TY  - JOUR
AU  - Perez-Garcia, Pablo
AU  - Chow, Jennifer
AU  - Costanzi, Elisa
AU  - Gurschke, Marno
AU  - Dittrich, Jonas
AU  - Dierkes, Robert F.
AU  - Molitor, Rebecka
AU  - Applegate, Violetta
AU  - Feuerriegel, Golo
AU  - Tete, Prince
AU  - Danso, Dominik
AU  - Thies, Stephan
AU  - Schumacher, Julia
AU  - Pfleger, Christopher
AU  - Jaeger, Karl-Erich
AU  - Gohlke, Holger
AU  - Smits, Sander H. J.
AU  - Schmitz, Ruth A.
AU  - Streit, Wolfgang R.
TI  - An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate
JO  - Communications chemistry
VL  - 6
IS  - 1
SN  - 2399-3669
CY  - [London]
PB  - Macmillan Publishers Limited, part of Springer Nature
M1  - FZJ-2023-03512
SP  - 193
PY  - 2023
AB  - Polyethylene terephthalate (PET) is a commodity polymer known to globally contaminate marine and terrestrial environments. Today, around 80 bacterial and fungal PET-active enzymes (PETases) are known, originating from four bacterial and two fungal phyla. In contrast, no archaeal enzyme had been identified to degrade PET. Here we report on the structural and biochemical characterization of PET46 (RLI42440.1), an archaeal promiscuous feruloyl esterase exhibiting degradation activity on semi-crystalline PET powder comparable to IsPETase and LCC (wildtypes), and higher activity on bis-, and mono-(2-hydroxyethyl) terephthalate (BHET and MHET). The enzyme, found by a sequence-based metagenome search, is derived from a non-cultivated, deep-sea Candidatus Bathyarchaeota archaeon. Biochemical characterization demonstrated that PET46 is a promiscuous, heat-adapted hydrolase. Its crystal structure was solved at a resolution of 1.71 Å. It shares the core alpha/beta-hydrolase fold with bacterial PETases, but contains a unique lid common in feruloyl esterases, which is involved in substrate binding. Thus, our study widens the currently known diversity of PET-hydrolyzing enzymes, by demonstrating PET depolymerization by a plant cell wall-degrading esterase.
LB  - PUB:(DE-HGF)16
C6  - 37697032
UR  - <Go to ISI:>//WOS:001066506600001
DO  - DOI:10.1038/s42004-023-00998-z
UR  - https://juser.fz-juelich.de/record/1014968
ER  -