ArticleChembiochem : a European journal of chemical biology2022
Fusion of Formate Dehydrogenase and Alanine Dehydrogenase as an Amino Donor Regenerating System Coupled to Transaminases.
Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 15 citations in OpenAlex.
- Advances in biosynthesis of chiral amide herbicides and the key enzymes: dimethenamid-P and S-metolachlor as case studies.Bioresources and bioprocessing · 2025Review
- Self-sufficient biocatalytic cascade for the continuous synthesis of danshensu in flow.Applied microbiology and biotechnology · 2025Article
- Engineering a Bifunctional Fusion Purine/Pyrimidine Nucleoside Phosphorylase for the Production of Nucleoside Analogs.Biomolecules · 2024Article
- Overcoming Protein Orientation Mismatch Enables Efficient Nanoscale Light-Driven ATP Production.ACS synthetic biology · 2024Article
- Halomonas elongata: a microbial source of highly stable enzymes for applied biotechnology.Applied microbiology and biotechnology · 2023Review
- Fusion of Formate Dehydrogenase and Alanine Dehydrogenase as an Amino Donor Regenerating System Coupled to Transaminases.Chembiochem : a European journal of chemical biology · 2022Article
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4 authors at 1 institution in 1 country.
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Abstract
Fusion enzymes are attractive tools for facilitating the assembly of biocatalytic cascades for chemical synthesis. This approach can offer great advantages for cooperative redox cascades that need the constant supply of a donor molecule. In this work, we have developed a self-sufficient bifunctional enzyme that can be coupled to transaminase-catalyzed reactions for the efficient recycling of the amino donor (L-alanine). By genetic fusion of an alanine dehydrogenase (AlaDH) and a formate dehydrogenase (FDH), a redox-complementary system was applied to recycle the amino donor and the cofactor (NADH), respectively. AlaDH and FDH were assembled in both combinations (FDH-AlaDH and AlaDH-FDH), with a 2.5-fold higher enzymatic activity of the latter system. Then, AlaDH-FDH was coupled to two different S-selective transaminases for the synthesis of vanillyl amine (10 mM) reaching up to 99 % conversion in 24 h in both cases. Finally, the multienzyme system was reused for at least 3 consecutive cycles when implemented in dialysis-assisted biotransformations.
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