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