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

BRENDA support

Refine search

Search KM Value [mM]

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
Image of 2D Structure

Search term:

Results 1 - 7 of 7
download as CSV
download all results as CSV
EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.168-999 - more reaction kinetics, rutinoside transferase 753044
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.1681.77 - hesperidin pH 5.0, 60°C 701955
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.1681.8 - hesperidin free enzyme, pH 5.0, 60°C 716806
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.1688 - hesperidin immobilized enzyme, pH 5.0, 60°C, the change in the affinity of the enzyme to its substrate compared to the free enzyme is probably caused by structural changes introduced by the immobilization process and by the lower accessibility to the active site 716806
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.1688.7 - hesperidin methylchalcone free enzyme, pH 5.0, 60°C 716806
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.1688.73 - hesperidin methylchalcone pH 5.0, 60°C 701955
Display the word mapDisplay the reaction diagram Show all sequences 3.2.1.16838.7 - hesperidin methylchalcone immobilized enzyme, pH 5.0, 60°C, the change in the affinity of the enzyme to its substrate compared to the free enzyme is probably caused by structural changes introduced by the immobilization process and by the lower accessibility to the active site 716806
Results 1 - 7 of 7
download as CSV
download all results as CSV