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pyruvate + 9,10-anthraquinone-2,6-disulfonic acid + H2O
acetate + CO2 + ?
pyruvate + a quinone
acetate + CO2 + a quinol
-
-
-
-
?
pyruvate + dimethylmenoquinone + H2O
acetate + CO2 + dimethylmenoquinol
-
-
-
-
?
pyruvate + ferricyanide
acetate + CO2 + ferrocyanide
-
activity assayed photometrically by monitoring the reduction of 2,6-dichloroindophenol
-
-
?
pyruvate + ferricyanide + H2O
acetate + CO2 + ferrocyanide
pyruvate + ferricytochrome b1 + H2O
acetate + CO2 + ferrocytochrome b1
pyruvate + menaquinone + H2O
acetate + CO2 + menaquinol
-
-
-
-
?
pyruvate + oxidized 2,6-dichloroindophenol
acetate + CO2 + reduced 2,6-dichloroindophenol
-
activity assayed photometrically by monitoring the reduction of 2,6-dichloroindophenol, pH 6.0, 40°C
-
-
?
pyruvate + oxidized 2,6-dichloroindophenol + H2O
acetate + CO2 + reduced 2,6-dichloroindophenol
-
-
-
-
?
pyruvate + quinone + H2O
acetate + CO2 + quinol
-
-
-
-
?
pyruvate + ubiquinol-6 + H2O
acetate + CO2 + ubiquinol-6
-
the natural electron acceptor for the reduced enzyme is a cell-membrane-associated electron transport system including both ubiquinone-6 and cytochrome b1, with oxygen being the terminal electron acceptor
-
-
?
pyruvate + ubiquinone + H2O
acetate + CO2 + ubiquinol
pyruvate + ubiquinone-30 + H2O
acetate + CO2 + ubiquinol-30
-
ubiquinone-30 is rapidly reduced by pyruvate oxidase only in the presence of palmitic acid
-
-
?
pyruvate + ubiquinone-6 + H2O
acetate + CO2 + ubiquinol-6
-
-
-
-
?
pyruvate + ubiquinone-8
acetate + CO2 + ubiquinol-8
pyruvate + ubiquinone-8 + H2O
acetate + CO2 + ubiquinol-8
pyruvate + 9,10-anthraquinone-2,6-disulfonic acid + H2O
acetate + CO2 + ?
-
-
-
-
?
pyruvate + 9,10-anthraquinone-2,6-disulfonic acid + H2O
acetate + CO2 + ?
-
-
-
-
?
pyruvate + ferricyanide + H2O
acetate + CO2 + ferrocyanide
-
-
-
-
?
pyruvate + ferricyanide + H2O
acetate + CO2 + ferrocyanide
-
-
-
?
pyruvate + ferricyanide + H2O
acetate + CO2 + ferrocyanide
-
addition of 1% lauric acid
-
-
?
pyruvate + ferricyanide + H2O
acetate + CO2 + ferrocyanide
-
enzyme also catalyzes the formation of acetoin from pyruvate and acetaldehyde
-
-
?
pyruvate + ferricyanide + H2O
acetate + CO2 + ferrocyanide
-
addition of 1% lauric acid
-
-
?
pyruvate + ferricyanide + H2O
acetate + CO2 + ferrocyanide
-
-
-
-
?
pyruvate + ferricytochrome b1 + H2O
acetate + CO2 + ferrocytochrome b1
-
-
-
-
?
pyruvate + ferricytochrome b1 + H2O
acetate + CO2 + ferrocytochrome b1
-
the natural electron acceptor for the reduced enzyme is a cell-membrane-associated electron transport system including both ubiquinone-6- and cytochrome b1, with oxygen being the terminal electron acceptor
-
-
?
pyruvate + ubiquinone + H2O
acetate + CO2 + ubiquinol
-
-
-
-
?
