EC Number |
Reaction |
Reference |
---|
3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides |
- |
- |
3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides |
catalytic mechanism, structure-function relationship |
683926 |
3.4.21.26 | 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 |
683337 |
3.4.21.26 | 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 |
683926 |
3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides |
catalytic residues are Ser477, Asp559, and His591 |
683690 |
3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides |
catalytic triad consists of Ser548-Asp631-His667 |
667500 |
3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides |
the catalytic triad is formed by conserved residues Ser548, Asp631, and His667 |
683369 |
3.4.21.26 | 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 |
683344 |
3.4.21.26 | 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 |
683389 |