EC Number   |
Reaction |
Reference |
|---|
    5.4.2.2 | alpha-D-glucose 1-phosphate = D-glucose 6-phosphate |
acid-base catalysis mechanism, key role for conformational change in its multistep reaction, which requires a dramatic 180 degree reorientation of the intermediate within the active site. Modeling shows that increased enzyme flexibility facilitates the reorientation of the reaction intermediate, coupling changes in structural dynamics with the unique catalytic mechanism of this enzyme |
727988 |
| 5.4.2.2 | alpha-D-glucose 1-phosphate = D-glucose 6-phosphate |
acid-base catalysis mechanism, overview. His329 is appropriately positioned to abstract a proton from the O1/O6 hydroxyl of the phosphosugar substrates, and thus may serve as the general base in the reaction |
727479 |
| 5.4.2.2 | alpha-D-glucose 1-phosphate = D-glucose 6-phosphate |
in the forward reaction a phosphate from the enzyme is transferred to C-6 of glucose 1-phosphate which results in a dephosphoenzyme intermediate. In the second step phosphate from the C-1 of glucose is transferred to the enzyme for its regeneration. The reverse reaction proceeds via a similar mechanism |
3281 |
| 5.4.2.2 | alpha-D-glucose 1-phosphate = D-glucose 6-phosphate |
ping-pong mechanism |
3295 |
| 5.4.2.2 | alpha-D-glucose 1-phosphate = D-glucose 6-phosphate |
reaction sequence |
3214 |
