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Literature summary for 7.5.2.1 extracted from

  • Davidson, A.L.; Nikaido, H.
    Purification and characterization of the membrane associated components of the maltose transport system from Escherichia coli (1991), J. Biol. Chem., 266, 8946-8951.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasmic membrane the three membrane-associated components of the transport system MalF, MalG and MalK behave as a multiprotein complex Escherichia coli
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
170000
-
tetrameric FGK2 complex, gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.011
-
-
Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? F,G,K2, the three membrane-associated components of the transport system MalF, MalG and MalK behave as a multiprotein complex Escherichia coli