Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Protein Variants

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 26 > >>
EC Number Protein Variants Commentary Reference
Display the reaction diagram Show all sequences 3.2.1.B28A419T 159% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 109% with 4-nitrophenyl beta-D-galactoside, 53% residual activity after 1 h at 106°C 735663
Display the reaction diagram Show all sequences 3.2.1.B28E372D 200-fold reduction in specific activity 722489
Display the reaction diagram Show all sequences 3.2.1.B28E372Q 1000-fold reduction in specific activity 722489
Display the reaction diagram Show all sequences 3.2.1.B28E386G mutation in nucleophile residue E387, mutation completely abolishes activity under statndard conditions. The addition of 2 M sodium formate as an external nucleophile leads to the recovery of 8.40% activity with accumulation of oligosaccharides. At pH 3.0 and low concentrations of sodium formate buffer, the hyperthermophilic glycosynthase shows kcat values similar to those of the wild-type and 17fold higher than those observed at the usual reactivation conditions in 2 M sodium formate at pH 6.5 735665
Display the reaction diagram Show all sequences 3.2.1.B28E417S mutation in phosphate binding site, 5fold increase of the efficiency of hydrolyzing o-nitrophenol-beta-D-galactopyranoside-6-phosphate. Activity on nonphosphorylated sugars is largely reduced 326270
Display the reaction diagram Show all sequences 3.2.1.B28E417S/M424K/F426Y mutations in phosphate binding site, 3fold increase of the efficiency of hydrolyzing 2-nitrophenyl beta-D-galactopyranoside-6-phosphate. Activity on nonphosphorylated sugars is largely reduced 326270
Display the reaction diagram Show all sequences 3.2.1.B28F426Y mutant has lower activity than the wild-type enzyme, but provides a higher ratio of transglucosylation product to hydrolysis products compared to wild-type enzyme, 2.6fold increase. The mutant enzyme has higher selectivity over the wide range of temperatures tested 721888
Display the reaction diagram Show all sequences 3.2.1.B28F426Y mutation in phosphate binding site, results in an increased affinity for galactosides. Activity on nonphosphorylated sugars is largely reduced 326270
Display the reaction diagram Show all sequences 3.2.1.B28I161V 110% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 37% with 4-nitrophenyl beta-D-galactoside, 84% residual activity after 1 h at 106°C 735663
Display the reaction diagram Show all sequences 3.2.1.B28I67T 110% of wild-type activity with 4-nitrophenyl beta-D-glucoside, 97% with 4-nitrophenyl beta-D-galactoside, 100% residual activity after 1 h at 106°C 735663
Results 1 - 10 of 26 > >>