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Information on EC 1.2.3.3 - pyruvate oxidase
for references in articles please use BRENDA:EC1.2.3.3
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EC Tree 1 Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.3 With oxygen as acceptor
1.2.3.3 pyruvate oxidase
IUBMB Comments
A flavoprotein (FAD) requiring thiamine diphosphate. Two reducing equivalents are transferred from the resonant carbanion/enamine forms of 2-hydroxyethyl-thiamine-diphosphate to the adjacent flavin cofactor, yielding 2-acetyl-thiamine diphosphate (AcThDP) and reduced flavin. FADH2 is reoxidized by O2 to yield H2O2 and FAD and AcThDP is cleaved phosphorolytically to acetyl phosphate and thiamine diphosphate .
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 1.2.3.3
- streptococcus
- thiamin
- plantarum
- sanguinis
-
pneumococcus
-
lipid-activated
-
acetohydroxy
-
diphosphate-dependent
- phosphotransacetylase
- synthesis
- oralis
- analysis
- medicine
Synonyms
pyruvate oxidase, pyrox, pox-2, acetyl phosphate-producing pyruvate oxidase, more
top
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
POX
poxB
PyOD
pyruvate oxidase
pyruvic oxidase
-
-
-
-
SpxB
SpxB protein
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pyruvate + phosphate + O2 = acetyl phosphate + CO2 + H2O2
a flavoprotein, FAD
-
-
-
pyruvate + phosphate + O2 = acetyl phosphate + CO2 + H2O2
A flavoprotein, FAD, requiring thiamine diphosphate
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidative decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
pyruvate:oxygen 2-oxidoreductase (phosphorylating)
A flavoprotein (FAD) requiring thiamine diphosphate. Two reducing equivalents are transferred from the resonant carbanion/enamine forms of 2-hydroxyethyl-thiamine-diphosphate to the adjacent flavin cofactor, yielding 2-acetyl-thiamine diphosphate (AcThDP) and reduced flavin. FADH2 is reoxidized by O2 to yield H2O2 and FAD and AcThDP is cleaved phosphorolytically to acetyl phosphate and thiamine diphosphate [2].
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CAS REGISTRY NUMBER
COMMENTARY
9001-96-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetaldehyde + phosphate + O2 + H2O
? + H2O2
-
Substrates: 15% of the activity compared to pyruvate as substrate
Products: -
Products: -
?
alpha-ketobutyrate + phosphate + O2 + H2O
? + H2O2
-
Substrates: very low activity
Products: -
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?
methylglyoxal + phosphate + O2 + H2O
? + H2O2
-
Substrates: 20% of the activity compared to pyruvate as substrate
Products: -
Products: -
?
pyruvate + arsenate + O2 + H2O
acetyl arsenate + CO2 + H2O2
-
Substrates: can replace phosphate, 25% higher activity compared to phosphate as cosubstrate
Products: -
Products: -
?
pyruvate + phosphate + 2,6-dichlorophenolindophenol + H2O
acetyl phosphate + CO2 + reduced 2,6-dichlorophenolindophenol + H2O2
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
Substrates: -
Products: -
Products: -
?
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
Substrates: -
Products: -
Products: -
?
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
Substrates: -
Products: -
Products: -
?
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + 2,6-dichlorophenolindophenol + H2O
acetyl phosphate + CO2 + reduced 2,6-dichlorophenolindophenol + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + 2,6-dichlorophenolindophenol + H2O
acetyl phosphate + CO2 + reduced 2,6-dichlorophenolindophenol + H2O2
-
Substrates: 36% of the activity compared to oxygen as electron acceptor
Products: -
Products: -
?
pyruvate + phosphate + 2,6-dichlorophenolindophenol + H2O
acetyl phosphate + CO2 + reduced 2,6-dichlorophenolindophenol + H2O2
-
Substrates: artificial electron acceptor 2,6-dichlorophenolindophenol reacts with the carbanion of the enzyme-bound intermediate hydroxyethyl-thiamine diphosphate
Products: -
Products: -
?
