EC Number   |
Reaction |
Reference |
|---|
    3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 |
enzyme-activator and enzyme-inhibitor complex have strucutral differences that also differ from ternary complex enzyme-activator-inhibitor. The occupation of the active site generates structural perturbations which extend to the other subunits, resulting in predominance of the R over the T forms in the population of deaminase hexamers |
667624 |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 |
formerly EC 5.3.1.10. Isomerization of the aldose-ketose type converts the -CH(-NH2)-CH=O group of D-glucosamine 6-phosphate into -C(=NH)-CH2-OH, forming 2-deoxy-2-imino-D-arabino-hexitol, which then hydrolyses to yield fructose 6-phosphate and ammonia. N-acetyl-D-glucosamine 6-phosphate, which is not broken down, activates the enzyme |
- |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 |
His143 has many functional roles in the active site of enzyme |
648239 |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 |
reaction mechanism involves a ring-opening step, followed by an enolization step that proceeds through a cis-enolamine and its tautomeric imine as reaction intermediates |
648221 |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 |
residue R172 has a specific role in binding the substrate to the enzyme in the T state |
667318 |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 |
the mechanism comprises steps to open the pyranose ring of the substrate and a sequence of general base-catalyzed reactions to bring about isomerization and deamination, with Asp72 playing a key role as a proton exchanger |
648229 |
| 3.5.99.6 | alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 |
thermodynamic study, the allosteric behavior of enzyme can be described by the Monod-Wyman-Changeux model |
648243 |
