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 | UniProt | Comment | Textmining |
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Escherichia coli | - |
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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 | Comment | Organism |
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poxB | - |
Escherichia coli |
Organism | Comment | Expression |
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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 |