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 36 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.2.23D17E site-directed mutagensis, increased activity -, 650103
Display the word mapDisplay the reaction diagram Show all sequences 3.1.2.23D17N site-directed mutagensis, highly reduced activity -, 650103
Display the word mapDisplay the reaction diagram Show all sequences 3.1.2.23D17N site-directed mutagensis, role of Asp17 in ligand binding -, 652279
Display the word mapDisplay the reaction diagram Show all sequences 3.1.2.23D17S site-directed mutagensis, highly reduced activity -, 650103
Display the word mapDisplay the reaction diagram Show all sequences 3.1.2.23D31A steady-state kinetic analysis 729220
Display the word mapDisplay the reaction diagram Show all sequences 3.1.2.23D31N steady-state kinetic analysis 729220
Display the word mapDisplay the reaction diagram Show all sequences 3.1.2.23E73A steady-state kinetic analysis, crystallization data -, 729220
Display the word mapDisplay the reaction diagram Show all sequences 3.1.2.23E73D mutation switches the function of the carboxylate residue from nucleophilic catalysis to base catalysis and thus, the reaction from a two-step process involving a covalent enzyme intermediate to a single-step hydrolysis reaction 729220
Display the word mapDisplay the reaction diagram Show all sequences 3.1.2.23E73D steady-state kinetic analysis 729220
Display the word mapDisplay the reaction diagram Show all sequences 3.1.2.23E73D/T77A mutant regains most of the catalytic efficiency lost in the E73D single mutant 729220
Results 1 - 10 of 36 > >>