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Characterization and engineering of a plastic-degrading aromatic polyesterase

Overview of attention for article published in Proceedings of the National Academy of Sciences of the United States of America, April 2018
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About this Attention Score

  • In the top 5% of all research outputs scored by Altmetric
  • High Attention Score compared to outputs of the same age (99th percentile)
  • High Attention Score compared to outputs of the same age and source (99th percentile)

Citations

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283 Dimensions

Readers on

mendeley
1606 Mendeley
citeulike
2 CiteULike
Title
Characterization and engineering of a plastic-degrading aromatic polyesterase
Published in
Proceedings of the National Academy of Sciences of the United States of America, April 2018
DOI 10.1073/pnas.1718804115
Pubmed ID
Authors

Harry P. Austin, Mark D. Allen, Bryon S. Donohoe, Nicholas A. Rorrer, Fiona L. Kearns, Rodrigo L. Silveira, Benjamin C. Pollard, Graham Dominick, Ramona Duman, Kamel El Omari, Vitaliy Mykhaylyk, Armin Wagner, William E. Michener, Antonella Amore, Munir S. Skaf, Michael F. Crowley, Alan W. Thorne, Christopher W. Johnson, H. Lee Woodcock, John E. McGeehan, Gregg T. Beckham

Abstract

Poly(ethylene terephthalate) (PET) is one of the most abundantly produced synthetic polymers and is accumulating in the environment at a staggering rate as discarded packaging and textiles. The properties that make PET so useful also endow it with an alarming resistance to biodegradation, likely lasting centuries in the environment. Our collective reliance on PET and other plastics means that this buildup will continue unless solutions are found. Recently, a newly discovered bacterium, Ideonella sakaiensis 201-F6, was shown to exhibit the rare ability to grow on PET as a major carbon and energy source. Central to its PET biodegradation capability is a secreted PETase (PET-digesting enzyme). Here, we present a 0.92 Å resolution X-ray crystal structure of PETase, which reveals features common to both cutinases and lipases. PETase retains the ancestral α/β-hydrolase fold but exhibits a more open active-site cleft than homologous cutinases. By narrowing the binding cleft via mutation of two active-site residues to conserved amino acids in cutinases, we surprisingly observe improved PET degradation, suggesting that PETase is not fully optimized for crystalline PET degradation, despite presumably evolving in a PET-rich environment. Additionally, we show that PETase degrades another semiaromatic polyester, polyethylene-2,5-furandicarboxylate (PEF), which is an emerging, bioderived PET replacement with improved barrier properties. In contrast, PETase does not degrade aliphatic polyesters, suggesting that it is generally an aromatic polyesterase. These findings suggest that additional protein engineering to increase PETase performance is realistic and highlight the need for further developments of structure/activity relationships for biodegradation of synthetic polyesters.

Twitter Demographics

The data shown below were collected from the profiles of 280 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 1,606 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 1606 100%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 358 22%
Student > Ph. D. Student 230 14%
Researcher 215 13%
Student > Master 208 13%
Other 50 3%
Other 208 13%
Unknown 337 21%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 450 28%
Agricultural and Biological Sciences 208 13%
Chemistry 158 10%
Engineering 92 6%
Chemical Engineering 70 4%
Other 227 14%
Unknown 401 25%

Attention Score in Context

This research output has an Altmetric Attention Score of 2157. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 23 July 2021.
All research outputs
#2,435
of 19,169,076 outputs
Outputs from Proceedings of the National Academy of Sciences of the United States of America
#87
of 92,424 outputs
Outputs of similar age
#44
of 292,057 outputs
Outputs of similar age from Proceedings of the National Academy of Sciences of the United States of America
#5
of 1,012 outputs
Altmetric has tracked 19,169,076 research outputs across all sources so far. Compared to these this one has done particularly well and is in the 99th percentile: it's in the top 5% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 92,424 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 32.9. This one has done particularly well, scoring higher than 99% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 292,057 tracked outputs that were published within six weeks on either side of this one in any source. This one has done particularly well, scoring higher than 99% of its contemporaries.
We're also able to compare this research output to 1,012 others from the same source and published within six weeks on either side of this one. This one has done particularly well, scoring higher than 99% of its contemporaries.