EC Number   |
Protein Variants |
Reference |
|---|
    2.2.1.2 | D17A |
lower specific activity than wild-type |
486044 |
| 2.2.1.2 | E60Q/F132Y |
the mutant enzyme has no transaldolase activity and shows D-fructose 6-phosphate aldolase activity |
756034 |
| 2.2.1.2 | E96A |
lower specific activity than wild-type |
486044 |
| 2.2.1.2 | E96Q |
the mutant enzyme with reduced transaldolase activity is irreversibly inhibited by D-tagatose 6-phosphate |
755719 |
| 2.2.1.2 | E96Q/F178Y |
the mutant enzyme is irreversibly inhibited by D-tagatose 6-phosphate |
755719 |
| 2.2.1.2 | F132Y |
the mutant enzyme has no transaldolase activity and shows D-fructose 6-phosphate aldolase activity |
756034 |
| 2.2.1.2 | F178E |
mutant is able to catalyze aldol reactions and readily accepts hihydroxypropanone and hydroxypropanone |
719298 |
| 2.2.1.2 | F178E/S176A |
improved acceptance of substrate hydroxypropanone compared with mutant F178E |
719298 |
| 2.2.1.2 | F178Y |
by screening of library of proteins bearing a mutation in the active site mutant protein F178Y is found to be able to synthesize fructose 6-phosphate from dihydroxyacetone and glyceraldehyde 3-phosphate. Mutant is not only able to transfer a dihydroxyacetone moiety from a ketose donor, fructose 6-phosphate, onto an aldehyde acceptor, erythrose 4-phosphate, but to use it as a substrate directly in an aldolase reaction. Mutant fructose 6-phosphate aldolase activity is increased considerably above 70fold compared to wild-type. Structural studies of the wild-type and mutant protein suggest that this is due to a different H-bond pattern in the active site leading to a destabilization of the Schiff base intermediate |
687768 |
| 2.2.1.2 | F178Y |
reaction fructose 6-phosphate synthesis from dihydroxyacetone and glyceraldehyde 3-phosphate: Km (mM): 30 (dihydroxyacetone), kcat (1/sec): 4.3 (dihydroxyacetone). Reaction fructose 6-phosphate cleavage into dihydroxyacetone and glyceraldehyde 3-phosphate: Km (mM) 1.5 (fructose 6-phosphate), kcat (1/sec): 0.22 (fructose 6-phosphate). Reaction: sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate formation from erythrose 4-phosphate + D-fructose 6-phosphate: Km (mM): 22 (fructose 6-phosphate), kcat (1/sec): 8.8 |
687768 |
