Palm_2019_Nat.Commun_10_1717

Reference

Title : Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate - Palm_2019_Nat.Commun_10_1717
Author(s) : Palm GJ , Reisky L , Bottcher D , Muller H , Michels EAP , Walczak MC , Berndt L , Weiss MS , Bornscheuer UT , Weber G
Ref : Nat Commun , 10 :1717 , 2019
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 a promising solution. First, Ideonella sakaiensis PETase, a structurally well-characterized consensus alpha/beta-hydrolase fold enzyme, converts PET to mono-(2-hydroxyethyl) terephthalate (MHET). MHETase, the second key enzyme, hydrolyzes MHET to the PET educts terephthalate and ethylene glycol. Here, we report the crystal structures of active ligand-free MHETase and MHETase bound to a nonhydrolyzable MHET analog. MHETase, which is reminiscent of feruloyl esterases, possesses a classic alpha/beta-hydrolase domain and a lid domain conferring substrate specificity. In the light of structure-based mapping of the active site, activity assays, mutagenesis studies and a first structure-guided alteration of substrate specificity towards bis-(2-hydroxyethyl) terephthalate (BHET) reported here, we anticipate MHETase to be a valuable resource to further advance enzymatic plastic degradation.
ESTHER : Palm_2019_Nat.Commun_10_1717
PubMedSearch : Palm_2019_Nat.Commun_10_1717
PubMedID: 30979881
Gene_locus related to this paper: idesa-mheth

Related information

Gene_locus related to this paper: idesa-mheth

Citations formats

Palm GJ, Reisky L, Bottcher D, Muller H, Michels EAP, Walczak MC, Berndt L, Weiss MS, Bornscheuer UT, Weber G (2019)
Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate
Nat Commun 10 :1717

Palm GJ, Reisky L, Bottcher D, Muller H, Michels EAP, Walczak MC, Berndt L, Weiss MS, Bornscheuer UT, Weber G (2019)
Nat Commun 10 :1717