Using Mutability Landscapes To Guide Enzyme Thermostabilization Article Swipe
Chao Guo
,
Yan Ni
,
Lieuwe Biewenga
,
Tjaard Pijning
,
A.M.W.H. Thunnissen
,
Gerrit J. Poelarends
·
YOU?
·
· 2020
· Open Access
·
· DOI: https://doi.org/10.1002/cbic.202000442
YOU?
·
· 2020
· Open Access
·
· DOI: https://doi.org/10.1002/cbic.202000442
Thermostabilizing enzymes while retaining their activity and enantioselectivity for applied biocatalysis is an important topic in protein engineering. Rational and computational design strategies as well as directed evolution have been used successfully to thermostabilize enzymes. Herein, we describe an alternative mutability‐landscape approach that identified three single mutations (R11Y, R11I and A33D) within the enzyme 4‐oxalocrotonate tautomerase (4‐OT), which has potential as a biocatalyst for pharmaceutical synthesis, that gave rise to significant increases in apparent melting temperature T m (up to 20 °C) and in half‐life at 80 °C (up to 111‐fold). Introduction of these beneficial mutations in an enantioselective but thermolabile 4‐OT variant (M45Y/F50A) afforded improved triple‐mutant enzyme variants showing an up to 39 °C increase in T m value, with no reduction in catalytic activity or enantioselectivity. This study illustrates the power of mutability‐landscape‐guided protein engineering for thermostabilizing enzymes.
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- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1002/cbic.202000442
- https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/cbic.202000442
- OA Status
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- Cited By
- 11
- References
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- Related Works
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- OpenAlex ID
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https://doi.org/10.1002/cbic.202000442Digital Object Identifier
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Using Mutability Landscapes To Guide Enzyme ThermostabilizationWork title
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articleOpenAlex work type
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enPrimary language
- Publication year
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2020Year of publication
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2020-08-13Full publication date if available
- Authors
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Chao Guo, Yan Ni, Lieuwe Biewenga, Tjaard Pijning, A.M.W.H. Thunnissen, Gerrit J. PoelarendsList of authors in order
- Landing page
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https://doi.org/10.1002/cbic.202000442Publisher landing page
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https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/cbic.202000442Direct link to full text PDF
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YesWhether a free full text is available
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hybridOpen access status per OpenAlex
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https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/cbic.202000442Direct OA link when available
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Enzyme, Chemistry, Computational biology, Biophysics, Biochemistry, Nanotechnology, Biology, Materials scienceTop concepts (fields/topics) attached by OpenAlex
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11Total citation count in OpenAlex
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2025: 2, 2024: 1, 2023: 3, 2022: 3, 2021: 1Per-year citation counts (last 5 years)
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10Other works algorithmically related by OpenAlex
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