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Literature summary extracted from
- The maltose ABC transporter in the 21(st) century - towards a structural-dynamic perspective on its mode of action (2010), Mol. Microbiol., 77, 1354-1366.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 7.5.2.1 | analysis | the maltose/maltodextrin transport system of Escherichia coli/Salmonella serves as a model for canonical ATP-binding cassette importers in general | Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.5.2.1 | analysis | the maltose/maltodextrin transport system of Escherichia coli/Salmonella serves as a model for canonical ATP-binding cassette importers in general | Escherichia coli |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 7.5.2.1 | the type I maltose ABC importer is encoded within the maltose regulon | Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.5.2.1 | the type I maltose ABC importer is encoded within the maltose regulon | Escherichia coli |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 7.5.2.1 | crystal structure analysis | Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.5.2.1 | crystal structure analysis, e.g. of the crystal structure of the complex in the presence of ATP and MalE, containing MalK mutant E159Q, is resolved at 2.8 A, revealing that MalFG are in a periplasmically open state | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 7.5.2.1 | E159 | the E159Q substitution in MalK prevents ATP from being hydrolysed. This results in an ATP-bound structure, which is thought to represent the transition state for ATP hydrolysis. The crystal shows an open (unliganded) MalE bound to the periplasmic side of the complex, a maltose molecule bound solely to a transmembrane region of MalF, and a closed conformation of the ATP-bound MalK(E59Q)2 subunits | Escherichia coli |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.5.2.1 | membrane | - |
Salmonella enterica subsp. enterica serovar Typhimurium | 16020 | - |
| 7.5.2.1 | membrane | - |
Escherichia coli | 16020 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.5.2.1 | ATP + H2O + maltose/out | Salmonella enterica subsp. enterica serovar Typhimurium | - |
ADP + phosphate + maltose/in | - |
? |  |
| 7.5.2.1 | ATP + H2O + maltose/out | Escherichia coli | - |
ADP + phosphate + maltose/in | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.5.2.1 | Escherichia coli | P68187 | - |
- |
| 7.5.2.1 | Salmonella enterica subsp. enterica serovar Typhimurium | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.5.2.1 | ATP + H2O + maltose/out | - |
Salmonella enterica subsp. enterica serovar Typhimurium | ADP + phosphate + maltose/in | - |
? | |
| 7.5.2.1 | ATP + H2O + maltose/out | - |
Escherichia coli | ADP + phosphate + maltose/in | - |
? | |
| 7.5.2.1 | ATP + H2O + maltose/out | the MalK dimer complex component provides the energy for maltose transport by hydrolysing ATP | Salmonella enterica subsp. enterica serovar Typhimurium | ADP + phosphate + maltose/in | - |
? | |
| 7.5.2.1 | ATP + H2O + maltose/out | the MalK dimer complex component provides the energy for maltose transport by hydrolysing ATP | Escherichia coli | ADP + phosphate + maltose/in | - |
? | |
| 7.5.2.1 | additional information | the maltose transporter solubilized in detergent micelles hydrolyses ATP independently of the presence of liganded MalE, ATP-induced MalK dimer closure occurs in absence of MalK. The isolated MalK2 domains are also known to exhibit a spontaneous but low ATPase activity | Salmonella enterica subsp. enterica serovar Typhimurium | ? | - |
? | |
| 7.5.2.1 | additional information | the maltose transporter solubilized in detergent micelles hydrolyses ATP independently of the presence of liganded MalE, ATP-induced MalK dimer closure occurs in absence of MalK. The isolated MalK2 domains are also known to exhibit a spontaneous but low ATPase activity | Escherichia coli | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.5.2.1 | More | the maltose/maltodextrin transport system is composed of periplasmic maltose-binding protein, MalE, the pore-forming subunits MalF and MalG, and a homodimer of the nucleotide-binding subunit, MalK, overall structure, component interactions, and comparison, detailed overview. Structure modelling. The MalK dimer provides the energy for maltose transport by hydrolysing ATP. The structure of MalK is solved in two (nucleotide-free) apo-states, one ADP-bound and one ATP-bound state, representing two open, a semi-open and a closed conformation of the dimer, respectively, dynamics, overview | Escherichia coli |
| 7.5.2.1 | More | the maltose/maltodextrin transport system is composed of periplasmic maltose-binding protein, MalE, the pore-forming subunits MalF and MalG, and a homodimer of the nucleotide-binding subunit, MalK, overall structure, component interactions, and comparison, detailed overview. Structure modelling.. The MalK dimer provides the energy for maltose transport by hydrolysing ATP | Salmonella enterica subsp. enterica serovar Typhimurium |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.5.2.1 | maltose ABC transporter | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.5.2.1 | maltose ABC transporter | - |
Escherichia coli |
| 7.5.2.1 | More | the enzyme belongs to the type I canonical ABC importers of the ATP-binding cassette, ABC, transporters | Salmonella enterica subsp. enterica serovar Typhimurium |
| 7.5.2.1 | More | the enzyme belongs to the type I canonical ABC importers of the ATP-binding cassette, ABC, transporters | Escherichia coli |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 7.5.2.1 | metabolism | the type I maltose ABC importer is encoded within the maltose regulon, which enables the bacteria to feed on maltose and maltodextrins, alpha-1,4-linked oligosaccharides up to seven glucose units, formed by enzymatic cleavage of starch or glycogen | Escherichia coli |
| 7.5.2.1 | metabolism | the type I maltose ABC importer is encoded within the maltose regulon, which enables the bacteria to feed on maltose and maltodextrins, alpha-1,4-linked oligosaccharides up to seven glucose units, formed by enzymatic cleavage of starch or glycogen. The C-terminal domain of MalK has a dual regulatory function: it controls the activity of MalT, the positive transcriptional regulator of the maltose regulon, and it is the primary site at which dephosphorylated enzyme IIAGlc of the phosphoenolpyruvate phosphotransferase system binds, preventing maltose uptake | Salmonella enterica subsp. enterica serovar Typhimurium |
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Release 2023.1 (January 2023)
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