EC Number   |
General Information |
Reference |
|---|
   2.7.1.211 | metabolism |
the enzyme is responsible for transporting the extracellular sucrose into the cell |
761831 |
| 2.7.1.211 | physiological function |
a mutant lacking sucrose phosphotransferase activity retains phosphotransferase activity for glucose, fructose, mannose, mannitol, sorbitol, lactose, and maltose |
738363 |
| 2.7.1.211 | physiological function |
deletion of repressor TreR enables uptake of sucrose via TreB, an enzyme II protein required for phoshotransferase mediated uptake of trehalose. Once inside the cell, this sucrose is not processed by the TreC hydrolase, nor is it sufficient for growth of the strain. Levels of cscA (invertase) transcript increase in the treR mutant relative to the wild-type strain when grown under low sucrose conditions |
-, 737143 |
| 2.7.1.211 | physiological function |
distinct enzymes II for sucrose and glucose transport exist in Streptococcus mutans. Two integral membrane proteins, enzyme IIScr and enzyme IIG1c, each specific for its sugar substrate, sucrose or glucose, catalyze specific sugar:sugar-phosphate exchange reactions |
-, 738364 |
| 2.7.1.211 | physiological function |
gene disruption does not result in a recognizable phenotype |
739075 |
| 2.7.1.211 | physiological function |
loss of phosphotransferase ScrA activity leads to growth stimulation on fructooligosaccharides, due in large part to increased expression of the fruAB (fructanase) operon. ScrA is required for activation of levD expression (a component of fructose/mannose-PTS EII permease) by sucrose through components of the LevQRST complex, but not for activation by the cognate LevQRST sugars fructose or mannose. Sucrose-dependent catabolite repression is also evident in strains containing an intact sucrose phosphotransferase system |
-, 738525 |
| 2.7.1.211 | physiological function |
the sucrose permease lacks a sucrose-specific Enzyme III-like domain or a separate, soluble IIIScr protein. Enzyme IIScr is capable of utilizing the enzyme IIIGlc-like domain of the glucose permease. The IIIGlc-like domain therefore is an autonomous structural unit that assumes a conformation independent of the hydrophobic, N-terminal intramembranal domain of Enzyme IIGlc. Addition of the purified IIIGlc-like domain strongly stimulates the phosphorylation of sucrose, but not that of glucose, in phosphorylation assays that contain the two sugars simultaneously |
738560 |
| 2.7.1.211 | physiological function |
the sucrose phosphotransferase system of Streptococcus mutans is independent of regulatory enzyme III |
-, 738492 |
