ArticleNature communications2016
Using mutability landscapes of a promiscuous tautomerase to guide the engineering of enantioselective Michaelases.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 102 citations in OpenAlex.
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- Decoding the substrate specificity landscape of a promiscuous enzyme through multi-substrate mutational scanning.Nature communications · 2026Article
- Advances in ligand-specific biosensing for structurally similar molecules.Cell systems · 2023Review
- Enhancing the Peroxygenase Activity of a Cofactor-Independent Peroxyzyme by Directed Evolution Enabling Gram-Scale Epoxide Synthesis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Unlocking New Reactivities in Enzymes by Iminium Catalysis.Angewandte Chemie (International ed. in English) · 2022Review
- Making Enzymes Suitable for Organic Chemistry by Rational Protein Design.Chembiochem : a European journal of chemical biology · 2022Review
- Traceless enzymatic protein synthesis without ligation sites constraint.National science review · 2022Article
- Enantiocomplementary Michael Additions of Acetaldehyde to Aliphatic Nitroalkenes Catalyzed by Proline-Based Carboligases.Chembiochem : a European journal of chemical biology · 2022Article
- High-throughput screening, next generation sequencing and machine learning: advanced methods in enzyme engineering.Chemical communications (Cambridge, England) · 2022Review
- Gene Fusion and Directed Evolution to Break Structural Symmetry and Boost Catalysis by an Oligomeric C-C Bond-Forming Enzyme.Angewandte Chemie (International ed. in English) · 2022Article
- Learning Strategies in Protein Directed Evolution.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Engineered Myoglobin Catalysts for Asymmetric Intermolecular Cyclopropanation Reactions.Bulletin of Japan Society of Coordination Chemistry · 2022Article
- The role of streptavidin and its variants in catalysis by biotinylated secondary amines.Organic & biomolecular chemistry · 2021Article
- Biocatalytic Asymmetric Cyclopropanations via Enzyme-Bound Iminium Ion Intermediates.Angewandte Chemie (International ed. in English) · 2021Article
- Enzymatic strategies for asymmetric synthesis.RSC chemical biology · 2021Review
- Power of Biocatalysis for Organic Synthesis.ACS central science · 2021Review
- Using Mutability Landscapes To Guide Enzyme Thermostabilization.Chembiochem : a European journal of chemical biology · 2021Article
- Structure and evolutionary trace-assisted screening of a residue swapping the substrate ambiguity and chiral specificity in an esterase.Computational and structural biotechnology journal · 2021Article
- Targeted mutagenesis of multiple chromosomal regions in microbes.Current opinion in microbiology · 2020Review
- A mechanistic view of enzyme evolution.Protein science : a publication of the Protein Society · 2020Review
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Michael-type addition reaction is widely used in organic synthesis for carbon-carbon bond formation. However, biocatalytic methodologies for this type of reaction are scarce, which is related to the fact that enzymes naturally catalysing carbon-carbon bond-forming Michael-type additions are rare. A promising template to develop new biocatalysts for carbon-carbon bond formation is the enzyme 4-oxalocrotonate tautomerase, which exhibits promiscuous Michael-type addition activity. Here we present mutability landscapes for the expression, tautomerase and Michael-type addition activities, and enantioselectivity of 4-oxalocrotonate tautomerase. These maps of neutral, beneficial and detrimental amino acids for each residue position and enzyme property provide detailed insight into sequence-function relationships. This offers exciting opportunities for enzyme engineering, which is illustrated by the redesign of 4-oxalocrotonate tautomerase into two enantiocomplementary 'Michaelases'. These 'Michaelases' catalyse the asymmetric addition of acetaldehyde to various nitroolefins, providing access to both enantiomers of γ-nitroaldehydes, which are important precursors for pharmaceutically active γ-aminobutyric acid derivatives.
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