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SRE0069

Sigma-Aldrich

Phosphoglucomutase from rabbit muscle

Sinónimos:

α-D-Glucose-1,6-bisphosphatase, α-D-Glucose-1-phosphate phosphotransferase

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About This Item

Número de CAS:
9001-81-4
Comisión internacional de enzimas:
5.4.2.2 (BRENDA, IUBMB)
MDL number:
MFCD00131886
UNSPSC Code:
12352204
NACRES:
NA.32

form

lyophilized powder

Quality Level

200

specific activity

≥100 units/mg protein

foreign activity

Lactic dehydroenase ≤0.5%
Phosphoglucose Isomerase ≤0.01%
pyruvate kinase ≤0.05%

shipped in

wet ice

storage temp.

−20°C

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General description

Research area: CellSignalling. The phosphoglucomutase (PGM) molecule, a single polypeptide chain, is made up of four α/β domains. The domains form a compact heart-shaped structure with a large fissure between the two lobes, and the molecule comprises about 40 secondary structural components. The active enzymatic site of the molecule is located at the bottom of the crevice on the surface of domain I. Rabbit muscle phosphoglucomutase (RB-PGM) is a monomer with a unique four-domain architecture.

Application

Phosphoglucomutase from rabbit muscle may be used in dephosphorylation to investigate the hexose bisphosphate activation of phosphoglucomutase.

Biochem/physiol Actions

Phosphoglucomutase (PGM) mainly catalyzes the interconversion of glucose 1-phosphate and glucose 6-phosphate via a glucose 1,6-diphosphate intermediate. Hence it plays a key role in glycolysis and gluconeogenesis.

Unit Definition

One unit will convert 1.0 μmole of α-D-glucose 1-phosphate to α-D-glucose 6-phosphate per min at pH 7.4 at 30 °C.

Physical form

Lyophilized powder containing Tris HCl, EDTA, magnesium acetate and carbohydrate

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

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C M Galloway et al.
Plant physiology, 79(3), 920-922 (1985-11-01)
The hexose bisphosphate activation of phosphoglucomutase was investigated with both plant (pea and mung bean) and animal (rabbit muscle) sources of the enzyme. Plant phosphoglucomutase was purified about 50-fold from seeds, and to a lesser extent, from seedlings of Pisum
S Levin et al.
Protein engineering, 12(9), 737-746 (1999-10-03)
Three-dimensional structural models of three members of the phosphoglucomutase (PGM) superfamily, parafusin, phosphoglucomutase-related protein and sarcoplasmic reticulum phosphoglucomutase, were constructed by homology modeling based on the known crystal structure of rabbit muscle phosphoglucomutase. Parafusin, phosphoglucomutase-related protein and sarcoplasmic reticulum phosphoglucomutase

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