ArticleScientific reports2015
A new target region for changing the substrate specificity of amine transaminases.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Transaminases engineering and their cascade systems for natural product synthesis.Applied biochemistry and biotechnology · 2026Review
- SPIN-guided engineering of a novel (Synthetic and systems biotechnology · 2026Article
- Article
- Bioproduction of 3,4-methylenedioxymethamphetamine and derivatives.Biodesign research · 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
- A transaminase-mediated aldol reaction and applications in cascades to styryl pyridines.Catalysis science & technology · 2024Article
- Protein engineering of transaminase facilitating enzyme cascade reaction for the biosynthesis of azasugars.iScience · 2024Article
- Biocatalytic cascade to polysaccharide amination.Biotechnology for biofuels and bioproducts · 2024Article
- The rapid high-throughput screening of ω-transaminases via a colorimetric method using aliphatic α-diketones as amino acceptors.Analytical and bioanalytical chemistry · 2023Article
- Regiospecific C-H amination of (-)-limonene into (-)-perillamine by multi-enzymatic cascade reactions.Bioresources and bioprocessing · 2022Article
- Engineering Novel (Applied and environmental microbiology · 2022Article
- Non-Canonical Amino Acid-Based Engineering of (Frontiers in chemistry · 2022Article
- Identification, Characterization, and Site-Specific Mutagenesis of a Thermostable ω-Transaminase fromACS omega · 2021Article
- High Regio- and Stereoselective Multi-enzymatic Synthesis of All Phenylpropanolamine Stereoisomers from β-Methylstyrene.Chembiochem : a European journal of chemical biology · 2021Article
- Expanding the Toolbox of R-Selective Amine Transaminases by Identification and Characterization of New Members.Chembiochem : a European journal of chemical biology · 2021Article
- Probing the role of the residues in the active site of the transaminase from Thermobaculum terrenum.PloS one · 2021Article
- Reshaping the substrate binding region of (R)-selective ω-transaminase for asymmetric synthesis of (R)-3-amino-1-butanol.Applied microbiology and biotechnology · 2020Article
- Structural basis of substrate recognition by a novel thermostable (S)-enantioselective ω-transaminase from Thermomicrobium roseum.Scientific reports · 2019Article
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
(R)-stereospecific amine transaminases (R-ATAs) are important biocatalysts for the production of (R)-amine compounds in a strict stereospecific manner. An improved R-ATA, ATA-117-Rd11, was successfully engineered for the manufacture of sitagliptin, a widely used therapeutic agent for type-2 diabetes. The effects of the individual mutations, however, have not yet been demonstrated due to the lack of experimentally determined structural information. Here we describe three crystal structures of the first isolated R-ATA, its G136F mutant and engineered ATA-117-Rd11, which indicated that the mutation introduced into the 136(th) residue altered the conformation of a loop next to the active site, resulting in a substrate-binding site with drastically modified volume, shape, and surface properties, to accommodate the large pro-sitagliptin ketone. Our findings provide a detailed explanation of the previously reported molecular engineering of ATA-117-Rd11 and propose that the loop near the active site is a new target for the rational design to change the substrate specificity of ATAs.
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