ArticleChembiochem : a European journal of chemical biology2019
B-factor Guided Proline Substitutions in Chromobacterium violaceum Amine Transaminase: Evaluation of the Proline Rule as a Method for Enzyme Stabilization.
Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 31 citations in OpenAlex.
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- Research Advances of d-allulose: An Overview of Physiological Functions, Enzymatic Biotransformation Technologies, and Production Processes.Foods (Basel, Switzerland) · 2021Review
- Engineering of Thermal Stability in a Cold-Active Oligo-1,6-Glucosidase fromBiomolecules · 2021Article
- Improving enzyme activity of glucosamine-6-phosphate synthase by semi-rational design strategy and computer analysis.Biotechnology letters · 2020Article
- Improving the catalytic thermostability of3 Biotech · 2020Article
- Robust ω-Transaminases by Computational Stabilization of the Subunit Interface.ACS catalysis · 2020Article
- Genome mining and characterisation of a novel transaminase with remote stereoselectivity.Scientific reports · 2019Article
- Insight into the dimer dissociation process of the Chromobacterium violaceum (S)-selective amine transaminase.Scientific reports · 2019Article
- B-factor Guided Proline Substitutions in Chromobacterium violaceum Amine Transaminase: Evaluation of the Proline Rule as a Method for Enzyme Stabilization.Chembiochem : a European journal of chemical biology · 2019Article
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4 authors at 3 institutions in 1 country.
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Abstract
Biocatalysis is attracting interest in the chemical industry as a sustainable alternative in large-scale chemical transformations. However, low operational stability of naturally evolved enzymes is a challenge and major efforts are required to engineer protein stability, usually by directed evolution. The development of methods for protein stabilization based on rational design is of great interest, as it would minimize the efforts needed to generate stable enzymes. Here we present a rational design strategy based on proline substitutions in flexible areas of the protein identified by analyzing B-factors. Several proline substitutions in the amine transaminase from Chromobacterium violaceum were shown to have a positive impact on stability with increased half-life at 60 °C by a factor of 2.7 (variant K69P/D218P/K304P/R432P) as well as increased melting temperature by 8.3 °C (variant K167P). Finally, the presented method utilizing B-factor analysis in combination with the proline rule was deemed successful at increasing the stability of this enzyme.
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