EC Number   |
Protein Variants |
Reference |
|---|
   2.4.1.7 | A498H |
site-directed mutagenesis, the mutant shows reduced activity and thermostability compared to the wild-type enzyme |
720963 |
| 2.4.1.7 | D196A |
inactive mutant enzyme. External azide partly complements the catalytic defect in D196A while formate, acetate and halides can not restore activity. The mutant utilizes azide to convert alpha-D-glucose 1-phosphate into beta-D-glucose 1-azide, reflecting a change in stereochemical course of glucosyl transfer from alpha-retaining in wild-type to inverting in D196A. Phosphorolysis of beta-D-glucose 1-azide by D196A occurrs through a ternary complex kinetic mechanism, in contrast to the wild-type whose reactions feature a common glucosyl enzyme intermediate and ping-pong kinetics |
679829 |
| 2.4.1.7 | D196A |
site-directed mutagenesis, the purified D196A mutant shows 40% reduced activity compared to the wild-type in phosphorolysis and synthesis of sucrose as well as arsenolysis of alpha-glucose 1-phosphate, however, with azide as an alternative nucleophile, the conversion of alpha-glucose 1-phosphate proceeds at a slow rate and results in the formation of product glucose 1-azide with a beta-anomeric configuration, activity enhancement in the D196A mutant results from the direct participation of azide in the now inverting, single displacement-like mechanism of glucosyl transfer, overview |
685965 |
| 2.4.1.7 | D196N/E237Q |
the mutation affects the the stereoselectivity of the reaction |
703198 |
| 2.4.1.7 | D249G |
mutation contributes to the enhancement of thermal stability, mutant enzyme retains activity after heat treatment at 55°C for 20 min |
680405 |
| 2.4.1.7 | D295E |
mutation decreases the catalytic center activity of sucrose phosphorylase to about 0.01% of the wild-type level. The 100000fold preference of the wild-type for glucosyl transfer compared with mannosyl transfer from phosphate to fructose is lost |
679850 |
| 2.4.1.7 | D295E |
site-directed mutagenesis of the catalytic residue, the mutant shows about 0.01% of the wild-type enzyme activity, the preference of the wild-type enzyme for glucosyl transfer compared with mannosyl transfer from phosphate to fructose is lost in the mutant enzyme |
679850 |
| 2.4.1.7 | D295E |
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme |
-, 702848 |
| 2.4.1.7 | D295N |
mutation decreases the catalytic center activity of sucrose phosphorylase to about 0.01% of the wild-type level. Glucosylation and deglucosylation steps are affected uniformly, and independently of leaving group ability and nucleophilic reactivity of the substrate, respectively. The 100000fold preference of the wild-type for glucosyl transfer compared with mannosyl transfer from phosphate to fructose is lost |
679850 |
| 2.4.1.7 | D295N |
site-directed mutagenesis of the catalytic residue, the mutant shows about 0.01% of the wild-type enzyme activity, the preference of the wild-type enzyme for glucosyl transfer compared with mannosyl transfer from phosphate to fructose is lost in the mutant enzyme |
679850 |
