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Information on EC 1.2.3.3 - pyruvate oxidase and Organism(s) Lactiplantibacillus plantarum and UniProt Accession P37063
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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 taxonomic range for the selected organisms is: Lactiplantibacillus plantarum
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
pyruvate oxidase, pyrox, pox-2, acetyl phosphate-producing pyruvate oxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
pyruvic oxidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
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].
CAS REGISTRY NUMBER
COMMENTARY
9001-96-1
-
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
pyruvate + phosphate + O2 + H2O
acetyl phosphate + CO2 + H2O2
-
-
-
?
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
pyruvate + phosphate + ferricyanide + H2O
acetyl phosphate + ferrocyanide + H2O2
-
65% of the activity compared to oxygen as electron acceptor
-
?
additional information
?
-
-
predominant role in the control of acetate production under aerobic conditions
-
-
?
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 + 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 + 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
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
pyruvate + phosphate + O2
acetyl phosphate + CO2 + H2O2
-
-
-
-
?
additional information
?
-
-
predominant role in the control of acetate production under aerobic conditions
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
binding of FAD in a monophasic, pseudo first order process
thiamine diphosphate
-
indirect activation by FAD that is mediated by the protein moiety
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
2,6-dichlorophenolindophenol
-
artificial electron acceptor
4.5
phosphate
-
electron acceptor: 2,6-dichlorophenolindophenol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.9
pyruvate
-
electron acceptor: 2,6-dichlorophenolindophenol
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enhanced activity at aerobic growth conditions, reduced activity in the presence of glucose
-
mRNA expression under aerobic conditions and glucose exhaustion
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
-
composed of four identical subunits, each subunit binds one FAD and one thiamine diphosphate-Mg2+, analysis from X-ray diffraction data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V265A
similar catalytic properties compared to the wild-type protein, but decreased affinity for FAD
P178S/S188N/A458V
-
stabilizes quaternary rather than tertiary structure
additional information
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6 - 5.8
-
highest stability at 4°C and highest remaining activity of 67%
390437
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity, ultracentrifugation and chromatography techniques
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
constitutive overproduction of enzyme, acetate becomes the only fermentation end product
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Muller, Y.A.; Lindqvist, Y.; Furey, W.; Schulz, G.E.; Jordan, F.; Schneider, G.
A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase
Structure
1
95-103
1993
Lactiplantibacillus plantarum
Tittmann, K.; Golbik, R.; Ghisla, S.; Hubner, G.
Mechanism of elementary catalytic steps of pyruvate oxidase from Lactobacillus plantarum
Biochemistry
39
10747-10754
2000
Lactiplantibacillus plantarum
Tittmann, K.; Proske, D.; Spinka, M.; Ghisla, S.; Rudolph, R.; Hubner, G.; Kern, G.
Activation of thiamin diphosphate and FAD in the phosphate-dependent pyruvate oxidase from Lactobacillus plantarum
J. Biol. Chem.
273
12929-12934
1998
Lactiplantibacillus plantarum
Muller, Y.A.; Schumacher, G.; Rudolph, R.; Schulz, G.E.
The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum
J. Mol. Biol.
237
315-335
1994
Lactiplantibacillus plantarum
Sedewitz, B.; Schleifer, K.H.; Gtz, F.
Physiological role of pyruvate oxidase on the aerobic metabolism of Lactobacillus plantarum
J. Bacteriol.
160
462-465
1984
Lactiplantibacillus plantarum
Sedewitz, B.; Schleifer, K.H.; Gtz, F.
Purification and biochemical characterization of pyruvate oxidase from Lactobacillus plantarum
J. Bacteriol.
160
273-278
1984
Lactiplantibacillus plantarum
Wille, G.; Ritter, M.; Friedemann, R.; Mantele, W.; Hubner, G.
Redox-triggered FTIR difference spectra of FAD in aqueous solution and bound to flavoproteins
Biochemistry
42
14814-14821
2003
Lactiplantibacillus plantarum
Lorquet, F.; Goffin, P.; Muscariello, L.; Baudry, J.B.; Ladero, V.; Sacco, M.; Kleerebezem, M.; Hols, P.
Characterization and functional analysis of the poxB gene, which encodes pyruvate oxidase in Lactobacillus plantarum
J. Bacteriol.
186
3749-3759
2004
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum Lp80
Goffin, P.; Muscariello, L.; Lorquet, F.; Stukkens, A.; Prozzi, D.; Sacco, M.; Kleerebezem, M.; Hols, P.
Involvement of pyruvate oxidase activity and acetate production in the survival of Lactobacillus plantarum during the stationary phase of aerobic growth
Appl. Environ. Microbiol.
72
7933-7940
2006
Lactiplantibacillus plantarum
Tittmann, K.; Wille, G.; Golbik, R.; Weidner, A.; Ghisla, S.; Huebner, G.
Radical phosphate transfer mechanism for the thiamin diphosphate- and FAD-dependent pyruvate oxidase from Lactobacillus plantarum. Kinetic coupling of intercofactor electron transfer with phosphate transfer to acetyl-thiamin diphosphate via a transient FA
Biochemistry
44
13291-13303
2005
Lactiplantibacillus plantarum
Wille, G.; Ritter, M.; Weiss, M.S.; Koenig, S.; Maentele, W.; Huebner, G.
The role of Val-265 for flavin adenine dinucleotide (FAD) binding in pyruvate oxidase: FTIR, kinetic, and crystallographic studies on the enzyme variant V265A
Biochemistry
44
5086-5094
2005
Lactiplantibacillus plantarum (P37063), Lactiplantibacillus plantarum
Schreiner, M.E.; Eikmanns, B.J.
Pyruvate:quinone oxidoreductase from Corynebacterium glutamicum: purification and biochemical characterization
J. Bacteriol.
187
862-871
2005
Lactiplantibacillus plantarum, Lactococcus lactis, Streptococcus pyogenes
Tittmann, K.
Reaction mechanisms of thiamin diphosphate enzymes: redox reactions
FEBS J.
276
2454-2468
2009
Lactiplantibacillus plantarum (P37063)
Schroeder-Tittmann, K.; Meyer, D.; Arens, J.; Wechsler, C.; Tietzel, M.; Golbik, R.; Tittmann, K.
Alternating sites reactivity is a common feature of thiamin diphosphate-dependent enzymes as evidenced by isothermal titration calorimetry studies of substrate binding
Biochemistry
52
2505-2507
2013
Lactiplantibacillus plantarum
Meyer, D.; Neumann, P.; Koers, E.; Sjuts, H.; Luedtke, S.; Sheldrick, G.M.; Ficner, R.; Tittmann, K.
Unexpected tautomeric equilibria of the carbanion-enamine intermediate in pyruvate oxidase highlight unrecognized chemical versatility of thiamin
Proc. Natl. Acad. Sci. USA
109
10867-10872
2012
Lactiplantibacillus plantarum
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