pyruvate + phosphate + ferricyanide + H2O
acetyl phosphate + ferrocyanide + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + ferricyanide + H2O
acetyl phosphate + ferrocyanide + H2O2
-
Substrates: 65% of the activity compared to oxygen as electron acceptor
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: preferred substrate
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: enzyme is immobilized by a nafion matrix and covered by a poly carbamoyl sulfonate hydrogel on an electrode
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
r
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
r
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: reduction of enzyme by its substrate, pyruvate, in the absence of oxygen
Products: -
Products: -
ir
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: 5step catalytic reaction
Products: -
Products: -
ir
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: involved in lactate metabolism
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: specifically favors phosphorylysis rather than hydrolysis, decarboxylation step not rate-limiting
Products: -
Products: -
ir
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: 5 step catalytic reaction
Products: -
Products: -
ir
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: contribution to attachment to glycoconjugates of nasopharyngeal cell receptor, type II lung cells and human endothelial cells
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: cell membrane-associated electron transport system, which includes both ubiquinone-6 and cytochrome b, is the natural electron acceptor for the reduced enzyme and oxygen is the terminal electron acceptor of this system
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with L-lactare, phosphoenolpyruvate, very low activity with 2-oxobutyrate and oxaloacetate
Products: -
Products: -
?
additional information
?
-
-
Substrates: predominant role in the control of acetate production under aerobic conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: predominant role in the control of acetate production under aerobic conditions
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
Substrates: -
Products: -
Products: -
?
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
Substrates: -
Products: -
Products: -
?
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
Substrates: -
Products: -
Products: -
?
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: preferred substrate
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
r
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: involved in lactate metabolism
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: specifically favors phosphorylysis rather than hydrolysis, decarboxylation step not rate-limiting
Products: -
Products: -
ir
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: 5 step catalytic reaction
Products: -
Products: -
ir
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: contribution to attachment to glycoconjugates of nasopharyngeal cell receptor, type II lung cells and human endothelial cells
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with L-lactare, phosphoenolpyruvate, very low activity with 2-oxobutyrate and oxaloacetate
Products: -
Products: -
?
additional information
?
-
-
Substrates: predominant role in the control of acetate production under aerobic conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: predominant role in the control of acetate production under aerobic conditions
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
binding of FAD in a monophasic, pseudo first order process
FAD
-
important in stabilization of enzyme, irreversible removal during pressure-induced dissociation of enzyme
thiamine diphosphate
-
indirect activation by FAD that is mediated by the protein moiety
thiamine diphosphate
-
PyOd binds one thiamine diphosphate per subunit in the presence of Mg2+, optimum concentration 1 mM
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
-
PyOd binds one thiamine diphosphate per subunit in the presence of Mg2+, optimum concentration 10 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphatidylethanolamine
-
enzyme is specifically activated by phosphotidylethanolamine (16:0-18:1). The C-terminal sequence is important for activation
thiamine
-
activates the enzyme. Can be used as an activator on the biosensor responses
additional information
-
pyrodoxin, nicotinic acid, and riboflavin have no activating effects
-
additional information
-
pyrodoxin, riboflavin and nicotinic acid do not play an activator role
-
additional information
yeast extract, ammonium sulfate and composite phosphate are significant factors on PyOD production. Glycerol and peptone in the medium do not affect the PyOD production significantly
-
additional information
-
not activating: phosphotidylcholine or phosphotidylglycerol
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hypersensitivity
Molecular and functional characterization of Salmonella enterica serovar typhimurium poxA gene: effect on attenuation of virulence and protection.
Infections
Streptococcus oralis Induces Lysosomal Impairment of Macrophages via Bacterial Hydrogen Peroxide.
Periodontitis
Interspecies Inhibition of Porphyromonas gingivalis by Yogurt-Derived Lactobacillus delbrueckii Requires Active Pyruvate Oxidase.
Plague
[The effect of plague microbe toxin on the activity of pyruvate oxidase and lactate dehydrogenase in plague-susceptible animals]
pyruvate oxidase deficiency
Pleiotropic effects of poxA regulatory mutations of Escherichia coli and Salmonella typhimurium, mutations conferring sulfometuron methyl and alpha-ketobutyrate hypersensitivity.
