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Literature summary for 1.2.5.1 extracted from

  • Chang, Y.Y.; Cronan, J.E., Jr.
    Sulfhydryl chemistry detects three conformations of the lipid binding region of Escherichia coli pyruvate oxidase (1997), Biochemistry, 36, 11564-11573.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate + ubiquinone-8 Escherichia coli binding to the phospholipid bilayers is essential for PoxB function in vivo, since ubiquinone, the natural electron acceptor of the enzyme, is dissolved within the membfrane lipid bilayer acetate + CO2 + ubiquinol-8
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + ferricyanide activity assayed photometrically by monitoring the reduction of 2,6-dichloroindophenol Escherichia coli acetate + CO2 + ferrocyanide
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 ?
pyruvate + ubiquinone-8 binding to the phospholipid bilayers is essential for PoxB function in vivo, since ubiquinone, the natural electron acceptor of the enzyme, is dissolved within the membfrane lipid bilayer Escherichia coli acetate + CO2 + ubiquinol-8
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 ?

Synonyms

Synonyms Comment Organism
poxB
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 Escherichia coli

Expression

Organism Comment Expression
Escherichia coli 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 additional information