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Information on EC 1.2.3.3 - pyruvate oxidase
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EC Tree
1.2.3.3 pyruvate oxidaseIUBMB 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 .
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Word Map
- 1.2.3.3
- streptococcus
- thiamin
- plantarum
- sanguinis
-
pneumococcus
-
lipid-activated
-
acetohydroxy
-
diphosphate-dependent
- phosphotransacetylase
- synthesis
- oralis
- analysis
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
pyruvate oxidase, pyrox, pox-2, acetyl phosphate-producing pyruvate oxidase, 
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetaldehyde + phosphate + O2 + H2O
? + H2O2
-
15% of the activity compared to pyruvate as substrate
-
?
alpha-ketobutyrate + phosphate + O2 + H2O
? + H2O2
-
very low activity
-
?
methylglyoxal + phosphate + O2 + H2O
? + H2O2
-
20% of the activity compared to pyruvate as substrate
-
?
pyruvate + arsenate + O2 + H2O
acetyl arsenate + CO2 + H2O2
-
can replace phosphate, 25% higher activity compared to phosphate as cosubstrate
-
?
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
-
-
-
-
?
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
-
-
-
?
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
-
-
-
?
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
-
-
-
?
pyruvate + phosphate + 2,6-dichlorophenolindophenol + H2O
acetyl phosphate + CO2 + reduced 2,6-dichlorophenolindophenol + H2O2
-
-
-
?
pyruvate + phosphate + 2,6-dichlorophenolindophenol + H2O
acetyl phosphate + CO2 + reduced 2,6-dichlorophenolindophenol + H2O2
-
36% of the activity compared to oxygen as electron acceptor
-
?
pyruvate + phosphate + 2,6-dichlorophenolindophenol + H2O
acetyl phosphate + CO2 + reduced 2,6-dichlorophenolindophenol + H2O2
-
artificial electron acceptor 2,6-dichlorophenolindophenol reacts with the carbanion of the enzyme-bound intermediate hydroxyethyl-thiamine diphosphate
-
?
pyruvate + phosphate + ferricyanide + H2O
acetyl phosphate + ferrocyanide + H2O2
-
-
-
-
?
pyruvate + phosphate + ferricyanide + H2O
acetyl phosphate + ferrocyanide + H2O2
-
65% of the activity compared to oxygen as electron acceptor
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
preferred substrate
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
enzyme is immobilized by a nafion matrix and covered by a poly carbamoyl sulfonate hydrogel on an electrode
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
r
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
reduction of enzyme by its substrate, pyruvate, in the absence of oxygen
-
ir
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
5step catalytic reaction
-
ir
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
involved in lactate metabolism
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
specifically favors phosphorylysis rather than hydrolysis, decarboxylation step not rate-limiting
-
ir
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
5 step catalytic reaction
-
ir
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
contribution to attachment to glycoconjugates of nasopharyngeal cell receptor, type II lung cells and human endothelial cells
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
no activity with L-lactare, phosphoenolpyruvate, very low activity with 2-oxobutyrate and oxaloacetate
-
-
?
additional information
?
-
-
predominant role in the control of acetate production under aerobic conditions
-
-
?
additional information
?
-
-
predominant role in the control of acetate production under aerobic conditions
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
-
-
-
-
?
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
-
-
-
?
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
-
-
-
?
2 pyruvate + phosphate + 2 O2 + H2O
acetate + acetyl phosphate + 2 CO2 + 2 H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
preferred substrate
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
involved in lactate metabolism
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
specifically favors phosphorylysis rather than hydrolysis, decarboxylation step not rate-limiting
-
ir
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
5 step catalytic reaction
-
ir
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
contribution to attachment to glycoconjugates of nasopharyngeal cell receptor, type II lung cells and human endothelial cells
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
additional information
?
-
-
no activity with L-lactare, phosphoenolpyruvate, very low activity with 2-oxobutyrate and oxaloacetate
-
-
?
additional information
?
-
-
predominant role in the control of acetate production under aerobic conditions
-
-
?
additional information
?
-
-
predominant role in the control of acetate production under aerobic conditions
-
-
?
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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