1.2.3.3: pyruvate oxidase
This is an abbreviated version!
For detailed information about pyruvate oxidase, go to the full flat file.
Word Map on EC 1.2.3.3
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1.2.3.3
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streptococcus
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thiamin
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plantarum
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sanguinis
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pneumococcus
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lipid-activated
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acetohydroxy
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diphosphate-dependent
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phosphotransacetylase
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synthesis
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oralis
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analysis
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medicine
- 1.2.3.3
- streptococcus
- thiamin
- plantarum
- sanguinis
-
pneumococcus
-
lipid-activated
-
acetohydroxy
-
diphosphate-dependent
- phosphotransacetylase
- synthesis
- oralis
- analysis
- medicine
Reaction
Synonyms
acetyl phosphate-producing pyruvate oxidase, phosphate-dependent pyruvate oxidase, POD, POX, POX-2, poxB, PoxF, PyOD, PyrOx, pyruvate oxidase, pyruvate:oxygen-2-oxidoreductase (phosphorylating), pyruvic oxidase, SpxB, SpxB protein
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Application
Application on EC 1.2.3.3 - pyruvate oxidase
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analysis
medicine
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Lactobacillus delbrueckii commercia l yogurt strains STYM1 and GVKM1 inhibit Pseudomonas gingivalis growth in vitro, while raw milk isolates SYB7 and SYB13 have little impaxct. Purified, catalytically active, recombinant pyruvate oxidase is sufficient to inhibit P. gingivalis growth in vitro without the addition of cofactors
synthesis
additional information
analysis
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construction of an amperometric biosensor using nanoparticles of pyruvate oxidase, immobilized covalently onto pencil graphite electrode. The biosensor shows ideal working within 5 s under defined conditions of pH 6.0 and 30°C at an applied voltage of -0.1 V. Under standard assay conditions, a linear response is obtained between pyruvate concentration from 0.001 to 6000 microM and current. Lower detection limit is 0.58 microM, the biosensor can be used for over 210 days for the measurement of pyruvate in blood sera
analysis
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use of nanoparticles of commercially available pyruvate oxidase covalently immobilized onto gold electrode as amperometric pyruvate biosensor for detection of pyruvate in serum. The biosensor shows optimum response within 7.5 s, at a potential of 0.28 V, pH 5.5 and 35°C and a lower detection limit of 0.67 microM. The analytical recovery of added pyruvate in sera is 99.0% and 99.5% within and between batches. The biosensor can be utilized for detection of total pyruvate level in sera of apparently healthy individuals and patients suffering from cardiogenic stress
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constitutive overproduction of enzyme, acetate becomes the only fermentation end product
synthesis
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effect of acettae pathway mutations on production of pyruvate, pH value of 7.0 and 32°C favor greatest pyruvate generation
synthesis
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high-level expression of enzyme is achieved in recombinant Escherichia coli by optimizing the expression system and induction conditions. Optimization leads to the highest pyruvate oxidase yield (4106.9 U/l) under conditions of 25°C, 0.5 mM IPTG, 0.5 OD600, after 24 h of induction
synthesis
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pH stress during recombinant Escherichia coli cultivation leads to great losses of enzyme. Residual POD activity (3.1%) is increased to 43.3, 88.0 and 61.5% by maintaining the pH at 5.0, 6.0 and 7.0 respectively during the induction phase, which decreases inclusion body formation and increases production of soluble POD. Glycerol addition increases the cell density and volumetric POD activity to 21243.3 U/l at pH 6.0 after 64 h induction
synthesis
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POD expression in Escherichia coli is achieved by coexpression of chaperone SecB under three promoters (T7, lac, bla). The weakest promoter, bla, when compared with T7 and lac promoters, provides the optimum extracellular POD activity among these three. After optimization of cultivation conditions, the extracellular POD yield increases to 795.7 U/l. By using glycine to disrupt recombinant Escherichia coli cell wall and Cu2+ ions as POD stabilizer, the final extracellular POD yield reaches 2926.3 U/l
synthesis
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production of enzyme in recombinant Escherichia coli constitutively expressing paruvate oxidase. A high-cell density fed-batch cultivation with gradient temperature decrease strategy is achieved, under which the biomass (OD600) of recombinant E. coli can reach to 71 and the highest PyOD activity in broth can reach to 3307 U/l in 26 h fermentation
synthesis
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constitutive overproduction of enzyme, acetate becomes the only fermentation end product
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synthesis
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production of enzyme in recombinant Escherichia coli constitutively expressing paruvate oxidase. A high-cell density fed-batch cultivation with gradient temperature decrease strategy is achieved, under which the biomass (OD600) of recombinant E. coli can reach to 71 and the highest PyOD activity in broth can reach to 3307 U/l in 26 h fermentation
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aerobiosis makes the concerted action of lactate oxidase and pyruvate oxidase possible, enabling cells of Streptococcus pneumoniae to gain more ATP from glucose than under anaerobiosis
additional information
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development of a biosensor based on POX enzyme for the investigation of the effect of thiamine (vitamin B1) molecule on the activity of the enzyme
additional information
optimization of the medium for PyOD production by recombinant Escherichia coli using shake flask method
additional information
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pyruvate oxidase is not only a stationary-phase enzyme. Removal of the poxB gene affects the central metabolism at the enzyme level
additional information
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aerobiosis makes the concerted action of lactate oxidase and pyruvate oxidase possible, enabling cells of Streptococcus pneumoniae to gain more ATP from glucose than under anaerobiosis
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additional information
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optimization of the medium for PyOD production by recombinant Escherichia coli using shake flask method
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