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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.

Wordmap for 1.2.5.1

Word Map on EC 1.2.5.1 Wordmap for 1.2.5.1

Reaction

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pyruvate
+
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ubiquinone
+
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H2O
=
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acetate
+
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CO2
+
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ubiquinol

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

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.5 With a quinone or similar compound as acceptor
                EC 1.2.5.11.2.5.1 pyruvate dehydrogenase (quinone)

Expression

Expression on EC 1.2.5.1 - pyruvate dehydrogenase (quinone)

for references in articles please use BRENDA:EC1.2.5.1

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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is reduced anaerobically
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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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