ArticleBiotechnology journal2017
Exploring Bacterial Carboxylate Reductases for the Reduction of Bifunctional Carboxylic Acids.
Article in Biotechnology journal, 2017. 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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Who cites it
14 citing papers in PubMed, 88 citations in OpenAlex.
- Biocatalytic Carboxylic Acid Reduction and Transamination in Cell-Free Lysates at High Substrate Loading.ChemSusChem · 2026Article
- ATP regeneration-driven biocatalytic production of 1,12-dodecanediol with improved cofactor supply.Bioresources and bioprocessing · 2026Article
- Recent advances in pathway engineering for the biosynthesis of 1,4-butanediol.Applied microbiology and biotechnology · 2026Review
- Synthetic redesign of Corynebacterium glutamicum for 1,4-butanediol production via L-glutamate-derived CoA-independent pathway.Journal of biological engineering · 2025Article
- Metabolic Engineering of Corynebacterium glutamicum for High-Level Production of 1,5-Pentanediol, a C5 Diol Platform Chemical.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Computation-driven redesign of an NRPS-like carboxylic acid reductase improves activity and selectivity.Science advances · 2024Article
- Reductive amination cascades in cell-free and resting whole cell formats for valorization of lignin deconstruction products.Biotechnology and bioengineering · 2024Article
- Fatty Acids and their Derivatives as Renewable Platform Molecules for the Chemical Industry.Angewandte Chemie (International ed. in English) · 2021Review
- Biocatalytic Reduction Reactions from a Chemist's Perspective.Angewandte Chemie (International ed. in English) · 2021Review
- Biocatalysis: Enzymatic Synthesis for Industrial Applications.Angewandte Chemie (International ed. in English) · 2021Review
- Engineering a Seven Enzyme Biotransformation using Mathematical Modelling and Characterized Enzyme Parts.ChemCatChem · 2019Article
- Enzymatic One-Step Reduction of Carboxylates to Aldehydes with Cell-Free Regeneration of ATP and NADPH.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Highly thermostable carboxylic acid reductases generated by ancestral sequence reconstruction.Communications biology · 2019Article
- Identification of Key Residues for Enzymatic Carboxylate Reduction.Frontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
Carboxylic acid reductases (CARs) selectively reduce carboxylic acids to aldehydes using ATP and NADPH as cofactors under mild conditions. Although CARs attracts significant interest, only a few enzymes have been characterized to date, whereas the vast majority of CARs have yet to be examined. Herein the authors report that 12 bacterial CARs reduces a broad range of bifunctional carboxylic acids containing oxo-, hydroxy-, amino-, or second carboxyl groups with several enzymes showing activity toward 4-hydroxybutanoic (4-HB) and adipic acids. These CARs exhibits significant reductase activity against substrates whose second functional group is separated from the carboxylate by at least three carbons with both carboxylate groups being reduced in dicarboxylic acids. Purified CARs supplemented with cofactor regenerating systems (for ATP and NADPH), an inorganic pyrophosphatase, and an aldo-keto reductase catalyzes a high conversion (50-76%) of 4-HB to 1,4-butanediol (1,4-BDO) and adipic acid to 1,6-hexanediol (1,6-HDO). Likewise, Escherichia coli strains expressing eight different CARs efficiently reduces 4-HB to 1,4-BDO with 50-95% conversion, whereas adipic acid is reduced to a mixture of 6-hydroxyhexanoic acid (6-HHA) and 1,6-HDO. Thus, our results illustrate the broad biochemical diversity of bacterial CARs and their compatibility with other enzymes for applications in biocatalysis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.