Starvation
Diversion of the metabolic flux from pyruvate dehydrogenase to pyruvate oxidase decreases oxidative stress during glucose metabolism in nongrowing Escherichia coli cells incubated under aerobic, phosphate starvation conditions.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
2,6-dichlorophenolindophenol
-
artificial electron acceptor
1.25
phosphate
-
presence of phosphatidylethanolamine, pH 5.6, 25°C
4.5
phosphate
-
electron acceptor: 2,6-dichlorophenolindophenol
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.9
pyruvate
-
electron acceptor: 2,6-dichlorophenolindophenol
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
a temperature of 25°C gives the highest sensitivity, the enzyme loses activity above 25°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
analysis of a pyruvate oxidase deficient mutant, that fails to attach to human endothelial and type II lung cells and to nasopharyngeal cell receptor
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
enhanced activity at aerobic growth conditions, reduced activity in the presence of glucose
brenda
-
mRNA expression under aerobic conditions and glucose exhaustion
brenda
-
mRNA expression under aerobic conditions and glucose exhaustion
-
brenda
additional information
-
enzyme activity detectable even in the early exponential phase of growth and attains the highest levels in the early stationary phase
brenda
additional information
-
enzyme activity detectable even in the early exponential phase of growth and attains the highest levels in the early stationary phase
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
a truncated pyruvate oxidase mutant containing an in-frame fusion of TnphoA to the pyruvate oxidase gene is defective in H2O2 production
malfunction
-
in an enzyme-deficient mutant of Lactobacillus johnsonii NCC 533, oxygen is not able to overcome acetate dependency nor does it relieve the CO2 dependency. The mutant has a lower growth rate, both aerobically and aerobically
malfunction
-
inactivation of pox causes a dramatic reduction in H2O2 production from lactate
malfunction
mutants lacking the enzyme gene are defective in pneumolysin release
malfunction
-
in an enzyme-deficient mutant of Lactobacillus johnsonii NCC 533, oxygen is not able to overcome acetate dependency nor does it relieve the CO2 dependency. The mutant has a lower growth rate, both aerobically and aerobically
-
metabolism
-
C1- and C2-compound production is largely depend on pyruvate oxidase activity
metabolism
-
C1- and C2-compound production is largely depend on pyruvate oxidase activity
-
physiological function
-
pyruvate oxidase is involved in hydrogen peroxide production
physiological function
-
Pox performs a synergistic action with lactate oxidases in converting lactate into H2O2
physiological function
-
pyruvate oxidase expressed in Chlamydomonas reinhardtii increases oxygen consumption and has potential for improving photosynthetic hydrogen production in Chlamydomonas reinhardtii
physiological function
enzyme expression of enhances pneumolysin-dependent cell death
physiological function
enzyme-mediated H2O2 induces programmed cell death in Streptococcus sanguinis
physiological function
-
the enzyme is required for capsule formation
physiological function
-
Lactobacillus delbrueckii displays strain-specific inhibition of Pseudomonas gingivalis growth in vitro. Purified, catalytically active, recombinant pyruvate oxidase is sufficient to inhibit P. gingivalis growth in vitro without the addition of cofactors
physiological function
-
pyruvate oxidase is involved in hydrogen peroxide production
-
physiological function
-
enzyme-mediated H2O2 induces programmed cell death in Streptococcus sanguinis
-
Show AA Sequence and Transmembrane Helices (1477 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
homotetramer
pentamer
tetramer
tetramer
-
composed of four identical subunits, each subunit binds one FAD and one thiamine diphosphate-Mg2+, analysis from X-ray diffraction data
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by the hanging-drop vapour-diffusion method. POX complexed with FAD, with FAD and thiamine diphosphate, and with FAD and the 2-acetyl-thiamine diphosphate intermediate at 1.6, 1.8 and 1.9 A resolution, respectively. Each subunit of the homotetrameric POX enzyme consists of three domains. FAD is bound within one subunit in the elongated conformation and with the flavin moiety being planar in the oxidized form, while thiamine diphosphate is bound in a conserved V-conformation at the subunit-subunit interface. The structures reveal flexible regions in the active-site tunnel which may undergo conformational changes to allow the entrance of the substrates and the exit of the reaction products. Lys478, the side chain of which may be bent or extended depending on the stage of catalysis
the full-length form and a proteolytically activated C-terminal truncation variant which lacks the last 23 amino acids, by the hanging-drop vapour-diffusion method using either protamine sulfate (fulllength POX) or 2-methyl-2,4-pentanediol (DELTA23 POX) as precipitants. To 2.9 A resolution. Fulllength POX crystallizes in the tetragonal space group P43212 with two monomers per asymmetric unit, the crystals of DELTA23 POX belong to the orthorhombic space group P212121 and contain 12 monomers per asymmetric unit
