Literature summary for 7.5.2.1 extracted from

Mourez, M.; Jehanno, M.; Schneider, E.; Dassa, E.
In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: modulation by ATP (1998), Mol. Microbiol., 30, 353-363.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + maltose/out	the putative helical domain of the nucleotide binding domains is involved, through its conformational changes, in the coupling between the transmembrane domains and the ATP binding/hydrolysis at the nucleotide-binding domains	Escherichia coli	ADP + phosphate + maltose/in	-	?

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Release 2023.1 (January 2023)