Pyruvate Oxidase, Microorganisms
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Pyruvate Oxidase, Microorganisms (PoxB) is a peripheral membrane enzyme, isolated from microorganisms. Pyruvate oxidase catalyzes the oxidative decarboxylation of pyruvate to acetyl phosphate, carbon dioxide and water. Pyruvate oxidase is an important enzyme in bacterial metabolism and is often used in biochemical research.
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- CAS No.: 9001-96-1
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Stockage:
Please store the product under the recommended conditions in the Certificate of Analysis.
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Activité biologique
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Chemical Information
- Pureté et documentation
- Références
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Help & FAQs
Activité biologique
Pyruvate Oxidase contributes to stationary-phase acetate accumulation in Escherichia coli K-12 strain JRG3456[2].
Pyruvate Oxidase (50 mM phosphate buffer; 10 min) has an initial activity optimum at 38°C, but is unstable at temperatures above 30°C, with activity declining after 10 min of incubation at temperatures exceeding 30°C[4].
Pyruvate Oxidase (0.1-150 mM) exhibits highest activity with pyruvate, reacts with methylglyoxal and acetaldehyde[4].
Pyruvate Oxidase (1-10 mM) is only slightly inhibited by 10 mM EDTA (11%) and 10 mM KCN (25%), and is unaffected by 10 mM NaN3, 1 mM iodoacetamide, or 1 mM p-hydroxymercuribenzoate[4].
Pyruvate oxidase requires TPP, FAD, and a divalent cation (e.g., Mn2+) to catalyze the four-step oxidative decarboxylation of pyruvate, producing acetylphosphate and H2O2 to support aerobic lactobacterial growth[5].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
1.2.3.3
≥35 U/mg protein
Chemical Information
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CAS No. 9001-96-1
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Appearance Solid
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Color Light yellow to yellow
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SMILES
[Pyruvate Oxidase, Microorganisms]
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Synonyms
PoxB
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Livraison
Room temperature in continental US; may vary elsewhere.
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Stockage
Please store the product under the recommended conditions in the Certificate of Analysis.
Pureté et documentation
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Fiche technique (265 KB)
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SDS (418 KB)
- English - EN (418 KB)
- Français - FR (418 KB)
- Deutsch - DE (418 KB)
- Norwegian - NO (418 KB)
- Español - ES (418 KB)
- Swedish - SV (418 KB)
- Italian - IT (418 KB)
- Portuguese - PT (418 KB)
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Instruction de manipulation (2659 KB)
Références
[1]. ROBERT B, et al. Pyruvate Oxidase. 2013.
[2]. Abdel-Hamid AM, et al. Pyruvate oxidase contributes to the aerobic growth efficiency of Escherichia coli. Microbiology (Reading). 2001;147(Pt 6):1483-1498. [Content Brief]
[3]. Spellerberg B, et al. Pyruvate oxidase, as a determinant of virulence in Streptococcus pneumoniae. Mol Microbiol. 1996;19(4):803-813. [Content Brief]
[4]. Sedewitz B, et al. Purification and biochemical characterization of pyruvate oxidase from Lactobacillus plantarum. J Bacteriol. 1984;160(1):273-278. [Content Brief]
[5]. Muller YA, et al. Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase. Science. 1993;259(5097):965-967. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
Pyruvate Oxidase, Microorganisms Related Classifications
Cat. No.: HY-P2891
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- Pyruvate Oxidase, Microorganisms
- 9001-96-1
- PoxB
- Biochemical Assay Reagents
- Lactobacillus plantarum L-809
- flavin adenine dinucleotide
- Escherichia coli K-12 strain JRG3445
- acetyl-CoA synthetase
- Pyruvate Oxidase
- Microorganisms
- thiamine pyrophosphate
- Escherichia coli strain 191-6
- Escherichia coli K-12 strain JRG3980
- Streptococcus pneumoniae
- Escherichia coli K-12 strain JRG3456
- Inhibitor
- inhibitor
- inhibit