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Literature summary for 7.5.2.1 extracted from

  • Horn, C.; Jenewein, S.; Tschapek, B.; Bouschen, W.; Metzger, S.; Bremer, E.; Schmitt, L.
    Monitoring conformational changes during the catalytic cycle of OpuAA, the ATPase subunit of the ABC transporter OpuA from Bacillus subtilis (2008), Biochem. J., 412, 233-244.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
MalK crystal structure analysis in the semi-open, nucleotide-free, the open nucleotide-free, the ATP-bound, and the ADP-bound states 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 MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P68187
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + maltose/out
-
Escherichia coli ADP + phosphate + maltose/in
-
?
additional information MalK is the ABC-ATPase of the maltose importer of Escherichia coli. The MalK accessory domain interacts with at least two enzymes, MalT and IIA Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
dimer MalK structure comparison, the enzyme contains two cystathione beta-synthetase domains Escherichia coli
More MalK-derived homology model, overview Escherichia coli

Synonyms

Synonyms Comment Organism
MalK
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Escherichia coli
maltose importer
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP structure of the nucleotide-binding domain of the maltose importer, comparison, overview Escherichia coli