Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate

• DOI: 10.1038/s41467-019-09326-3
• Publication Date: 2019-04-12T10:02:59Z
• Authors: Gottfried J. Palm; Lukas Reisky; Dominique Böttcher; Henrik Müller; Emil A. P. Michels; Miriam C. Walczak; Leona Berndt; Manfred S. Weiss; Uwe T. Bornscheuer; Gert Weber
• Keywords: Hydrolase; Serine hydrolase

Abstract The extreme durability of polyethylene terephthalate (PET) debris has rendered it a long-term environmental burden. At the same time, current recycling efforts still lack sustainability. Two recently discovered bacterial enzymes that specifically degrade PET represent promising solution. First, Ideonella sakaiensis PETase, structurally well-characterized consensus α/β-hydrolase fold enzyme, converts to mono-(2-hydroxyethyl) (MHET). MHETase, second key hydrolyzes MHET educts and ethylene glycol. Here, we report crystal structures active ligand-free MHETase bound nonhydrolyzable analog. which is reminiscent feruloyl esterases, possesses classic domain lid conferring substrate specificity. In light structure-based mapping site, activity assays, mutagenesis studies first structure-guided alteration specificity towards bis-(2-hydroxyethyl) (BHET) reported here, anticipate be valuable resource further advance enzymatic plastic degradation.