-
in complex with the thiamin diphosphate carbanion-enamine and two-electron reduced FAD, hanging drop vapor diffusion method
-
wild-type at 2.5 A resolution, triple mutant at 2.1 A resolution, hanging drop vapour diffusion technique
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P178S/S188N/A458V
-
stabilizes quaternary rather than tertiary structure
V265A
additional information
V265A
similar catalytic properties compared to the wild-type protein, but decreased affinity for FAD
additional information
-
poxB mutant, absence of pyruvate oxidase activity, which reduces glucose uptake rate, biomass yield, acetate production and cell growth rate, and increases O2 consumption and CO2 evolution. Glucokinase activity increases, whereas the flux through glycolysis is reduced due to down-regulation of other glycolytic enzymes such as 6-phosphofructosekinase and fructose bisphosphate aldolase. TCA cycle enzymes such as citrate synthase and malate dehydrogenase are repressed in the poxB mutant when cells are cultivated in LB medium. Activation of glucose-6-phosphate dehydrogenase and acetyl-CoA synthetase
additional information
-
enzyme deletion mutant, 20-25% decrease in acetate production during gr0wth on glucose as sole carbon source, 60-80% decrease in acetate production during growth on maltose, constitutive overproduction of enzyme, acetate becomes the only fermentation end product
additional information
-
no pyruvate oxidase activity detectable in a PoxB/PoxF double mutant
additional information
-
enzyme deletion mutant, 20-25% decrease in acetate production during gr0wth on glucose as sole carbon source, 60-80% decrease in acetate production during growth on maltose, constitutive overproduction of enzyme, acetate becomes the only fermentation end product
-
additional information
-
a cidC pyruvate oxidase mutant exhibited decreased pyruvate oxidase activity and shows reduced cell lysis in stationary phase
additional information
-
a cidC pyruvate oxidase mutant exhibited decreased pyruvate oxidase activity and shows reduced cell lysis in stationary phase
-
additional information
-
SpxB-deficient mutant, shows drastically diminished H2O2 production
additional information
-
SpxB-deficient mutant, shows drastically diminished H2O2 production
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6 - 5.8
-
highest stability at 4°C and highest remaining activity of 67%
390437
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
substrate pyruvate can significantly stabilize the enzyme against pressure
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ion exchange column chromatography, immobilization on aminoalkylated controlled pore glass by crosslinking with glutaraldehyde
-
to homogeneity, ultracentrifugation and chromatography techniques
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
into the expression vector pSML104 to generate a N-terminus His-tagged fusion expression plasmid pSMLPyODp and expressed in Escherichia coli DH5alpha
overexpressed in Escherichia coli strain ZK126 carrying the plasmid pYYC102 which encodes the poxB gene
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of spxB is decreased in the acetate kinase and SpxR (a regulator of spxB) mutants
the expression of spxB is significantly increased in the thiamine pyrophosphokinase mutant
the expression of spxB is decreased in the acetate kinase and SpxR (a regulator of spxB) mutants
-
the expression of spxB is decreased in the acetate kinase and SpxR (a regulator of spxB) mutants
-
-
the expression of spxB is significantly increased in the thiamine pyrophosphokinase mutant
-
the expression of spxB is significantly increased in the thiamine pyrophosphokinase mutant
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
-
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
-
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
-
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
synthesis
-
constitutive overproduction of enzyme, acetate becomes the only fermentation end product
synthesis
-
effect of acettae pathway mutations on production of pyruvate, pH value of 7.0 and 32°C favor greatest pyruvate generation
synthesis
-
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
-
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
-
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
-
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
-
constitutive overproduction of enzyme, acetate becomes the only fermentation end product
-
synthesis
-
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
-
additional information
-
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
-
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
-
pyruvate oxidase is not only a stationary-phase enzyme. Removal of the poxB gene affects the central metabolism at the enzyme level
additional information
-
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
-
optimization of the medium for PyOD production by recombinant Escherichia coli using shake flask method
-
