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Literature summary for 7.5.2.1 extracted from

  • Oloo, E.O.; Fung, E.Y.; Tieleman, D.P.
    The dynamics of the MgATP-driven closure of MalK, the energy-transducing subunit of the maltose ABC transporter (2006), J. Biol. Chem., 281, 28397-28407.
    View publication on PubMed
Search for more literature for 7.5.2.1

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, bound to ATP, binding structure and mechanism of MgATP to the enzyme 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
-
 ?
additional information Escherichia coli interactions of MalK with the regulatory proteins MalT and enzyme IIAglc ?
-
 ?

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
-
 ?
ATP + H2O + maltose/out molecular dynamics simulations to study the ATP-driven association of the NBDs of the maltose ABC transporter, MalK, based on the crystal structures of its open and semiopen dimers, MgATP-dependent opening and closure, mechanism, overview Escherichia coli ADP + phosphate + maltose/in
-
 ?
additional information interactions of MalK with the regulatory proteins MalT and enzyme IIAglc Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
MalK
-
 Escherichia coli