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Literature summary for 1.19.1.1 extracted from

  • Crain, A.V.; Broderick, J.B.
    Flavodoxin cofactor binding induces structural changes that are required for protein-protein interactions with NADP(+) oxidoreductase and pyruvate formate-lyase activating enzyme (2013), Biochim. Biophys. Acta, 1834, 2512-2519.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Escherichia coli B / ATCC 11303
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate flavodoxin is more structured when the FMN cofactor is bound. Holo-flavodoxin is capable of associating with NADP+-dependent flavodoxin oxidoreductase, whereas there is no detectable interaction between apo-flavodoxin and the protein Escherichia coli ?
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additional information substrate flavodoxin is more structured when the FMN cofactor is bound. Holo-flavodoxin is capable of associating with NADP+-dependent flavodoxin oxidoreductase, whereas there is no detectable interaction between apo-flavodoxin and the protein Escherichia coli B / ATCC 11303 ?
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?