EC Number   |
Reaction |
Reference |
|---|
   5.4.2.6 | beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate |
- |
- |
| 5.4.2.6 | beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate |
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 |
661214 |
| 5.4.2.6 | beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate |
mechanism is a nucleophilic substitution via an associative pathway, enzyme stablizes the phosphorane intermediate along that pathway |
661947 |
| 5.4.2.6 | beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate |
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 |
678202 |
| 5.4.2.6 | beta-D-Glucose 1-phosphate = beta-D-glucose 6-phosphate |
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 |
728173 |
