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Literature summary for 7.5.2.1 extracted from

  • Hulsmann, A.; Lurz, R.; Scheffel, F.; Schneider, E.
    Maltose and maltodextrin transport in the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius is mediated by a high-affinity transport system that includes a maltose binding protein tolerant to low pH (2000), J. Bacteriol., 182, 6292-6301.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.5.2.1

Cloned(Commentary)

Cloned (Comment) Organism
maltose-binding protein MalE expressed in Escherichia coli Alicyclobacillus acidocaldarius

Inhibitors

Inhibitors Comment Organism Structure
acarbose
-
 Alicyclobacillus acidocaldarius
alpha-cyclodextrin
-
 Alicyclobacillus acidocaldarius
beta-cyclodextrin
-
 Alicyclobacillus acidocaldarius
gamma-cyclodextrin
-
 Alicyclobacillus acidocaldarius
maltotetraose
-
 Alicyclobacillus acidocaldarius

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00091
-
 maltose
-
 Alicyclobacillus acidocaldarius

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall the majority of the maltose binding protein is distributed throughout the cell wall, while only smaller quantities are located in the cytoplasmic membrane Alicyclobacillus acidocaldarius 5618
-
cytoplasmic membrane the majority of the maltose binding protein is distributed throughout the cell wall, while only smaller quantities are located in the cytoplasmic membrane Alicyclobacillus acidocaldarius
-
-

Organism

Organism UniProt Comment Textmining
Alicyclobacillus acidocaldarius
-
-
-

Purification (Commentary)

Purification (Comment) Organism
maltose binding protein MalE Alicyclobacillus acidocaldarius

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + maltose/out
-
 Alicyclobacillus acidocaldarius ADP + phosphate + maltose/in
-
 ?