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Results 1 - 9 of 9
EC Number
Reaction
Commentary
Reference
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
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Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship
Hydrolysis 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
Hydrolysis 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
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic residues are Ser477, Asp559, and His591
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic triad consists of Ser548-Asp631-His667
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad is formed by conserved residues Ser548, Asp631, and His667
Hydrolysis 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
Hydrolysis 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
Results 1 - 9 of 9