphiles.
R Blake et al.
The Journal of biological chemistry, 253(6), 1963-1971 (1978-03-25)
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
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
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