P4109
β-Phosphoglucomutase from Lactococcus sp.
recombinant, expressed in E. coli
Synonym(s):
β-D-Glucose 1,6-phosphomutase
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About This Item
Specific activity:
≥10 unit/mg solid
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
form
solid
specific activity
≥10 unit/mg solid
storage temp.
−20°C
Quality Level
Application
β-Phosphoglucomutase is used to study starch and sucrose metabolism. It is used for the determination of α-amylase in clinical analysis. It is used to study galactose utilization and generalized glycogenosis (Pompe′s Disease).
Biochem/physiol Actions
β-Phosphoglucomutase enzymatically converts β-D-glucose 1-phosphate to β-D-glucose 6-phosphate. It is involved in starch and sucrose metabolism.
Enzymatically converts β-D-glucose-1-phosphate to β-D-glucose-6-phosphate.
Other Notes
Contains EDTA and lactose.
One unit is defined as the amount of enzyme which converts 1μmol of β-D-glucose-1-phosphate to β-D-glucose-6-phosphate per minute at 37°C and pH 7.0.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Erika Pellegrini et al.
Acta crystallographica. Section D, Biological crystallography, 67(Pt 10), 902-906 (2011-09-21)
Over the last 20 years cryocrystallography has revolutionized the field of macromolecular crystallography, greatly reducing radiation damage and allowing the collection of complete data sets at synchrotron sources. However, in order to cool crystals to 100 K cryoprotective agents must usually
Jianying Dai et al.
Biochemistry, 45(25), 7818-7824 (2006-06-21)
Activated Lactococcus lactis beta-phosphoglucomutase (betaPGM) catalyzes the conversion of beta-d-glucose 1-phosphate (betaG1P) derived from maltose to beta-d-glucose 6-phosphate (G6P). Activation requires Mg(2+) binding and phosphorylation of the active site residue Asp8. Initial velocity techniques were used to define the steady-state
Joanna L Griffin et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(18), 6910-6915 (2012-04-17)
Experimental observations of fluoromagnesate and fluoroaluminate complexes of β-phosphoglucomutase (β-PGM) have demonstrated the importance of charge balance in transition-state stabilization for phosphoryl transfer enzymes. Here, direct observations of ground-state analog complexes of β-PGM involving trifluoroberyllate establish that when the geometry
Cecelia A Garcia et al.
Applied microbiology and biotechnology, 105(10), 4033-4052 (2021-05-08)
In a competitive microbial environment, nutrient acquisition is a major contributor to the survival of any individual bacterial species, and the ability to access uncommon energy sources can provide a fitness advantage. One set of soluble carbohydrates that have attracted
F Levander et al.
Applied and environmental microbiology, 67(6), 2734-2738 (2001-05-26)
To study the influence of phosphoglucomutase (PGM) activity on exopolysaccharide (EPS) synthesis in glucose- and lactose-growing Streptococcus thermophilus, a knockout PGM mutant and a strain with elevated PGM activity were constructed. The pgmA gene, encoding PGM in S. thermophilus LY03
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