EC Number   |
Reaction |
Reference |
|---|
    5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate |
catalytic reaction mechanism |
661510 |
| 5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate |
catalytic reaction mechanism involving K369, K412, K373, and K489 |
652523 |
| 5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate |
catalytic reaction mechanism, induced-fit active site formation by substrate binding |
661510 |
| 5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate |
formation of 5-keto-D-glucose 6-phosphate as an enzyme-bound intermediate in the conversion of D-glucose 6-phosphate into 1L-myo-inositol 1-phosphate |
3681 |
| 5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate |
it is possible that the enzyme has an aldol step in the enzymatic pathway which is of neither classical aldolase type |
3690 |
| 5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate |
mechanism, the phosphate-bearing carbon-atom in D-glucose 6-phosphate is the same atom which bears the phosphate in L-myo-inositol-1-phosphate |
3678 |
| 5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate |
no upregulation of transcription by salinity stress |
3677 |
| 5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate |
ordered sequential mechanism with NAD+ adding first |
3694 |
| 5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate |
pro-S specificity of the first step, the reversible oxidation of glucose 6-phosphate to 5-ketoglucose 6-phosphate and in the second oxidation-reduction step, the reduction of myo-inosose-2 1-phosphate to myo-inositol 1-phosphate |
3709 |
| 5.5.1.4 | D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate |
reaction proceeds with stereospecific loss of the pro-6R and incorporation of the pro-6S hydrogen into the product. The ring closure thus occurs in a retention mode at C-6 of the substrate |
3713 |
