Enhancing cofactor recycling in the bioconversion of racemic alcohols to chiral amines with alcohol dehydrogenase and amine dehydrogenase by coupling cells and cell‐free system
Sign Up to like & getrecommendations! Published in 2019 at "Biotechnology and Bioengineering"
DOI: 10.1002/bit.26896
Abstract: Alcohol dehydrogenase (ADH) and amine dehydrogenase (AmDH)‐catalyzed one‐pot cascade conversion of an alcohol to an amine provides a simple preparation of chiral amines. To enhance the cofactor recycling in this reaction, we report a new… read more here.
Keywords: dehydrogenase; racemic alcohols; conversion; alcohol dehydrogenase ... See more keywords
Advanced Insights into Catalytic and Structural Features of the Zinc‐Dependent Alcohol Dehydrogenase from Thauera aromatica
Sign Up to like & getrecommendations! Published in 2022 at "Chembiochem"
DOI: 10.1002/cbic.202200149
Abstract: The asymmetric reduction of ketones to chiral hydroxyl compounds by alcohol dehydrogenases (ADHs) is an established strategy for the provision of valuable precursors for fine chemicals and pharmaceutics. However, most ADHs favor linear aliphatic and… read more here.
Keywords: alcohol dehydrogenase; thauera aromatica; dehydrogenase thauera; catalytic structural ... See more keywords
Cloning, Expression and Characterization of a Highly Active Alcohol Dehydrogenase for Production of Ethyl (S)-4-Chloro-3-Hydroxybutyrate
Sign Up to like & getrecommendations! Published in 2019 at "Indian Journal of Microbiology"
DOI: 10.1007/s12088-019-00795-0
Abstract: A novel alcohol dehydrogenase from Bartonella apis (BaADH) was heterologous expressed in Escherichia coli. Its biochemical properties were investigated and used to catalyze the synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-CHBE), which is a chiral intermediate of… read more here.
Keywords: ethyl chloro; dehydrogenase; cloning expression; alcohol dehydrogenase ... See more keywords
Oxidation of ethanol by human alcohol dehydrogenase (ADH) 1A is activated by ATP.
Sign Up to like & getrecommendations! Published in 2021 at "Biochimie"
DOI: 10.1016/j.biochi.2021.11.002
Abstract: Presently we report that enzymatic oxidation of ethanol (EtOH) by ADH1A alcohol dehydrogenase is strongly accelerated in presence of adenosine triphosphate (ATP), by up to the factor of 20 in vitro. This result provides a… read more here.
Keywords: ethanol human; alcohol; oxidation ethanol; alcohol dehydrogenase ... See more keywords
Effective immobilization of alcohol dehydrogenase on carbon nanoscaffolds for ethanol biofuel cell.
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DOI: 10.1016/j.bioelechem.2017.07.008
Abstract: An efficient approach for immobilizing alcohol dehydrogenase (ADH) while enhancing its electron transfer ability has been developed using poly(2-(trimethylamino)ethyl methacrylate) (MADQUAT) cationic polymer and carbon nanoscaffolds. The carbon nanoscaffolds were comprised of single-walled carbon nanotubes… read more here.
Keywords: biofuel; carbon; immobilization; carbon nanoscaffolds ... See more keywords
A novel metabolic disorder in the degradation pathway of endogenous methanol due to a mutation in the gene of alcohol dehydrogenase.
Sign Up to like & getrecommendations! Published in 2021 at "Clinical biochemistry"
DOI: 10.1016/j.clinbiochem.2021.01.007
Abstract: BACKGROUND A small amount of methanol is produced endogenously in the human body but it is efficiently metabolized by alcohol dehydrogenase (ADH) and other enzymes, and the products eliminated without harm. In this study, we… read more here.
Keywords: due mutation; methanol due; alcohol dehydrogenase; gene ... See more keywords
Co-expression of an alcohol dehydrogenase and a cyclohexanone monooxygenase for cascade reactions facilitates the regeneration of the NADPH cofactor.
Sign Up to like & getrecommendations! Published in 2018 at "Enzyme and microbial technology"
DOI: 10.1016/j.enzmictec.2017.09.003
Abstract: The introduction of a three-enzyme cascade (comprising a cyclohexanone monooxygenase (CHMO), an alcohol dehydrogenase (ADH) and a lipase (CAL-A)) for the production of oligo-ε-caprolactone provided self-sufficiency with respect to NADPH-cofactor regeneration and reduced inhibiting effects… read more here.
Keywords: cyclohexanone monooxygenase; regeneration; expression; alcohol dehydrogenase ... See more keywords
Integrating a light-driven coenzyme regeneration system by expression of an alcohol dehydrogenase in phototrophic bacteria for synthesis of chiral alcohol.
Sign Up to like & getrecommendations! Published in 2017 at "Journal of biotechnology"
DOI: 10.1016/j.jbiotec.2017.07.032
Abstract: Herein, we reported that Rhodobacter sphaeroides (R. sphaeroides) can be engineered by heterologous expression of an alcohol dehydrogenase (adh) from Leifsonia sp. to build a light-driven cofactor regeneration system for synthesis of chiral alcohol. The… read more here.
Keywords: expression alcohol; system; regeneration; light driven ... See more keywords
Molecular switch manipulating Prelog priority of an alcohol dehydrogenase toward bulky-bulky ketones
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DOI: 10.1016/j.mcat.2019.110741
Abstract: Abstract Structure-guided rational design revealed the molecular switch manipulating the Prelog and anti-Prelog priorities of an NADPH-dependent alcohol dehydrogenase toward prochiral ketones with bulky and similar substituents. Synergistic effects of unconserved residues at 214 and… read more here.
Keywords: prelog; manipulating prelog; switch manipulating; alcohol dehydrogenase ... See more keywords
Enzymatic preparation of optically pure t-butyl 6-chloro-(3R,5S)-dihydroxyhexanoate by a novel alcohol dehydrogenase discovered from Klebsiella oxytoca
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DOI: 10.1016/j.procbio.2017.03.019
Abstract: Abstract Alcohol dehydrogenases can catalyze the inter-conversion of aldehydes and alcohols. The t -butyl 6-chloro-(3 R ,5 S )-dihydroxyhexanoate is a key chiral intermediate in the synthesis of statin-type drugs such as Crestor (rosuvastatin calcium)… read more here.
Keywords: butyl chloro; novel alcohol; chloro dihydroxyhexanoate; alcohol dehydrogenase ... See more keywords
The alcohol dehydrogenase with a broad range of substrate specificity regulates vitality and reproduction of the plant-parasitic nematode Bursaphelenchus xylophilus
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DOI: 10.1017/s0031182018001695
Abstract: Abstract Pine wilt disease, which is caused by the pine wood nematode (PWN), Bursaphelenchus xylophilus, has caused huge damage to pine forests around the world. In this study, we analysed the PWN transcriptome to investigate… read more here.
Keywords: vitality reproduction; nematode; alcohol dehydrogenase; adh ... See more keywords