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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Activating Compound
Activating Compound on EC 1.2.5.1 - pyruvate dehydrogenase (quinone)
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cis-12-hydroxy-9-octadecenoic acid
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119% of the activitation with palmitic acid
lecithin
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the hydrophobic moieties of lecithin activate pyruvate oxidase whereas the hydrophilic portions of the molecule have no stimulatory effect
lysophosphatidylethanolamine
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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
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103% of the activitation with palmitic acid
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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
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additional information
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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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