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ORGANISM (UNIPROT)
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SOURCE
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Structure
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brenda
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50
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Escherichia coli
brenda
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186
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72
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Lactiplantibacillus plantarum
brenda
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A screen-printed biosensor using pyruvate oxidase for rapid determination of phosphate in synthetic wastewater
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66
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Aerococcus viridans
brenda
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Biochemistry
44
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2005
Lactiplantibacillus plantarum
brenda
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44
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Lactiplantibacillus plantarum (P37063), Lactiplantibacillus plantarum
brenda
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21
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Escherichia coli, Escherichia coli MG1655
brenda
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187
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Lactiplantibacillus plantarum, Lactococcus lactis, Streptococcus pyogenes
brenda
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8
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Escherichia coli, Escherichia coli JM101, Escherichia coli PB11, Escherichia coli PB12
brenda
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56
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Staphylococcus aureus, Staphylococcus aureus UAMS-1
brenda
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63
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Aerococcus viridans (A9X9K8), Aerococcus viridans
brenda
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Escherichia coli
brenda
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-
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brenda
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brenda
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-
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brenda
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Streptococcus sanguinis, Streptococcus sanguinis SK36
brenda
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Probing oral microbial functionality - expression of spxB in plaque samples
PLoS ONE
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brenda
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Pyruvate oxidase as a critical link between metabolism and capsule biosynthesis in Streptococcus pneumoniae
PLoS Pathog.
12
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2016
Streptococcus pneumoniae
brenda
Cornacchione, L.P.; Klein, B.A.; Duncan, M.J.; Hu, L.T.
Interspecies inhibition of Porphyromonas gingivalis by yogurt-derived Lactobacillus delbrueckii requires active pyruvate oxidase
Appl. Environ. Microbiol.
85
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2019
Lactobacillus delbrueckii
brenda
Cornacchione, L.P.; Hu, L.T.
Hydrogen peroxide-producing pyruvate oxidase from Lactobacillus delbrueckii is catalytically activated by phosphotidylethanolamine
BMC Microbiol.
20
128
2020
Lactobacillus delbrueckii, Lactobacillus delbrueckii STYM1
brenda
Malik, M.; Chaudhary, R.; Pundir, C.S.
An improved enzyme nanoparticles based amperometric pyruvate biosensor for detection of pyruvate in serum
Enzyme Microb. Technol.
123
30-38
2019
Aerococcus sp.
brenda
Zhang, J.; Lu, J.; Su, E.
Soluble recombinant pyruvate oxidase production in Escherichia coli can be enhanced and inclusion bodies minimized by avoiding pH stress
J. Chem. Technol. Biotechnol.
94
2661-2670
2019
Aerococcus viridans
-
brenda
Lu, J.; Zhao, Y.; Zhang, J.
High-level expression of Aerococcus viridans pyruvate oxidase in Escherichia coli by optimization of vectors and induction conditions
Lett. Appl. Microbiol.
67
262-269
2018
Aerococcus viridans
brenda
Liang, J.; Zhao, J.; Wang, Z.; Wang, Y.
Temperature gradient-based high-cell density fed-batch fermentation for the production of pyruvate oxidase by recombinant E. coli
Prep. Biochem. Biotechnol.
48
188-193
2018
Aerococcus viridans, Aerococcus viridans ATCC 10400
brenda
Malik, M.; Chaudhary, R.; Pundir, C.
An amperometric pyruvate biosensor based on pyruvate oxidase nanoparticles immobilized onto pencil graphite electrode
Process Biochem.
93
12-20
2020
Aerococcus sp.
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brenda
Lu, J.; Zhang, J.
Extracellular expression of Aerococcus viridans pyruvate oxidase in recombinant Escherichia coli through SecB co-expression
RSC Adv.
9
26291-26301
2019
Aerococcus viridans
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brenda
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Release 2023.1 (January 2023)
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