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Cited by 166

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Structural studies reveal the molecular mechanism of PET ase

Chen, Chun‐Chi, Han, Xu, Ko, Tzu‐Ping, Liu, Weidong, Guo, Rey‐Ting·2018·The FEBS Journal

Abstract

Poly(ethylene terephthalate) (PET) is a class of plastic material widely used in modern society, but large amounts of PET waste cause severe environmental problems. Obtained from a PET‐consuming bacterium Ideonella sakaiensis, the enzyme PET ase exhibits superb hydrolytic activity and substrate preference toward PET. Here, we summarize some recent advances in the crystallographic analysis of PET ase. These reports uncover structural features of PET ase that are involved in its catalytic activity. In comparison to homologous enzymes, PET ase contains an additional disulfide bond as well as an extended β8‐α6 loop. More importantly, the crystal structures of PET ase in complex with substrate and product analogs provide critical information for understanding the mechanism of action of PET ase. In particular, the wobbling conformation of W156 is closely related to the binding of substrate and product. These new findings are of great importance for further in‐depth research and engineering development of PET ase, and should advance the implementation of plastic biodegradation strategy.

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Metadata

Authors
Chen, C., Han, X., Ko, T., Liu, W., & Guo, R.
Venue
The FEBS Journal
Publisher
Wiley
Published
2018-08-17
Volume
285
Issue
20
Pages
3717-3723
ISSN
  • 1742-464X (ISSN-L)
  • 1742-4658
OpenAlex
W2883813712
Cited by
166
References
1
FWCI
4.25
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structural studies reveal the molecular mechanism of PET ase. https://app.cochat.ai/papers/10.1111/febs.14612
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Chen, C., Han, X., Ko, T., Liu, W., & Guo, R. (2018). Structural studies reveal the molecular mechanism of PET ase. The FEBS Journal. https://doi.org/10.1111/febs.14612

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