1.2.5.1: pyruvate dehydrogenase (quinone)
This is an abbreviated version!
For detailed information about pyruvate dehydrogenase (quinone), go to the full flat file.
Word Map on EC 1.2.5.1
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1.2.5.1
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corynebacterium
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glutamicum
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flavoprotein
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fed-batch
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thiamin
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acetohydroxyacid
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transaminase
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volumetric
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2-ketoisovalerate
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isomeroreductase
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l-valine
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ilvbncd
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dihydroxyacid
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l-lactate
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transhydrogenase
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pta-acka
- 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
Reaction
Synonyms
EC 1.2.2.2, ECPOX, POX, poxB, POXEC, pqo, pyruvate (quinone) dehydrogenase, pyruvate oxidase, pyruvate oxidase B, pyruvate:quinone oxidoreductase, pyruvate:ubiquinone-8-oxidoreductase, ubiquinione-dependent pyruvate oxidase, ubiquinone-dependent pyruvate oxidase
ECTree
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General Information
General Information on EC 1.2.5.1 - pyruvate dehydrogenase (quinone)
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malfunction
physiological function
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inactivation of the pyruvate:quinone oxidoreductase results in a more efficient L-valine production in Corynebacterium glutamicum strain aceE A16
malfunction
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there is a positive effect on L-valine production by the inactivation of the pyruvate:quinone oxidoreductase due to increased pyruvate availability
malfunction
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there is a positive effect on L-valine production by the inactivation of the pyruvate:quinone oxidoreductase due to increased pyruvate availability
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malfunction
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inactivation of the pyruvate:quinone oxidoreductase results in a more efficient L-valine production in Corynebacterium glutamicum strain aceE A16
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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
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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
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the activated enzyme can be efficiently regulated by the oxidation level of the quinone pool in natural membranes
physiological function
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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