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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Expression
Expression on EC 1.2.5.1 - pyruvate dehydrogenase (quinone)
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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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