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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)

Renatured

Renatured on EC 1.2.5.1 - pyruvate dehydrogenase (quinone)

for references in articles please use BRENDA:EC1.2.5.1

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of a minimal respiratory chain consisting of pyruvate oxidase and cytochrome d terminal oxidase plus ubiquinone8 incorporated in phospholipid vesicles. The catalytic velocity of the reconstituted liposome system is about 30% of that observed when the flavoprotein is reconstituted with Escherichia coli membranes
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reconstitution of enzyme with a supported lipidic structure. The activated enzyme can be efficiently regulated by the oxidation level of the quinone pool in natural membranes
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reconstitution of the native enzymatically active protein can be accomplished by incubating equimolar concentrations of apomonomers and FAD at pH 6.5. The second order reaction of apomonomers with FAD to form an initial monomer-FAD complex is fast. The rate-limiting step for enzymatic reactivation appears to be the folding of the polypeptide chain in the monomer-FAD complex to reconstitute the three-dimensional FAD binding site prior to subunit reassociation. The subsequent formation of native tetramers proceeds via an essentially irreversible dimer assembly pathway
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removal of the lipids from the membrane particles by extraction with aqueous acetone or hydrolysis of the phospholipids by treatment with Bacillus cereus phospholipase C results in a complete loss of electron transport activity. Practically all the neutral lipids and 65% of the phospholipids are removed by this treatment. Phospholipase treatment results in a loss of 75% of the membrane phospholipid phosphorus. The diglycerides and the neutral lipids produced by phospholipase hydrolysis remain associated with the particles. Addition of neutral lipid and detergent hepta-D,L-alanyl-dodecylamide to the acetone-extracted material results in a restoration of 37% of the original particle activity. Addition of neutral lipid and hepta-DL-alanyl dodecylamide to phospholipase-treated particles completely restores the original electron transport activity. Addition of ubiquinone from either yeast or Escherichia coli will restore pyruvate oxidase activity when the quinones are supplemented with photoinactivated neutral lipid. No restoration of activity to phospholipase-treated particles is noted upon the addition of either menaquinone 6 or menaquinone 8 to the reconstitution system
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