Next, we assessed whether the enzymes could accept both aliphatic and aromatic low molar mass substrates by combining wet-lab experiments and computational docking simulations. We used bis-(2-hydroxyethyl) terephthalate ( ) (EG-TPA-EG) and bis-(2-hydroxyethyl) adipate ( ) (EG-ADA-EG) (NMR data in SI, Fig. ) as model substrates because these are structurally similar to the targeted polyester polymers and therefore offer a simplified testbed for our studies. Although these experiments do not account for the restricted molecular accessibility typical of solid materials, they accurately reflect the enzyme's propensity for hydrolysis. Molecular docking simulations using either 8 or 9 as substrates revealed that both Tc_Cut2NV WCCG and LCC WCCG are receptors. Moreover, in the computational models showing the substrate in a productive binding pose, the catalytically active serine (S131 for Tc_Cut2NV WCCG or S165 for LCC WCCG ) was found to be in close proximity to the reactive carbon of the substrate's carbonyl group (<3 Å) (Fig. and SI, Fig. ).