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Merck

P4591

Pyruvate Oxidase from microorganisms

lyophilized powder, ≥1.5 U/mg

Sinónimos:

Pyruvate:oxygen oxidoreductase (phosphorylating)

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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-644-5
MDL number:
Número CE:
Specific activity:
≥1.5 U/mg

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form

lyophilized powder

specific activity

≥1.5 U/mg

mol wt

~260 kDa

storage temp.

−20°C

Quality Level

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Este artículo
P4105C8868A6941
specific activity

≥1.5 U/mg

specific activity

≥35 units/mg protein (biuret)

specific activity

≥50 units/mg protein

specific activity

5-15 units/mg protein

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

mol wt

~260 kDa

mol wt

-

mol wt

64 kDa

mol wt

octomer 600 kDa by sedimentation equilibrium

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

General description

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)

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.[1] It has also been used in developing near real-time continuous detection system for pyruvate.[2]

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 carbondioxide.[1] 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.[3]

Physical form

Lyophilized powder containing FAD and sugar as stabilizer

Other Notes

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.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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)
Masoom Yasinzai
The International journal of biological markers, 24(2), 107-111 (2009-07-28)
Cancer patients are found to have elevated serum levels of lipid-associated sialic acid (LASA). LASA measurement provides a valuable test for the diagnosis of human cancer. The currently used measurement methods are tedious and nonselective. Here we report a method
A novel biosensor based on activation effect of thiamine on the activity of pyruvate oxidase
Akyilmaz E and Yorganci E
Biosensors And Bioelectronics, 23(12), 1874-1877 (2008)
Piotr Neumann et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(45), 17390-17395 (2008-11-08)
The thiamin- and flavin-dependent peripheral membrane enzyme pyruvate oxidase from E. coli catalyzes the oxidative decarboxylation of the central metabolite pyruvate to CO(2) and acetate. Concomitant reduction of the enzyme-bound flavin triggers membrane binding of the C terminus and shuttling
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

Protocolos

Protocol for Assay Procedure for Pyruvate Oxidase Bacterial

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