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Literature summary for 7.5.2.1 extracted from

  • Cui, J.; Qasim, S.; Davidson, A.
    Uncoupling substrate transport from ATP hydrolysis in the Escherichia coli maltose transporter (2010), J. Biol. Chem., 285, 39986-39993.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D380G substitution of aspartate for glycine in the maltose-binding site of MalF likely generates a futile cycle by preventing maltose from binding to MalFGK2 during the catalytic cycle Escherichia coli
E159Q the transporter containing the MalK-E159Q mutation is defective in ATP hydrolysis Escherichia coli
additional information in deletion mutant MalG-DELTAscoop a four-residue deletion of a periplasmic loop of MalG limits its reach into the maltose-binding pocket of MBP, allowing maltose to remain associated with MBP during the catalytic cycle. Uncoupling of transport and ATP hydrolysis in the MalG-DELTAscoop and MalF-G380D mutants, overview Escherichia coli
W230C site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein Escherichia coli
W340C site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein Escherichia coli
W62C site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein, but retains good function in maltose transport and MBP-stimulated ATPase activities Escherichia coli
Y155C site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein Escherichia coli
Y341C site-directed mutagenesis, mutation in the maltose binding protein, the mutant shows altered kinetics of substrate binding compared to the wild-type maltose binding protein, but retaines good function in maltose transport and MBP-stimulated ATPase activities Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
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
multimer the maltose transporter consists of a periplasmic maltose binding protein and a multisubunit membrane transporter, MalFGK2 Escherichia coli

Synonyms

Synonyms Comment Organism
MalFGK2
-
Escherichia coli
maltose transporter
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2
-
maltose transport assay Escherichia coli
8
-
ATPase assay at Escherichia coli

General Information

General Information Comment Organism
evolution the enzyme is a member of the ATP-binding cassette superfamily Escherichia coli
malfunction the addition of ATP and EDTA (to trigger the outwardfacing conformation) to the MBP-MalFGK2 system in the absence of maltose increases the mobility of W62C-SL in the MalG-DELTAscoop system but decreases it in the wild-type Escherichia coli
physiological function the enzyme couples the energy from ATP hydrolysis to the active transport of substrates across the membrane Escherichia coli