ArticleNature chemical biology2010
Rational assignment of key motifs for function guides in silico enzyme identification.
Article in Nature chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed.
- Cloning and characterization of a new oleate hydratase from Acinetobacter ursingii for asymmetric hydration of unactivated alkenes.Biotechnology letters · 2025Article
- Development of Sustainable Biocatalytic Furfurylamine Production in a Magnetic Field-Assisted Microfluidic Reactor.ACS sustainable chemistry & engineering · 2025Article
- Contribution of Second-Shell Residues to PLP-Dependent Transaminase Catalysis: A Case Study of D-Amino Acid Transaminase fromInternational journal of molecular sciences · 2025Article
- Exploring the Stability and Substrate Profile of Transaminase from Silicibacter pomeroyi with Ancestral Sequence Reconstruction.Chembiochem : a European journal of chemical biology · 2025Article
- Advances in the Molecular Modification of Microbial ω-Transaminases for Asymmetric Synthesis of Bulky Chiral Amines.Microorganisms · 2025Review
- The pedal-like loop of (R)-selective transaminases plays a critical role to the functionality of the enzyme.Biotechnology letters · 2025Article
- From Structure to Function: Analysis of the First Monomeric Pyridoxal-5'-Phosphate-Dependent Transaminase from the BacteriumBiomolecules · 2024Article
- Novel enzymatic route to the synthesis of C-8 hydroxyflavonoids including flavonols and isoflavones.Scientific reports · 2024Article
- A transaminase-mediated aldol reaction and applications in cascades to styryl pyridines.Catalysis science & technology · 2024Article
- Reprogramming biocatalytic futile cycles through computational engineering of stereochemical promiscuity to create an amine racemase.Nature communications · 2024Article
- Tuning of Protein Expression by Promoter Engineering.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Expanded Substrate Specificity in D-Amino Acid Transaminases: A Case Study of Transaminase fromInternational journal of molecular sciences · 2023Article
- Enantio-Complementary Synthesis of 2-Substituted Pyrrolidines and Piperidines via Transaminase-Triggered Cyclizations.JACS Au · 2023Article
- Biocatalytic Transamination of Aldolase-Derived 3-Hydroxy Ketones.Advanced synthesis & catalysis · 2023Article
- To the Understanding of Catalysis by D-Amino Acid Transaminases: A Case Study of the Enzyme fromMolecules (Basel, Switzerland) · 2023Article
- Regulation of Human Endogenous Metabolites by Drug Transporters and Drug Metabolizing Enzymes: An Analysis of Targeted SNP-Metabolite Associations.Metabolites · 2023Article
- Shifting the pH Optima of (International journal of molecular sciences · 2022Article
- A growth selection system for the directed evolution of amine-forming or converting enzymes.Nature communications · 2022Article
- High-Yield Synthesis of Enantiopure 1,2-Amino Alcohols from l-Phenylalanine via Linear and Divergent Enzymatic Cascades.Organic process research & development · 2022Review
- In silico screening and heterologous expression of soluble dimethyl sulfide monooxygenases of microbial origin in Escherichia coli.Applied microbiology and biotechnology · 2022Article
17 more citing papers are in PubMed but not listed here.
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Biocatalysis has emerged as a powerful alternative to traditional chemistry, especially for asymmetric synthesis. One key requirement during process development is the discovery of a biocatalyst with an appropriate enantiopreference and enantioselectivity, which can be achieved, for instance, by protein engineering or screening of metagenome libraries. We have developed an in silico strategy for a sequence-based prediction of substrate specificity and enantiopreference. First, we used rational protein design to predict key amino acid substitutions that indicate the desired activity. Then, we searched protein databases for proteins already carrying these mutations instead of constructing the corresponding mutants in the laboratory. This methodology exploits the fact that naturally evolved proteins have undergone selection over millions of years, which has resulted in highly optimized catalysts. Using this in silico approach, we have discovered 17 (R)-selective amine transaminases, which catalyzed the synthesis of several (R)-amines with excellent optical purity up to >99% enantiomeric excess.
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