EC Number   |
Protein Variants |
Reference |
|---|
   7.5.2.1 | C40S/S83C |
site-directed mutagenesis, the mutant shows altered subunit interactions in the maltose ABC transporter MALFGK2-E |
698908 |
| 7.5.2.1 | D123A |
the mutant shows wild type activity |
-, 749334 |
| 7.5.2.1 | D380G |
substitution of aspartate for glycine in the maltose-binding site of MalF likely generates a futile cycle by preventing maltose from binding to MalFGK2 during the catalytic cycle |
719904 |
| 7.5.2.1 | E120A |
the mutant shows strongly reduced activity compared to the wild type enzyme |
-, 749334 |
| 7.5.2.1 | E120A/D123A/E167A |
the mutations eliminate uphill maltose transport |
749334 |
| 7.5.2.1 | E120N/D123N/E167N |
the mutations eliminate uphill maltose transport |
749334 |
| 7.5.2.1 | E120Q |
the mutant shows reduced activity compared to the wild type enzyme |
-, 749334 |
| 7.5.2.1 | E120Q/D123Q/E167Q |
the mutations eliminate uphill maltose transport |
749334 |
| 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 |
713059 |
| 7.5.2.1 | E159Q |
the transporter containing the MalK-E159Q mutation is defective in ATP hydrolysis |
719904 |
