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In the case of another dipeptidyl peptidase, dipeptidyl peptidase IV (clan SC, family S9), in which a catalytic / hydrolase fold is covered by a regulatory -propeller domain, the N-terminus of the substrate is held precisely in position by strong interactions with the side chains of a double Glu motif (Glu205-Glu206) from an insertion helix of the regulatory -propeller domain 14,16 (Fig

The result is low energy and fatigue 3, 4