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Cited by 210

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Protein Crystallography and Site‐Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis

Liu, Bing, He, Lihui, Wang, Liping, Li, Tao, Li, Changcheng, Liu, Huayi, Luo, Yunzi, Bao, Rui·2018·ChemBioChem

Abstract

Unlike traditional recycling strategies, biodegradation is a sustainable solution for disposing of poly(ethylene terephthalate) (PET) waste. PETase, a newly identified enzyme from Ideonella sakaiensis, has high efficiency and specificity towards PET and is, thus, a prominent candidate for PET degradation. On the basis of biochemical analysis, we propose that a wide substrate‐binding pocket is critical for its excellent ability to hydrolyze crystallized PET. Structure‐guided site‐directed mutagenesis revealed an improvement in PETase catalytic efficiency, providing valuable insight into how the molecular engineering of PETase can optimize its application in biocatalysis.

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Metadata

Authors
Liu, B., He, L., Wang, L., Li, T., Li, C., Liu, H., Luo, Y., & Bao, R.
Venue
ChemBioChem
Publisher
Wiley
Published
2018-05-28
Volume
19
Issue
14
Pages
1471-1475
ISSN
  • 1439-4227 (ISSN-L)
  • 1439-7633
OpenAlex
W2795284646
Cited by
210
References
1
FWCI
7.77
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Protein Crystallography and Site‐Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis. https://app.cochat.ai/papers/10.1002/cbic.201800097
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Liu, B., He, L., Wang, L., Li, T., Li, C., Liu, H., Luo, Y., & Bao, R. (2018). Protein Crystallography and Site‐Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis. ChemBioChem. https://doi.org/10.1002/cbic.201800097

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.