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pyruvate + ferricyanide + H2O
acetate + CO2 + ferrocyanide
-
-
-
?
pyruvate + ubiquinone-8 + H2O
acetate + CO2 + ubiquinol-8
-
-
-
?
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 + 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 + 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 + 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 + 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-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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pyruvate + ubiquinone-8 + H2O
acetate + CO2 + ubiquinol-8
-
-
-
?
pyruvate + ferricytochrome b1 + H2O
acetate + CO2 + ferrocytochrome b1
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-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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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
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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Activation of pyruvate oxidase by monomeric and micellar amphiphiles
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253
1963-1971
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Escherichia coli
brenda
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