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

BRENDA support

Refine search

Search Reaction

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 - 9 of 9
download as CSV
download all results as CSV
EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.26Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides - -
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.26Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides catalytic mechanism, structure-function relationship 683926
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.26Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview 683337
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.26Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides catalytic mechanism, structure-function relationship, the substrate induces an opening at the interface pf the peptidase and the beta-propeller domains while entering into the active site, concerted movements of the domains are required for enzyme activity 683926
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.26Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides catalytic residues are Ser477, Asp559, and His591 683690
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.26Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides catalytic triad consists of Ser548-Asp631-His667 667500
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.26Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides the catalytic triad is formed by conserved residues Ser548, Asp631, and His667 683369
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.26Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance 683344
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.26Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides the catalytic triad Ser554, Asp641, His680 is located at the C-terminus in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance, catalytic mechanism, structure-function relationship, overview 683389
Results 1 - 9 of 9
download as CSV
download all results as CSV