The enzyme requires Mg2+ and phosphorylation of an aspartate residue at the active site. The enzyme is able to autophosphorylate itself with its substrate beta-D-glucose 1-phosphate. Although this is a slow reaction, only a single turnover is required for activation. Once the phosphorylated enzyme is formed, it generates the reaction intermediate beta-D-glucose 1,6-bisphosphate, which can be used to phosphorylate the enzyme in subsequent cycles . cf. EC 5.4.2.2, phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
a single Mg2+ coordination site accomodates water, phosphate, and the phosphorane intermediate during catalytic turnover. Bi-bi ping-pong mechanism, substrate induced-fit mechanism allows phosphomutase activity to dominate over the intrinsic phosphatase activity
phosphoryl transfer rather than ligand binding is rate-limiting. Beta-D-glucose 1,6-bisphosphate is a reaction intermediate and binds to the active site in two different orientations with roughly the same efficiency. Reorientation of the beta-D-glucose 1,6-bisphosphate intermediate occurs by diffusion into solvent followed by binding in the opposite orientation
reaction mechanism of the phosphoryl transfer starting from the bisphosphate intermediate beta-D-glucose-1,6-(bis)phosphate in both directions of the reversible reaction, overview. The calculated energy barrier of the reaction for the beta-D-glucose 1-phosphate to beta-D-glucose 1,6-diphosphate step is only slightly higher than for the beta-G1,6diP to beta-G6P step. Residues Ser114 and Lys145 and Mg2+ play important roles in stabilizing the large negative charge on the phosphate through strong coordination with the phosphate oxygens and guiding the phosphate group throughout the catalytic process
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SYSTEMATIC NAME
IUBMB Comments
beta-D-Glucose 1,6-phosphomutase
The enzyme requires Mg2+ and phosphorylation of an aspartate residue at the active site. The enzyme is able to autophosphorylate itself with its substrate beta-D-glucose 1-phosphate. Although this is a slow reaction, only a single turnover is required for activation. Once the phosphorylated enzyme is formed, it generates the reaction intermediate beta-D-glucose 1,6-bisphosphate, which can be used to phosphorylate the enzyme in subsequent cycles [4]. cf. EC 5.4.2.2, phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
formation of a MgF3- transition state analogue when glucose 6-phosphate, magnesium, and fluoride are present with the enzyme, in which MgF3- mimics the transferring PO3- moiety
fluoromagnesate and fluoroaluminate complexes of beta-phosphoglucomutase demonstrate the importance of charge balance in transition-state stabilization for phosphoryl transfer enzymes, overview
reaction mechanism analysis by docking techniques and QM/MM theoretical method, overview. Residues Ser114 and Lys145 and Mg2+ play important roles in stabilizing the large negative charge on the phosphate through strong coordination with the phosphate oxygens and guiding the phosphate group throughout the catalytic process
crystals of phosphorylated native beta-PGM are grown at pH 7.5 in the presence of 5 M Mg2+ using the vapor-diffusion method with hanging drop geometry, 100 mM ammonium fluoride and 16% polyethylene glycol 3350 are used as precipitating agents, crystals diffrakt to 2.3 A
beta-PGM is transferred to 1 mM HEPES, pH 7.5, 10 mM MgCl2 and 0.1 mM dithiothreitol, final beta-PGM concentration at 15 mg/ml, crystals are obtained from either 150 mM ammonium acetate, 100 mM trisodium citrate dihydrate, pH 4.5, 25% polyethylene glycol 4000 or 100 mM ammonium fluoride, 16% polyethylene glycol 3350 by hanging-drop vapor diffusion, crystals of selenium methionyl-substituted beta-PGM diffract to 2.3 A
purified recombinant enzyme in complex with transition-state analogue fluoromagnesate and glucose 6-phosphate or ground-state analogue fluoroaluminate and glucose 6-phosphate, sitting drop vapour diffusion method, mixing of 15 mg/mL 50 mM K+ HEPES, pH 7.2, 5 mM MgCl2, 1 mM azide, 0.1 mM DTT, 10 mM NH4F, and 10 mM BeCl2 1:1 with the precipitant containing 26-30% w/v PEG 4000, 200 mM Na acetate, and 100 mM Tris, pH 7.5, X-ray diffraction structure determination and analysis at 1.65 A resolution, molecular replacement