EC Number |
General Information |
Reference |
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5.4.2.6 | malfunction |
deletion of pgmB affects known virulence factors of Streptococcus mutans, specifically acid tolerance, mutant strain MU1593 is defective in its acid-responsiveness. The DELTApgmB strain shows a decreased ability to survive acid challenge. Additionally, the strain lacking beta-phosphoglucomutase has a diminished glycolytic profile compared with the parental strain. Proton permeability is increased in strain MU1593. Deletion of pgmB has a negative impact on the virulence of Streptococcus mutans in the Galleria mellonella (greater wax worm) animal model. Phenotype of strain MU1593, overview |
-, 728265 |
5.4.2.6 | more |
fluoromagnesate and fluoroaluminate complexes of beta-phosphoglucomutase demonstrate the importance of charge balance in transition-state stabilization for phosphoryl transfer enzymes, overview |
728684 |
5.4.2.6 | more |
reaction mechanism analysis by docking techniques and QM/MM theoretical method, overview. Residues Ser114 and Lys145 and Mg2+ play important roles in stabilizing the large negative charge on the phosphate through strong coordination with the phosphate oxygens and guiding the phosphate group throughout the catalytic process |
728173 |
5.4.2.6 | physiological function |
the enzyme is involved in conversion of kojibiose into beta-D-glucose 6-phosphate, a substrate of the glycolytic pathway. Disaccharide utilization pathway via phosphorolysis in hyperthermophilic archaea |
-, 725294 |
5.4.2.6 | physiological function |
the enzyme is involved in the kojibiose catabolic pathway |
-, 725294 |
5.4.2.6 | physiological function |
The enzyme plays a role at the juncture of carbohydrate metabolism and virulence. beta-Phosphoglucomutase contributes to aciduricity in Streptococcus mutans |
-, 728265 |