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 50 > >>
download as CSV
download all results as CSV
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.37A268T naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview 695221
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.37A268T naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview 695221
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.37C209A site-directed mutagenesis, mutant structure determination 690230
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.37C80S/C196S both the double and triple mutants show differing levels of disorder depending on their liganded state, with the level of disorder increasing when substrates are bound.The double mutant shows disorder over residues 177-180 in the unliganded and H-antigen bound forms, with disorder increasing to residues 176-185 for the UDP-, UDP + H-, and UDP-alpha-D-galactose + 3-deoxy-Gal inactive acceptor analog-bound structures. The double mutant has a reduction in Km for both donor and acceptor substrates. Mutation shows little effect over kcat 720246
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.37C80S/C196S/C209S both the double and triple mutants show differing levels of disorder depending on their liganded state, with the level of disorder increasing when substrates are bound.The unliganded triple mutant shows a nearly complete internal loop, with residues 176-181 disordered for the H-antigen-bound structure and 177-179 disordered for the UDP-bound structure. The UDP + H- and UDPGal + 3-deoxy-Gal inactive acceptor analog-bound structures of the triple mutant show an internal loop completely disordered over residues 176-184. The triple Cys-to-Ser mutant has an acceptor Km elevated approximately 5times over wild type, while the donor Km has doubled. Mutation shows little effect over kcat 720246
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.37D262N naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview 695221
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.37D262N naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview 695221
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.37D302A almost complete loss of activity 756890
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.37D302A/D316A strong decrease in kcat value 756890
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.37D302C kcat value is 9% that of wild-type GTB 756890
Results 1 - 10 of 50 > >>
download as CSV
download all results as CSV