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Literature summary for 7.5.2.1 extracted from

  • Gould, A.; Shilton, B.
    Studies of the maltose transport system reveal a mechanism for coupling ATP hydrolysis to substrate translocation without direct recognition of substrate (2010), J. Biol. Chem., 285, 11290-11296.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.5.2.1

Activating Compound

Activating Compound Comment Organism Structure
additional information the ATPase activity of the maltose transporter MalFGK2 is dependent on interactions with the maltose-binding protein, MBP. A mutant sMBP, that can bind both maltose and sucrose, can stimulate ATPase activity of MalFGK2 to equal levels with either ligand bound, the activation is highly reduced compared to the wild-type MBP, structural basis and modeling the open sMBP structure bound to MalFGK2 in the transition state for ATP hydrolysis, mechanism and structure-function relationship, overview Escherichia coli

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
-
 ?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 ATPase assay at Escherichia coli

pH Optimum

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

General Information

General Information Comment Organism
physiological function the ATPase activity of the maltose transporter MalFGK2 is dependent on interactions with the maltose-binding protein, MBP Escherichia coli