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Literature summary extracted from

  • Grote, M.; Bordignon, E.; Polyhach, Y.; Jeschke, G.; Steinhoff, H.J.; Schneider, E.
    A comparative electron paramagnetic resonance study of the nucleotide-binding domains catalytic cycle in the assembled maltose ATP-binding cassette importer (2008), Biophys. J., 95, 2924-2938.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.5.2.1 recombinant His-tagged enzyme expression in Escherichia coli strain JM109 Salmonella enterica subsp. enterica serovar Typhimurium
7.5.2.1 recombinant His-tagged enzyme expression in Escherichia coli strain JM109 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.5.2.1 vanadate
-
 Escherichia coli
7.5.2.1 vanadate
-
 Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.5.2.1 Mg2+ required Salmonella enterica subsp. enterica serovar Typhimurium
7.5.2.1 Mg2+ required Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
7.5.2.1 Escherichia coli P68187
-
-
7.5.2.1 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.5.2.1 recombinant His-tagged enzyme from Escherichia coli strain JM109 Salmonella enterica subsp. enterica serovar Typhimurium
7.5.2.1 recombinant His-tagged enzyme from Escherichia coli strain JM109 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.5.2.1 additional information although MalF and MalG differ in the number of transmembrane segments of 8 and 6, respectively, and their amino acid sequences, both contain the so-called EAA-motif, i.e. L-loop or coupling helix, which is in contact with MalK. MalF and MalG form a large central cavity for transport, but maltose is only bound to MalF. The MalK subunits bind and hydrolyze ATP, thereby generating the power stroke necessary for the rearrangements of MalFG, quantitative analysis of conformational changes of the nucleotide-binding subunits, MalK2, of the maltose ATP-binding cassette importer MalFGK2 during the transport cycle, overview Salmonella enterica subsp. enterica serovar Typhimurium ?
-
 ?
7.5.2.1 additional information quantitative analysis of conformational changes of the nucleotide-binding subunits, MalK2, of the maltose ATP-binding cassette importer MalFGK2 during the transport cycle, overview Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
7.5.2.1 More the maltose transporter consists of two transmembrane subunits, MalF and MalG, a homodimer of the nucleotide-binding subunits, MalK2, at the cytoplasmic side of the membrane and the periplasmic maltose-binding protein, MalE Salmonella enterica subsp. enterica serovar Typhimurium
7.5.2.1 More the maltose transporter consists of two transmembrane subunits, MalF and MalG, a homodimer of the nucleotide-binding subunits, MalK2, at the cytoplasmic side of the membrane and the periplasmic maltose-binding protein, MalE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
7.5.2.1 maltose ATP-binding cassette importer
-
 Salmonella enterica subsp. enterica serovar Typhimurium
7.5.2.1 maltose ATP-binding cassette importer
-
 Escherichia coli