Activating Compound | Comment | Organism | Structure |
---|---|---|---|
MalE | MalE and maltose together stimulate the ATPase activity of the enzyme. MalE stabilizes the enzyme in the outward-facing conformation | Escherichia coli | |
maltose | MalE and maltose together stimulate the ATPase activity of the enzyme. Maltose triggers return to the inward-facing state for substrate and Pi release | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.232 | - |
ATP | at pH 7.5 and 37°C | Escherichia coli | |
0.274 | - |
ATP | in the presence of MalE, at pH 7.5 and 37°C | Escherichia coli | |
0.283 | - |
ATP | in the presence of MalE and maltose, at pH 7.5 and 37°C | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + maltose-[maltose-binding protein][side 1] | Escherichia coli | - |
ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + maltose-[maltose-binding protein][side 1] | - |
Escherichia coli | ADP + phosphate + maltose[side 2] + [maltose-binding protein][side 1] | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MalFGK2 | - |
Escherichia coli |
maltose ABC transporter | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.3 | - |
ATP | at pH 7.5 and 37°C | Escherichia coli | |
1.2 | - |
ATP | in the presence of MalE, at pH 7.5 and 37°C | Escherichia coli | |
7.8 | - |
ATP | in the presence of MalE and maltose, at pH 7.5 and 37°C | Escherichia coli |