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Information on EC 1.2.5.1 - pyruvate dehydrogenase (quinone)
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1.2.5.1 pyruvate dehydrogenase (quinone)IUBMB Comments
Flavoprotein (FAD) . This bacterial enzyme is located on the inner surface of the cytoplasmic membrane and coupled to the respiratory chain via ubiquinone [2,3]. Does not accept menaquinone. Activity is greatly enhanced by lipids [4,5,6]. Requires thiamine diphosphate . The enzyme can also form acetoin .
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Word Map
- 1.2.5.1
-
corynebacterium
- glutamicum
- flavoprotein
-
fed-batch
- thiamin
-
acetohydroxyacid
- transaminase
-
volumetric
- 2-ketoisovalerate
-
isomeroreductase
- l-valine
-
ilvbncd
-
dihydroxyacid
- l-lactate
-
transhydrogenase
-
pta-acka
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
pyruvate:quinone oxidoreductase, poxec, pyruvate oxidase b, ubiquinone-dependent pyruvate oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
POX
poxB
pqo
pyruvate oxidase
pyruvate:quinone oxidoreductase
pyruvate oxidase
-
-
pyruvate oxidase
-
enzyme also catalyzes the formation of acetoin from pyruvate and acetaldehyde
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pyruvate + ubiquinone + H2O = acetate + CO2 + ubiquinol
-
-
-
-
pyruvate + ubiquinone + H2O = acetate + CO2 + ubiquinol
enzyme also catalyzes the formation of acetoin from pyruvate and acetaldehyde
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
pyruvate:ubiquinone oxidoreductase
Flavoprotein (FAD) [1]. This bacterial enzyme is located on the inner surface of the cytoplasmic membrane and coupled to the respiratory chain via ubiquinone [2,3]. Does not accept menaquinone. Activity is greatly enhanced by lipids [4,5,6]. Requires thiamine diphosphate [7]. The enzyme can also form acetoin [8].
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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
pyruvate + dimethylmenoquinone + H2O
acetate + CO2 + dimethylmenoquinol
-
-
-
-
?
pyruvate + ferricyanide
acetate + CO2 + ferrocyanide
-
activity assayed photometrically by monitoring the reduction of 2,6-dichloroindophenol
-
-
?
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 + 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-30 + H2O
acetate + CO2 + ubiquinol-30
-
ubiquinone-30 is rapidly reduced by pyruvate oxidase only in the presence of palmitic acid
-
-
?
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
-
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 + 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-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
-
-
?
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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
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 + 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-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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
role for FAD in acetoin formation is based on a structural requirement. In the acetoin reaction, FAD does not participate in a redox function
FAD
Pediococcus pseudomonas
-
role for FAD in acetoin formation is based on a structural requirement. In the acetoin reaction, FAD does not participate in a redox function
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alpha-chymotrypsin
-
20 micromol/ml, wild-type enzyme and the mutant poxB4 are activated 15- and 70fold, respectively, and the mutant poxB3 is activated 14fold
anionic detergents
-
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
Cationic detergents
-
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
SDS
-
20 microM, activates the wild-type and mutant enzymes, poxB3 and poxB4, 15-, 20-, and 70fold, respectively
Triton X-100
-
2.2 mM, activates the wild-type and mutant enzymes, poxB3 and poxB4, 32-, 4-, and 6fold, respectively. With the addition of alpha-chymotrypsin the activation of the mutant enzymes poxB3 and poxB4 is increased 14- and 39fold, respectively
Zwitterionic detergents
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cis-12-hydroxy-9-octadecenoic acid
-
119% 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
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
trans-12-hydroxy-9-octadecenoic acid
-
103% of the activitation with palmitic acid
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
the rate of decarboxylation of pyruvate to form CO2, and hydroxyethylthiamine diphosphate for both activated and unactivated forms of the enzyme is identical within experimental error. The pseudo-first order rate constant for the decarboxylation step is 60-80 per s. The pseudo-first order rate of oxidation of hydroxyethylthiamine diphosphate and concomitant enzyme-bound flavin reduction with unactivated enzyme is 2.85 per s and increases 145fold for lipid-activated enzyme to 413 per s and 61fold for the proteolytically activated enzyme to 173 per s. The rate of oxidation of enzyme-FADH is very fast for both unactivated and activated enzyme, being 1041 per s and 645 per s, respectively. The FAD reduction step is the rate-limiting step in the overall reaction for unactivated enzyme. Alternatively, the rate-limiting step in the overall reaction with the activated enzyme shifts to one of the partial steps in the decarboxylation reaction