pyruvate + ubiquinone + H2O
acetate + CO2 + ubiquinol
-
-
-
-
ir
pyruvate + ubiquinone + H2O
acetate + CO2 + ubiquinol
-
-
-
-
?
pyruvate + ubiquinone + H2O
acetate + CO2 + ubiquinol
-
-
-
-
ir
pyruvate + ubiquinone + H2O
acetate + CO2 + ubiquinol
-
-
-
-
?
pyruvate + ubiquinone-8
acetate + CO2 + ubiquinol-8
-
binding to the phospholipid bilayers is essential for PoxB function in vivo, since ubiquinone, the natural electron acceptor of the enzyme, is dissolved within the membfrane lipid bilayer
-
-
?
pyruvate + ubiquinone-8
acetate + CO2 + ubiquinol-8
-
the role of quinones in the pyruvate oxidase system is investigated in this paper
-
-
?
pyruvate + ubiquinone-8 + H2O
acetate + CO2 + ubiquinol-8
-
-
-
-
?
pyruvate + ubiquinone-8 + H2O
acetate + CO2 + ubiquinol-8
-
-
-
?
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pyruvate + a quinone
acetate + CO2 + a quinol
-
-
-
-
?
pyruvate + ferricytochrome b1 + H2O
acetate + CO2 + ferrocytochrome b1
pyruvate + quinone + H2O
acetate + CO2 + quinol
-
-
-
-
?
pyruvate + ubiquinol-6 + H2O
acetate + CO2 + ubiquinol-6
-
the natural electron acceptor for the reduced enzyme is a cell-membrane-associated electron transport system including both ubiquinone-6 and cytochrome b1, with oxygen being the terminal electron acceptor
-
-
?
pyruvate + ubiquinone + H2O
acetate + CO2 + ubiquinol
pyruvate + ubiquinone-6 + H2O
acetate + CO2 + ubiquinol-6
-
-
-
-
?
pyruvate + ubiquinone-8
acetate + CO2 + ubiquinol-8
pyruvate + ubiquinone-8 + H2O
acetate + CO2 + ubiquinol-8
pyruvate + ferricytochrome b1 + H2O
acetate + CO2 + ferrocytochrome b1
-
-
-
-
?
pyruvate + ferricytochrome b1 + H2O
acetate + CO2 + ferrocytochrome b1
-
the natural electron acceptor for the reduced enzyme is a cell-membrane-associated electron transport system including both ubiquinone-6- and cytochrome b1, with oxygen being the terminal electron acceptor
-
-
?
pyruvate + ubiquinone + H2O
acetate + CO2 + ubiquinol
-
-
-
-
?
pyruvate + ubiquinone + H2O
acetate + CO2 + ubiquinol
-
-
-
-
ir
pyruvate + ubiquinone + H2O
acetate + CO2 + ubiquinol
-
-
-
-
?
pyruvate + ubiquinone + H2O
acetate + CO2 + ubiquinol
-
-
-
-
ir
pyruvate + ubiquinone + H2O
acetate + CO2 + ubiquinol
-
-
-
-
?
pyruvate + ubiquinone-8
acetate + CO2 + ubiquinol-8
-
binding to the phospholipid bilayers is essential for PoxB function in vivo, since ubiquinone, the natural electron acceptor of the enzyme, is dissolved within the membfrane lipid bilayer
-
-
?
pyruvate + ubiquinone-8
acetate + CO2 + ubiquinol-8
-
the role of quinones in the pyruvate oxidase system is investigated in this paper
-
-
?
pyruvate + ubiquinone-8 + H2O
acetate + CO2 + ubiquinol-8
-
-
-
-
?
pyruvate + ubiquinone-8 + H2O
acetate + CO2 + ubiquinol-8
-
-
-
?
