EC Number   |
Reaction |
Reference |
|---|
    5.3.1.9 | alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate |
- |
- |
| 5.3.1.9 | alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate |
cis-endiol intermediate based mechanism with Glu97 acting as the catalytic base responsible for isomerization |
681378 |
| 5.3.1.9 | alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate |
in hydride shift mechanism of catalysis Fe2+ is responsible for proton transfer between O1 and O2, and the hydride shift between C1 and C2 is favored by a markedly hydrophobic environment in the active site. The absence of any obvious enzymatic machinery for catalyzing ring opening of the sugar substrates suggests that the pyrococcal enzyme has a preference for straight chain substrates |
722637 |
| 5.3.1.9 | alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate |
mechanism is based on an enediol intermediate |
662637 |
| 5.3.1.9 | alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate |
multistep catalytic mechanism, model including catalytically active amino acids |
663346 |
| 5.3.1.9 | alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate |
on the basis of the calculations and simulations, a zwitterionic intermediate mechanism for the low-energy enzymatic reaction is proposed, involving both proton and hydride transfers |
722445 |
| 5.3.1.9 | alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate |
push-pull mechanism of ring opening in which H388 breaks the O5-C1 bond by donating a proton, and simultaneously, K518 abstracts a proton from the C1 hydroxyl group |
662633 |