-
additional information
additional information
-
the unactivated form of enzyme is markedly hysteretic. At low substrate concentration, there is an initial acceleration in enzyme turnover due to slow interconversion between two forms of the enzyme, one with low turnover and one which rapidly turns over. During turnover, even in the absence of lipid activators, some of the enzyme converts to the rapid-turnover form. This slow interconversion precludes a steady state from being established. Lipid activators shift the equilibrium to favor the rapid turnover form of the enzyme. Once the enzyme is locked into an activated conformation, the hysteresis is no longer observed. Activation results in both increased rates of electron transfer into and out of the flavin
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
60
ferricyanide
-
without activation of the flavoprotein by proteolytic reactions, i.e. trypsin or chymotrypsin, pH and temperature not specified in the publication
883
ferricyanide
-
with activation of the flavoprotein by proteolytic reactions, i.e. trypsin or chymotrypsin, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
270
-
270 micromol of ferricyanide min-1 mg-1 of flavoprotein subunit, 25°C, pH not specified in the publication
60
-
mutant poxB4 in presence of 20 microM SDS, pH and temperature not specified in the publication
90
-
wild-type enzyme, pH and temperature not specified in the publication
additional information
additional information
-
purified enzyme, after crystallization, 6000 Units/mg protein
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the pyruvate oxidase system and the electron transport system are associated with the cell envelope-membrane fraction
brenda
-
inner surface of the cytoplasmic membrane and is coupled to the Escherichia coli aerobic respiratory chain
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
inactivation of the pyruvate:quinone oxidoreductase results in a more efficient L-valine production in Corynebacterium glutamicum strain aceE A16
malfunction
-
there is a positive effect on L-valine production by the inactivation of the pyruvate:quinone oxidoreductase due to increased pyruvate availability
malfunction
-
there is a positive effect on L-valine production by the inactivation of the pyruvate:quinone oxidoreductase due to increased pyruvate availability
-
malfunction
-
inactivation of the pyruvate:quinone oxidoreductase results in a more efficient L-valine production in Corynebacterium glutamicum strain aceE A16
-
physiological function
-
electron transport from pyruvate to oxygen in the liposome system generates a trans-membrane potential of at least 180 mV, negative inside, which is sensitive to the uncouplers carbonyl cyanide p-(trichloromethoxy)phenylhydrazone and valinomycin. A transmembrane potential is also generated by the oxidation of ubiquinol 1 by the terminal oxidase in the absence of the flavoprotein. The pyruvate oxidase can directly reduce ubiquinone 8 within the phospholipid bilayer, menaquinone 8 will not effectively substitute for ubiquinone 8 in this electron-transfer chain, and the cytochrome d terminal oxidase functions as a ubiquinol 8 oxidase and serves as a coupling site in the Escherichia coli aerobic respiratory chain
physiological function
-
inactivation of the chromosomal pqo gene leads to the absence of pyruvate:quinone oxidoreductase activity. Growth and amino acid production are not affected under either condition tested. Introduction of plasmid-bound pqo into a pyruvate dehydrogenase complex-negative strain partially relieves the growth phenotype of this mutant, indicating that high pyruvate:quinone oxidoreductase activity can compensate for the function of the pyruvate dehydrogenase complex
physiological function
-
the activated enzyme can be efficiently regulated by the oxidation level of the quinone pool in natural membranes
physiological function
-
the cytochrome o complex functions as an efficient ubiquinol-8 oxidase in reconstituted proteoliposomes, and ubiquinone-8 serves as an electron carrier from the flavoprotein pyruvate oxidase to the cytochrome complex. Electron flow from the flavoprotein to oxygen in the reconstituted proteoliposomes generates a transmembrane potential of at least 120 mV, negative inside, which is sensitive to ionophore uncouplers and inhibitorso f the terminal oxidase. The minimal composition of this respiratory chain is a flavoprotein dehydrogenase, ubiquinone-8, and the cytochrome o complex
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
