EC Number   |
Reaction |
Reference |
|---|
    5.3.1.1 | D-Glyceraldehyde 3-phosphate = glycerone phosphate |
in situ magnetic resonance probes of the enzyme-bound substrates to test the question of whether the equilibrium concentrations are perturbed by the enzyme. In the exergonic conversion of glycerinaldehyde 3-phosphate to dihydroxyacetone phosphate the high discrimination against solvent isotope uptake is consistent with chemistry protected by a water-tight active-site loop, therefore introducing asymmetry into the reversible reaction |
682559 |
| 5.3.1.1 | D-Glyceraldehyde 3-phosphate = glycerone phosphate |
intrinsic binding energy of the substrate phosphodianion group is utilized to drive closing of the mobile loop and a protein conformational change that leads to formation of an active site environment that is optimally organized for stabilization of the transition state for proton transfer from R-carbonyl carbon |
678283 |
| 5.3.1.1 | D-Glyceraldehyde 3-phosphate = glycerone phosphate |
mechanism |
2580 |
| 5.3.1.1 | D-Glyceraldehyde 3-phosphate = glycerone phosphate |
reaction mechanism via enediolate intermediate through proton abstraction by the catalytic base Glu167, overview |
706663 |
| 5.3.1.1 | D-Glyceraldehyde 3-phosphate = glycerone phosphate |
the active site of free enzyme, which has an open conformation needed to allow substrate binding, adopts a closed conformation at the enediolate-complex intermediate where the catalytic side chain is sequestered from interaction with imidazole dissolved in D2O |
694517 |
| 5.3.1.1 | D-Glyceraldehyde 3-phosphate = glycerone phosphate |
upon binding of ligand, the side chain of Glu167 flips from the inactive swung-out to the active swung-in conformation. A concerted movement of loop 6 and loop 7 from unliganded-open to liganded-closed is facilitated by the interactions of the phosphate moiety with loop 7. Rotation of the Gly211-Gly212 peptide plane of 90° is involved in this concerted movement |
678177 |
