ArticleComputational and structural biotechnology journal2021
Computational design of noncanonical amino acid-based thioether staples at N/C-terminal domains of multi-modular pullulanase for thermostabilization in enzyme catalysis.
Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 20 citations in OpenAlex.
- Computational Design of a Thermo-Acidostable Endo-Polygalacturonase for Efficient Juice Extraction.Foods (Basel, Switzerland) · 2026Article
- Noncanonical Amino Acids: Bringing New-to-Nature Functionalities to Biocatalysis.Chemical reviews · 2024Review
- Noncanonical Amino Acids in Biocatalysis.Chemical reviews · 2024Review
- The Minimum Protein Staple? - Towards 'bio'-Baldwin's rulesChemical science · 2024Article
- Thermal Stability Enhancement of L-Asparaginase fromFoods (Basel, Switzerland) · 2023Article
- Improving the catalytic activity of a detergent-compatible serine protease by rational design.Microbial biotechnology · 2023Article
- Possibilities of Using De Novo Design for Generating Diverse Functional Food Enzymes.International journal of molecular sciences · 2023Review
- Non-canonical amino acids as a tool for the thermal stabilization of enzymes.Protein engineering, design & selection : PEDS · 2023Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzyme thermostabilization is considered a critical and often obligatory step in biosynthesis, because thermostability is a significant property of enzymes that can be used to evaluate their feasibility for industrial applications. However, conventional strategies for thermostabilizing enzymes generally introduce non-covalent interactions and/or natural covalent bonds caused by natural amino acid substitutions, and the trade-off between the activity and stability of enzymes remains a challenge. Here, we developed a computationally guided strategy for constructing thioether staples by incorporating noncanonical amino acid (ncAA) into the more flexible N/C-terminal domains of the multi-modular pullulanase from
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