-
the lauric acid-labeled enzyme is not digested neither by trypsin nor alpha-chymotrypsin in the presence of 0.1% SDS. Effective digestion is achieved by thermolysin, to a 45000 and a 15000 Da fragment
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
when two poxB gene alleles coexist in cells either on a single plasmid or on two compatible plasmids, heterotetrameric species are formed in addition to homotetramers. The concentration of tetramer species varies according to the concentrations of the different subunit present. The distribution of each tetramer species seems virtually identical to those theoretically expected based on random mixing. The intrinsic activity of pyruvate oxidase is not affected by interactions among the four subunits. Each subunit of the tetramer catalyzes the oxidase reaction independently
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystalline enzyme does not contain thiamine diphosphate but has an absolute thiamine diphosphate requirement for the reduction of the enzyme-bound FAD
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the enzyme is purified from an Escherichia coli strain CG3 harboring a plasmid carrying a plasmid th eoxidase gene
-
the poxB4 mutant is purified from the strain CG3, carrying plasmid pYYC16, which overproduces the enzyme about 20fold. Purified on DEAE-cellulose, >90% pure
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
systematical substitution of cysteine at 18 amino acid positions within the C-terminal region to obtain a panel of proteins each having a single residue changed to cysteine. In the absence of pyruvate, the cysteine residues of the modified PoxB proteins fail to form disulfide bonds, generally fail to react with a large and rigid hydrophilic sulfhydryl reagent, 4-acetamido-4'-[(iodoacetyl)amino]stilbene-2,2'-disulfonic acid (IASD), and in some cases react weakly with a smaller more hydrophobic reagent, N-ethylmaleimide. In this conformation, the C termini appear fixed in a rigid environment having limited exposure to solvent. In the presence of pyruvate, all of the C-terminal cysteine residues, except the two most distal from the C terminus, react with both sulfhydryl reagents and readily formed disulfide cross-linked species. In the presence of lipid activators, Triton X-100 or dipalmitoylphosphatidylglycerol, a subset of the cysteine-substituted proteins no longer reacts with the membrane-impermeable IASD reagent, indicating penetration of these protein segments into the lipid micelle
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of a minimal respiratory chain consisting of pyruvate oxidase and cytochrome d terminal oxidase plus ubiquinone8 incorporated in phospholipid vesicles. The catalytic velocity of the reconstituted liposome system is about 30% of that observed when the flavoprotein is reconstituted with Escherichia coli membranes
-
reconstitution of enzyme with a supported lipidic structure. The activated enzyme can be efficiently regulated by the oxidation level of the quinone pool in natural membranes
-
reconstitution of the native enzymatically active protein can be accomplished by incubating equimolar concentrations of apomonomers and FAD at pH 6.5. The second order reaction of apomonomers with FAD to form an initial monomer-FAD complex is fast. The rate-limiting step for enzymatic reactivation appears to be the folding of the polypeptide chain in the monomer-FAD complex to reconstitute the three-dimensional FAD binding site prior to subunit reassociation. The subsequent formation of native tetramers proceeds via an essentially irreversible dimer assembly pathway
-
removal of the lipids from the membrane particles by extraction with aqueous acetone or hydrolysis of the phospholipids by treatment with Bacillus cereus phospholipase C results in a complete loss of electron transport activity. Practically all the neutral lipids and 65% of the phospholipids are removed by this treatment. Phospholipase treatment results in a loss of 75% of the membrane phospholipid phosphorus. The diglycerides and the neutral lipids produced by phospholipase hydrolysis remain associated with the particles. Addition of neutral lipid and detergent hepta-D,L-alanyl-dodecylamide to the acetone-extracted material results in a restoration of 37% of the original particle activity. Addition of neutral lipid and hepta-DL-alanyl dodecylamide to phospholipase-treated particles completely restores the original electron transport activity. Addition of ubiquinone from either yeast or Escherichia coli will restore pyruvate oxidase activity when the quinones are supplemented with photoinactivated neutral lipid. No restoration of activity to phospholipase-treated particles is noted upon the addition of either menaquinone 6 or menaquinone 8 to the reconstitution system
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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