White to light yellow solid
Phosphoglucomutase from rabbit muscle may be used in dephosphorylation to investigate the hexose bisphosphate activation of phosphoglucomutase.
Phosphoglucomutase exchanges a phosphoryl group with the substrate.
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 unique four-domain architecture.
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.
