EC Number   |
Protein Variants |
Reference |
|---|
    3.2.1.21 | A375P |
Km (2-nitrophenyl beta-D-glucopyranoside) decreased compared to wild-type, kcat (2-nitrophenyl beta-D-glucopyranoside) decreased. Relative efficacy toward (2-nitrophenyl beta-D-glucopyranoside) similar to wild-type. Km (dhurrin) similar to wild-type, kcat drastically decreased |
722632 |
| 3.2.1.21 | A433V |
random mutagenesis, identification of the thermostable mutant, kinetics in comparison to the wild-type enzyme |
663625 |
| 3.2.1.21 | C174V |
contrary to uncompetitive inhibition of wild-type by glucose, mutant is competitively inhibited |
-, 746364 |
| 3.2.1.21 | D206N |
catalytically active mutant enzyme, similar temperature optimum like wild-type enzyme. The high-catalytic turn-over rate by D206N for beta-glucosidase activity makes it a useful enzyme in cellulose degradation at high temperatures |
750443 |
| 3.2.1.21 | D206Q |
mutant enzyme shows less than 10% hydrolytic activity than the wild-type toward 4-nitrophenyl glycosides |
750443 |
| 3.2.1.21 | D229N |
site-directed mutagenesis, mutation of the isozyme BGL1A residue from subsite +1 to the correspondent residue of isozyme BGL1B, the mutant shows decreased catalytic efficiency compared to the wild-type BGL1A |
678852 |
| 3.2.1.21 | D229N/K253A |
site-directed mutagenesis, mutation of the isozyme BGL1A residues from subsite +1 to the correspondent residues of isozyme BGL1B, the double mutant has a hydrolytic activity at neutral pH that is restored to that of the wild-type enzyme |
678852 |
| 3.2.1.21 | D242G |
mutant loses 96% of wild-type activity, activity is partially restored after addition of NaN3 |
715909 |
| 3.2.1.21 | D261N |
the D261N substitution leads to a drastic decrease in relative efficiency of ZmGlu1 on all substrates tested, but little effect on the Km |
722632 |
| 3.2.1.21 | D270A |
nucleophile mutant, crystallization data |
-, 760014 |
