EC Number   |
General Information |
Reference |
|---|
   7.5.2.1 | evolution |
the enzyme is a member of the ATP-binding cassette superfamily |
719904 |
| 7.5.2.1 | malfunction |
a series of spontaneous mutants of Lactococcus lactis IL1403 show average 6 to 11fold lowered sensitivities to the circular bacteriocin garvicin ML and also changes in carbohydrate metabolism, specifically loss of the ability to metabolize starch and maltose, overview. Complementation of the mutants with genes malEFG recovers normal sensitivity to the bacteriocin |
-, 718597 |
| 7.5.2.1 | malfunction |
the addition of ATP and EDTA (to trigger the outwardfacing conformation) to the MBP-MalFGK2 system in the absence of maltose increases the mobility of W62C-SL in the MalG-DELTAscoop system but decreases it in the wild-type |
719904 |
| 7.5.2.1 | metabolism |
the maltose ABC transporter is carbon catabolite repression-regulated |
-, 718597 |
| 7.5.2.1 | metabolism |
the maltose transporter MalFGK2, together with the substrate-binding protein MalE, is a ABC transporter. MalE is bound in the periplasm with high-affinity to MalFGK2 to facilitate the acquisition of maltose. When the maltose concentration exceeds the transport capacity, MalE captures maltose and dissociates from the transporte, from the transporter past a threshold maltose concentration, in vivo, mechanism, overview. Maltose is both substrate and regulator of its own transporter, i.e. a homotropic regulator |
720859 |
| 7.5.2.1 | metabolism |
the type I maltose ABC importer is encoded within the maltose regulon, which enables the bacteria to feed on maltose and maltodextrins, alpha-1,4-linked oligosaccharides up to seven glucose units, formed by enzymatic cleavage of starch or glycogen |
713059 |
| 7.5.2.1 | metabolism |
the type I maltose ABC importer is encoded within the maltose regulon, which enables the bacteria to feed on maltose and maltodextrins, alpha-1,4-linked oligosaccharides up to seven glucose units, formed by enzymatic cleavage of starch or glycogen. The C-terminal domain of MalK has a dual regulatory function: it controls the activity of MalT, the positive transcriptional regulator of the maltose regulon, and it is the primary site at which dephosphorylated enzyme IIAGlc of the phosphoenolpyruvate phosphotransferase system binds, preventing maltose uptake |
713059 |
| 7.5.2.1 | more |
a malEFG-a deletion mutant is unable to grow in a minimal medium with maltose as sole carbon source and produce avermectin. Maltose utilization and avermectin production are restored by introduction of a single copy of malEFG-a. Overexpression of malEFG-a improves the utilization rate of starch, and thereby enhances avermectin production |
-, 711498 |
| 7.5.2.1 | more |
in the absence of MBP, MalFGK2 forms an inwardfacing conformation with the transmembrane-maltose-binding site exposed to the cytoplasm |
721055 |
| 7.5.2.1 | more |
substrate transport model for MalFGK2 |
720017 |