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cis-12-hydroxy-9-octadecenoic acid
-
119% of the activitation with palmitic acid
elaidic acid
-
122% of the activitation with palmitic acid
lecithin
-
the hydrophobic moieties of lecithin activate pyruvate oxidase whereas the hydrophilic portions of the molecule have no stimulatory effect
linoleic acid
-
116% of the activitation with palmitic acid
linolelaidic acid
-
113% of the activitation with palmitic acid
linolenic acid
-
126% of the activitation with palmitic acid
Lipids
-
enzyme is activated by lipids, high affinity binding site
-
lysophosphatidylethanolamine
-
highest stimulating activity among the phospholipid extracted from cell membranes tested, if the phospholipids are added directly to the assay mixtures. When water-soluble micellar preparations are substituted for direct addition of the phospholipid to the assay, all the phosphatides demonstrate higher specific activities for stimulating pyruvate oxidase, and the differences in their stimulating capacity are minimized
myristic acid
-
109% of the activitation with palmitic acid
n-nonanoic acid
-
42% of the activitation with palmitic acid
palmitoleic acid
-
137% of the activitation with palmitic acid
trans-12-hydroxy-9-octadecenoic acid
-
103% of the activitation with palmitic acid
lauric acid
-
126% of the activitation with palmitic acid
lauric acid
-
activation by covalent attachment, binding site Lys544
oleic acid
-
-
oleic acid
-
102% of the activitation with palmitic acid
palmitic acid
-
-
palmitic acid
-
activation
additional information
-
stimlating effect of phopholipids, if added directly to the assay mixtures. When water-soluble micellar preparations are substituted for direct addition of the phospholipid to the assay, all the phosphatides demonstrate higher specific activities for stimulating pyruvate oxidase. The differences originally noted in the activating capacities of the various cell envelope phospholipids are minimized. The Km values for the cell envelope phospholipids, synthetic phosphatidylethanolamine, lecithin, and lysolecithin range from 0.9 to 2.2 microM. The Km value for phosphatidylserine is 6.5 microM. The diacylphospholipids exhibit normal Michaelis-Menten kinetics. Lysophosphatides demonstrate considerable divergence from normal Michaelis-Menten kinetics
-
additional information
-
the enzyme activity is stimulated 20- to 50fold, if the enzyme is removed from the membrane particulate fraction of the cell by incubation with a wide variety of amphiphiles
-
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A533T
-
in native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. A533T mobility is similar to wild-type, and slower than Y549Term
A553V
-
in native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. A553V mobility is similar to wild-type, and slower than Y549Term
E564P
-
in native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. E564P has the slowest mobilityamong the mutants tested
R572E
-
in native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. R572E has the fastest mobility among the mutants tested
R572G
-
in native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. R572G shows a midway mobility
R572K
-
in native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. R572K mobility is similar to wild-type, and slower than Y549Term
R572Term
-
deletion of last amino acid. In native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities. R572Term shows a midway mobility
W570Term
-
deletion of last three amino acids. In native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities.. W570Term shows a midway mobility
Y549Term
-
deletion of last 24 amino acids. In native gel electrophoresis, mutant enzymes show differing electrophoretic mobilities.. Y549Term shows a midway mobility
A467T
-
mutant poxB4 is deficient in lipid activation. Mutation is located in the C-terminal half of the gene. The difference between poxB3 and poxB4 is the binding of Triton detergents
S536P
-
mutant poxB3 is deficient in lipid activation but retains full catlytic activity. Mutation is located in the C-terminal half of the gene. The difference between poxB3 and poxB4 is the binding of Triton detergents
additional information
-
expression of a truncated gene lacking the last 24 amino acids of the C-terminus, thus being closely analogous to the activated species produced in vitro by limited chymotrypsin cleavage. The truncated protein is fully active in vitro in the absence of lipid, and its activity is not further increased by addition of lipid activators. The truncated enzyme fails to bind Triton X-114. Strains producing the truncated protein are devoid of oxidase activity in vivo
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Blake, R.; Hager, L.P.
Activation of pyruvate oxidase by monomeric and micellar amphiphiles
J. Biol. Chem.
253
1963-1971
1978
Escherichia coli
brenda
Williams, F.R.; Hager, L.P.
