This enzyme catalyzes two phosphoryl transfer reactions as follows: (A) Transfer of phosphoryl group from hydroxyl group of Ser116 to 6-OH of glucose-1-phosphate, forming glucose-1,6-diphosphate: (B) Transfer of phosphoryl group from 1-OH of a glucose-1,6-diphosphate intermediate to Ser:
Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3
ASP 287;ASP 289;ASP 291(Magnesium binding)
ASP 308;ASP 310;ASP 312(Magnesium binding)
Functional diversity of the phosphoglucomutase superfamily: structural implications.
Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors.
Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase.
A tryptic peptide containing a unique serine phosphate residue in rabbit phosphoglucomutase.
Cobalt (II) and nickel (II) complexes of phosphoglucomutase.
Mechanism of action of rabbit muscle phosphoglucomutase. Rate of enzyme phosphate turnover studied with a rapid mixing technique.
The structure determination of rabbit phosphoglucomutase.
The structure of rabbit muscle phosphoglucomutase at intermediate resolution.
Mechanism-based inactivation of rabbit muscle phosphoglucomutase by nojirimycin 6-phosphate.
Removal of salt from a salt-induced protein crystal without cross-linking. Preliminary examination of "desalted" crystals of phosphoglucomutase by X-ray crystallography at low temperature.
Formation of substrate and transition-state analogue complexes in crystals of phosphoglucomutase after removing the crystallization salt.
Binding energy and catalysis: deoxyfluoro sugars as probes of hydrogen bonding in phosphoglucomutase.
19F NMR investigations of the catalytic mechanism of phosphoglucomutase using fluorinated substrates and inhibitors.
The crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution.
Structural changes at the metal ion binding site during the phosphoglucomutase reaction.
Reaction of the isosteric methylenephosphonate analog of alpha-D-glucose 1-phosphate with phosphoglucomutase. Induced-fit specificity revisited.
Structure of rabbit muscle phosphoglucomutase refined at 2.4-A
Crystal structure analysis of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase), from Paramecium reveals significant conformational variability.
Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.