EC Number   |
General Information |
Reference |
|---|
    2.5.1.31 | malfunction |
naturally occurring mutation T86I confers resistance to bacitracin and scandium in Bacillus subtilis mutants |
-, 722551 |
| 2.5.1.31 | malfunction |
the uppS1 mutation increases resistance to vancomycin, fosfomycin, and D-cycloserine in wild-type cells, but this effect is greatly reduced or eliminated in a sigmaM mutant background. Incomplete inhibition of UppS function may lead to increased resistance to some cell wall-active antibiotics. Phenotype, overview |
-, 737459 |
| 2.5.1.31 | metabolism |
an essential enzyme in the biosynthesis of bacterial cell wall |
-, 759248 |
| 2.5.1.31 | metabolism |
essential enzyme in bacterial cell wall synthesis |
-, 759596 |
| 2.5.1.31 | metabolism |
essential enzyme in the biosynthesis of the bacterial cell wall |
-, 759096 |
| 2.5.1.31 | metabolism |
the enzyme is responsible for the biogenesis of undecaprenyl phosphate, an indispensable glycosyl carrier lipid in bacterial cell wall biosynthesis |
-, 759474 |
| 2.5.1.31 | more |
molecular docking and homology modeling of UPP synthase |
-, 738467 |
| 2.5.1.31 | more |
overexpression of the wild-type uppS gene results in increased susceptibilities to both scandium and bacitracin, which prevents cell wall synthesis by inhibiting the dephosphorylation of undecaprenyl diphosphate, in addition to enhanced amylase production. Accumulation of undecaprenyl diphosphate renders cells more susceptible to rare earth elements |
-, 722551 |
| 2.5.1.31 | physiological function |
bactoprenyl diphosphate (BPP), a two-E eight-Z configuration C55 isoprenoid, serves as a critical anchor for the biosynthesis of complex glycans central to bacterial survival and pathogenesis. BPP is formed by the polymerase undecaprenyl diphosphate synthase (UppS), which catalyzes the elongation of a single farnesyl diphosphate (FPP) with eight Z-configuration isoprene units from eight isopentenyl diphosphates |
-, 737698 |
| 2.5.1.31 | physiological function |
expression of UPPS in the yeast mutant rer2DELTA, lacking undecaprenyl diphosphate synthase, complements the growth and the hypoglycosylation of carboxypeptidase Y defects. Mutant cells expressing UPPS synthesize dolichyl phosphate of chain length C55 and utilize it to form Man-P-(55)Dol in vitro and in vivo, and they synthesize N-linked glycoprotein |
722345 |
