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Literature summary for 7.5.2.1 extracted from

  • Nikaido, H.
    Maltose transport system of Escherichia coli: an ABC-type transporter (1994), FEBS Lett., 346, 55-58.
    View publication on PubMed
Search for more literature for 7.5.2.1

Activating Compound

Activating Compound Comment Organism Structure
maltose-binding protein required by wild-type strain, mutant strain does not require maltose-binding protein for transport. The major function of the maltose-binding protein is to send a transmembrane signal, in the presence of ligands, to the ATPase subunits on the inner side of the membrane. In addition it performs a special function in the translocation of the larger ligands, maltodextrins, perhaps by aligning them from entry into the channel Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasmic membrane the maltose transport system is composed of a periplasmic-binding protein, the presumed transmembrane channel made up of MalF and MalG proteins, and two copies of the ATPase subunit Escherichia coli
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periplasm the maltose transport system is composed of a periplasmic-binding protein, the presumed transmembrane channel is made up of MalF and MalG proteins, and two copies of the ATPase subunit Escherichia coli
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Purification (Commentary)

Purification (Comment) Organism
wild-type strain and mutant strain that does not require maltose-binding protein for transport Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + maltose/out
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 Escherichia coli ADP + phosphate + maltose/in
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 ?

Subunits

Subunits Comment Organism
? the maltose transport system is composed of a periplasmic-binding protein, the presumed transmembrane channel made up of MalF and MalG proteins, and two copies of the ATPase subunit Escherichia coli