5.4.2.6: beta-Phosphoglucomutase
This is an abbreviated version!
For detailed information about beta-Phosphoglucomutase, go to the full flat file.
Word Map on EC 5.4.2.6
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5.4.2.6
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1-phosphate
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lactis
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maltose
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phosphorane
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dehalogenase
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trehalose
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1,6-bisphosphate
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haloacid
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lactococci
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alpha-glucose
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analysis
- 5.4.2.6
- 1-phosphate
- lactis
- maltose
-
phosphorane
-
dehalogenase
- trehalose
- 1,6-bisphosphate
-
haloacid
-
lactococci
- alpha-glucose
- analysis
Reaction
Synonyms
beta-PGM, beta-phosphoglucomutase, betaPGM, PgcM, Phosphomutase, beta-glucose, PsPGM, Py04_1503, TM1254, YcjU
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General Information
General Information on EC 5.4.2.6 - beta-Phosphoglucomutase
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malfunction
physiological function
additional information
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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
malfunction
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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
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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
physiological function
the enzyme is involved in the kojibiose catabolic pathway
physiological function
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The enzyme plays a role at the juncture of carbohydrate metabolism and virulence. beta-Phosphoglucomutase contributes to aciduricity in Streptococcus mutans
physiological function
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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
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physiological function
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the enzyme is involved in the kojibiose catabolic pathway
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physiological function
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The enzyme plays a role at the juncture of carbohydrate metabolism and virulence. beta-Phosphoglucomutase contributes to aciduricity in Streptococcus mutans
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fluoromagnesate and fluoroaluminate complexes of beta-phosphoglucomutase demonstrate the importance of charge balance in transition-state stabilization for phosphoryl transfer enzymes, overview
additional information
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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