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Literature summary for 1.2.5.1 extracted from

  • Recny, M.A.; Hager, L.P.
    Reconstitution of native Escherichia coli pyruvate oxidase from apoenzyme monomers and FAD (1982), J. Biol. Chem., 257, 12878-12886.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
cell membrane cell membrane-associated Escherichia coli
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate + ferricytochrome b1 + H2O Escherichia coli
-
acetate + CO2 + ferrocytochrome b1
-
?
pyruvate + ubiquinone-6 + H2O Escherichia coli
-
acetate + CO2 + ubiquinol-6
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Renatured (Commentary)

Renatured (Comment) Organism
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 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + ferricyanide + H2O
-
Escherichia coli acetate + CO2 + ferrocyanide
-
?
pyruvate + ferricytochrome b1 + H2O
-
Escherichia coli acetate + CO2 + ferrocytochrome b1
-
?
pyruvate + ubiquinone-6 + H2O
-
Escherichia coli acetate + CO2 + ubiquinol-6
-
?

Cofactor

Cofactor Comment Organism Structure
FAD
-
Escherichia coli