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P4109

Sigma-Aldrich

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

Enzyme Commission number:
5.4.2.6 (BRENDA, IUBMB)
MDL number:
MFCD03456280
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

200

form

solid

specific activity

≥10 unit/mg solid

storage temp.

−20°C

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.

Unit Definition

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.

Other Notes

Contains EDTA and lactose.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

PRTR

Class I Designated Chemical Substances

ISHL Indicated Name

Substances Subject to be Indicated Names

ISHL Notified Names

Substances Subject to be Notified Names

JAN Code

P4109-BULK:
P4109-VAR:
P4109-250UN:
P4109-1000UN:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
OCULAR HISTOPATHOLOGY IN GENERALIZED GLYCOGENOSIS (POMEPE'S DISEASE).
D TOUSSAINT et al.
Archives of ophthalmology (Chicago, Ill. : 1960), 73, 342-349 (1965-03-01)
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