A crystalline flavin pyruvate oxidase
J. Biol. Chem.
236
PC36-PC37
1961
Escherichia coli
brenda
Cunningham, C.C.; Hager, L.P.
Crystalline pyruvate oxidase from Escherichia coli. II. Activation by phospholipids
J. Biol. Chem.
246
1575-1582
1971
Escherichia coli
brenda
Neumann, P.; Weidner, A.; Pech, A.; Stubbs, M.T.; Tittmann, K.
Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli
Proc. Natl. Acad. Sci. USA
105
17390-17395
2008
Escherichia coli (P07003)
brenda
Kiuchi, K.; Hager, L.P.
Reconstitution of the lipid-depleted pyruvate oxidase system of Escherichia coli: the palmitic acid effect
Arch. Biochem. Biophys.
233
776-784
1984
Escherichia coli
brenda
Bertagnolli, B.L.; Hager, L.P.
Role of flavin in acetoin production by two bacterial pyruvate oxidases
Arch. Biochem. Biophys.
300
364-371
1993
Escherichia coli, Pediococcus pseudomonas
brenda
Koland, J.G.; Miller, M.J.; Gennis, R.B.
Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase
Biochemistry
23
445-453
1984
Escherichia coli
brenda
Grabau, C.; Cronan, J.E., Jr.
In vivo function of Escherichia coli pyruvate oxidase specifically requires a functional lipid binding site
Biochemistry
25
3748-3751
1986
Escherichia coli
brenda
Chang, Y.Y.; Cronan, J.E., Jr.
Sulfhydryl chemistry detects three conformations of the lipid binding region of Escherichia coli pyruvate oxidase
Biochemistry
36
11564-11573
1997
Escherichia coli
brenda
Marchal, D.; Pantigny, J.; Laval, J.M.; Moiroux, J.; Bourdillon, C.
Rate constants in two dimensions of electron transfer between pyruvate oxidase, a membrane enzyme, and ubiquinone (coenzyme Q8), its water-insoluble electron carrier
Biochemistry
40
1248-1256
2001
Escherichia coli
brenda
Schreiner, M.E.; Riedel, C.; Holatko, J.; Patek, M.; Eikmanns, B.J.
Pyruvate:quinone oxidoreductase in Corynebacterium glutamicum: molecular analysis of the pqo gene, significance of the enzyme, and phylogenetic aspects
J. Bacteriol.
188
1341-1350
2006
Corynebacterium glutamicum
brenda
Cunningham, C.C.; Hager, L.P.
Reactivation of the lipid-depleted pyruvate oxidase system from Escherichia coli with cell envelope neutral lipids
J. Biol. Chem.
250
7139-7146
1975
Escherichia coli, Escherichia coli K-12
brenda
Recny, M.A.; Hager, L.P.
Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD
J. Biol. Chem.
257
12878-12886
1982
Escherichia coli
brenda
Carter, K.; Gennis, R.B.
Reconstitution of the Ubiquinone-dependent pyruvate oxidase system of Escherichia coli with the cytochrome o terminal oxidase complex
J. Biol. Chem.
260
10986-10990
1985
Escherichia coli
brenda
Mather, M.W.; Gennis, R.B.
Kinetic studies of the lipid-activated pyruvate oxidase flavoprotein of Escherichia coli
J. Biol. Chem.
260
16148-16155
1985
Escherichia coli
brenda
Bertagnolli, B.L.; Hager, L.P.
Activation of Escherichia coli pyruvate oxidase enhances the oxidation of hydroxyethylthiamin pyrophosphate
J. Biol. Chem.
266
10168-10173
1991
Escherichia coli
brenda
Wang, A.Y.; Chang, Y.Y.; Cronan, J.E., Jr.
