<p>Enzymes actuate catalysis through a combination of transition state stabilization and ground state destabilization, inducing enantioselectivity through chiral binding sites. Here, we present a supramolecular model system that employs these basic principles to catalyze the enantiomerization of [5]helicene. Catalysis is hereby mediated not through a network of functional groups but through π-π catalysis exerted from the curved aromatic framework of a chiral perylene bisimide (PBI) cyclophane offering a binding pocket that is intricately complementary with the enantiomerization transition structure. Although transition state stabilization originates simply from dispersion and electrostatic interactions, enantiomerization kinetics are accelerated by a factor of ca. 700 at 295 K. Comparison with the mesocongener of the catalytically active cyclophane shows that upon configurational inversion in only one PBI moiety the catalytic effect is lost, highlighting the importance of precise transition structure recognition in supramolecular enzyme mimics. </p>