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Bastos, Fernanda de M.; Santos, Alexandre Gonçalves; JonesJr., Joel; Oestreicher, Enrique G.; Pinto, Gerson F.; Paiva, Lucia Moreira Campos

doi:10.1023/a:1008957711413

Cited by 20 publications

(4 citation statements)

References 10 publications

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“…This enzyme utilizes cheap isopropanol as a co-substrate to regenerate cofactor NADPH, and has attracted much technological interest. 19,20 TbADH showed relatively high activity for small substrates (C4-C5 ketones), and low activity toward C5-C9 ketones. 19 Phillips et al employed sitedirected mutation to expand the substrate-binding pocket of TbADH, and the resulting mutants I86A and W110A exhibited increased activity toward phenyl ring-containing prochiral ketones, t-butyl and some α-branched ketones.…”

Section: Introductionmentioning

confidence: 99%

Directed evolution of an alcohol dehydrogenase for the desymmetric reduction of 2,2-disubstituted cyclopenta-1,3-diones by enzymatic hydrogen transfer

Zhang

Zhu

Feng

et al. 2022

Catal. Sci. Technol.

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Section: Introductionmentioning

confidence: 99%

Directed evolution of an alcohol dehydrogenase for the desymmetric reduction of 2,2-disubstituted cyclopenta-1,3-diones by enzymatic hydrogen transfer

Zhang

Zhu

Feng

et al. 2022

Catal. Sci. Technol.

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“…NADH and NADPH, as the most commonly used cofactors in the redox reaction, are not cost-effective for industrial applications. Although glucose dehydrogenase (GDH) , and formic dehydrogenase (FDH) , are usually coupled with oxidoreductase for the regeneration of NADH/NADPH, a large amount of additional by-substrates (glucose and formic acid) are required and the by-products (gluconic acid and CO 2 ) often affect the catalytic efficiency and product purity.…”

Section: Introductionmentioning

confidence: 99%

Self-Sufficient In Vitro Multi-Enzyme Cascade for Efficient Synthesis of Danshensu from l-DOPA

et al. 2022

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Danshensu (DSS), a traditional Chinese medicine, is widely used for the treatment of cardiovascular and cancer diseases. Here, a one-pot multi-enzyme cascade pathway was designed for DSS synthesis from l-DOPA using tyrosine aminotransferase from Escherichia coli (EcTyrB) and d-isomer-specific 2-hydroxyacid dehydrogenase from Lactobacillus frumenti (LfD2-HDH). Glutamate dehydrogenase from Clostridium difficile (CdgluD) was also introduced for a self-sufficient system of α-ketoglutaric acid and NADH. Under optimal conditions (35 °C, pH 7.0, EcTyrB:LfD2-HDH:CdgluD = 3:2:1, glutamate:NAD+ = 1:1), 98.3% yield (at 20 mM l-DOPA) and space-time yield of 6.61 g L–1 h–1 (at 40 mM l-DOPA) were achieved. Decreased yields of DSS at elevated l-DOPA concentrations (100 mM) could be attributed to an inhibited CdgluD activity caused by NH4 + accumulation. This developed multi-enzyme cascade pathway (including EcTyrB, LfD2-HDH, and CdgluD) provides an efficient and sustainable approach for the production of DSS from l-DOPA.

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“…Most chemical routes are hindered by cumbersome reaction conditions, low turnover number (TTN), expensive and/or toxic reagents, and/or unwanted side products, therefore not preferred for commercial or preparative applications. Biochemical methods with enzymes as catalysts have been demonstrated more efficient and applicable (Huisman et al 2010 ), including the use of glucose dehydrogenase (GDH) (Weckbecker and Hummel 2005 ), glucose-6-phosphate dehydrogenase (G6PDH) (Zhang et al 2006 ), alcohol dehydrogenase (ADH) (Bastos et al 1999 ), phosphite dehydrogenase (PDH) (Johannes et al 2007a ), formate dehydrogenase (FDH) (Celik et al 2014 ), hydrogenase (Fan et al 2020 ) and so forth. GDH and G6PDH with an advantage of high specific activity (200–500 U/mg at 25–30 °C) (Ding et al 2011 ; Wennekes et al 1993 ) suffer from high co-substrate consumption and by-product separation cost.…”

Section: Introductionmentioning

confidence: 99%

Computational design of highly stable and soluble alcohol dehydrogenase for NADPH regeneration

Zhou

et al. 2021

Bioresour. Bioprocess.

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Nicotinamide adenine dinucleotide phosphate (NADPH), as a well-known cofactor, is widely used in the most of enzymatic redox reactions, playing an important role in industrial catalysis. However, the absence of a comparable method for efficient NADP+ to NADPH cofactor regeneration radically impairs efficient green chemical synthesis. Alcohol dehydrogenase (ADH) enzymes, allowing the in situ regeneration of the redox cofactor NADPH with high specific activity and easy by-product separation process, are provided with great industrial application potential and research attention. Accordingly, herein a NADP+-specific ADH from Clostridium beijerinckii was selected to be engineered for cofactor recycle, using an automated algorithm named Protein Repair One-stop Shop (PROSS). The mutant CbADH-6M (S24P/G182A/G196A/H222D/S250E/S254R) exhibited a favorable soluble and highly active expression with an activity of 46.3 U/mL, which was 16 times higher than the wild type (2.9 U/mL), and a more stable protein conformation with an enhanced thermal stability: Δ $${T}_{1/2}^{60\mathrm{min}}$$ T 1 / 2 60 min = + 3.6 °C (temperature of 50% inactivation after incubation for 60 min). Furthermore, the activity of CbADH-6M was up-graded to 2401.8 U/mL by high cell density fermentation strategy using recombinant Escherichia coli, demonstrating its industrial potential. Finally, the superb efficiency for NADPH regeneration of the mutant enzyme was testified in the synthesis of some fine chiral aromatic alcohols coupling with another ADH from Lactobacillus kefir (LkADH).

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Cited by 20 publications

References 10 publications

Directed evolution of an alcohol dehydrogenase for the desymmetric reduction of 2,2-disubstituted cyclopenta-1,3-diones by enzymatic hydrogen transfer

Directed evolution of an alcohol dehydrogenase for the desymmetric reduction of 2,2-disubstituted cyclopenta-1,3-diones by enzymatic hydrogen transfer

Self-Sufficient In Vitro Multi-Enzyme Cascade for Efficient Synthesis of Danshensu from l-DOPA

Computational design of highly stable and soluble alcohol dehydrogenase for NADPH regeneration

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