Role of the tetrameric structure of Escherichia coli pyruvate oxidase in enzyme activation and lipid binding
J. Biol. Chem.
266
10959-10966
1991
Escherichia coli
brenda
Grabau, C.; Cronan, J.E., Jr.
Nucleotide sequence and deduced amino acid sequence of Escherichia coli pyruvate oxidase, a lipid-activated flavoprotein
Nucleic Acids Res.
14
5449-5460
1986
Escherichia coli
brenda
Hamilton, S.E.; Recny, M.; Hager, L.P.
Identification of the high-affinity lipid binding site in Escherichia coli pyruvate oxidase
Biochemistry
25
8179-8183
1986
Escherichia coli, Escherichia coli CG3
brenda
Buchholz, J.; Schwentner, A.; Brunnenkan, B.; Gabris, C.; Grimm, S.; Gerstmeir, R.; Takors, R.; Eikmanns, B.J.; Blombach, B.
Platform Engineering: Corynebacterium glutamicum with reduced pyruvate dehydrogenase complex activity for improved production of L-lysine, L-valine, and 2-ketoisovalerate
Appl. Environ. Microbiol.
79
5566-5575
2013
Corynebacterium glutamicum, Corynebacterium glutamicum aceE A16
brenda
Wieschalka, S.; Blombach, B.; Eikmanns, B.J.
Engineering Corynebacterium glutamicum for the production of pyruvate
Appl. Microbiol. Biotechnol.
94
449-459
2012
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
brenda
Ma, C.; Yu, Z.; Lu, Q.; Zhuang, L.; Zhou, S.
Anaerobic humus and Fe(III) reduction and electron transport pathway by a novel humus-reducing bacterium, Thauera humireducens SgZ-1
Appl. Microbiol. Biotechnol.
99
3619-3628
2015
Thauera humireducens, Thauera humireducens SgZ-1
brenda
Endo, A.; Tanizawa, Y.; Tanaka, N.; Maeno, S.; Kumar, H.; Shiwa, Y.; Okada, S.; Yoshikawa, H.; Dicks, L.; Nakagawa, J.; Arita, M.
Comparative genomics of Fructobacillus spp. and Leuconostoc spp. reveals niche-specific evolution of Fructobacillus spp.
BMC Genomics
16
1117
2015
no activity in Fructobacillus
brenda
Borisov, V.B.; Verkhovsky, M.I.
Oxygen as acceptor
EcoSal Plus
6
2
2015
Escherichia coli
brenda
An, T.T.; Picardal, F.W.
Desulfocarbo indianensis gen. nov., sp. nov., a benzoate-oxidizing, sulfate-reducing bacterium isolated from water extracted from a coal bed
Int. J. Syst. Evol. Microbiol.
64
2907-2914
2014
no activity in Desulfocarbo indianensis
brenda
Li, Z.; Nimtz, M.; Rinas, U.
The metabolic potential of Escherichia coli BL21 in defined and rich medium
Microb. Cell Fact.
13
45
2014
Escherichia coli
brenda
Ianniello, R.G.; Zotta, T.; Matera, A.; Genovese, F.; Parente, E.; Ricciardi, A.
Investigation of factors affecting aerobic and respiratory growth in the oxygen-tolerant strain Lactobacillus casei N87
PLoS ONE
11
e0164065
2016
Lacticaseibacillus casei, Lacticaseibacillus casei N87
brenda
Steinsiek, S.; Stagge, S.; Bettenbrock, K.
Analysis of Escherichia coli mutants with a linear respiratory chain
PLoS ONE
9
e87307
2014
Escherichia coli
brenda
Goris, T.; Schiffmann, C.L.; Gadkari, J.; Schubert, T.; Seifert, J.; Jehmlich, N.; von Bergen, M.; Diekert, G.
Proteomics of the organohalide-respiring Epsilonproteobacterium Sulfurospirillum multivorans adapted to tetrachloroethene and other energy substrates
Sci. Rep.
5
13794
2015
Sulfurospirillum multivorans
brenda