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
A tryptic peptide containing a unique serine phosphate residue in rabbit 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.
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.
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.
ASP 287;ASP 289;ASP 291(Magnesium binding)
ASP 308;ASP 310;ASP 312(Magnesium binding)