Enzymatic cascade synthesis of (S)-2-hydroxycarboxylic amides and acids: Cascade reactions employing a hydroxynitrile lyase, nitrile-converting enzymes and an amidase

Rantwijk, Fred van

doi:10.1016/j.molcatb.2014.08.012

Cited by 26 publications

(14 citation statements)

References 48 publications

(67 reference statements)

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“…L‐form amino acids were produced except for alanine. Enzymatic cascade synthesis of ( S )‐2‐hydroxy carboxylic amide and its acid from aldehydes was performed by hydroxynitrile lyase and nitrile‐converting enzymes . The cascade reaction needed two enzymes and the production level was low (less than 10 mM).…”

Section: Discussionmentioning

confidence: 99%

Retracted: Chemoenzymatic Method for Enantioselective Synthesis of (R)‐2‐Phenylglycine and (R)‐2‐Phenylglycine Amide from Benzaldehyde and KCN Using Difference of Enzyme Affinity to the Enantiomers

Kawahara

Asano

2018

ChemCatChem

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In general, enzymatic and chemoenzymatic methods for asymmetric synthesis of α‐amino acids are performed using highly enantioselective enzymes. The enzymatic reactions using α‐aminonitrile as a starting material have been performed using reaction conditions apart from the chemical Strecker synthesis. We developed a new chemoenzymatic method for the asymmetric synthesis of α‐amino acids from aldehydes and KCN by performing Strecker synthesis and nitrilase reaction in the same reaction mixture. Nitrilase AY487533 that showed rather low enantioselectivity in hydrolysis of 2‐phenylglycinonitrile (2PGN) to 2‐phenylglycine (2PG) was utilized in the hydrolysis of aminonitrile formed from benzaldehyde and KCN via 2PGN by Strecker synthesis, preferentially synthesizing (R)‐2PG with more than 95 % yield and enantiomeric excess (ee). The method was also utilized for the synthesis of (R)‐2‐phenylglycine amide ((R)‐2PGNH2) from benzaldehyde and KCN by the chemoenzymatic reaction in the presence of a mutated nitrilase AY487533W186A, which catalyzes the conversion of 2PGN to 2PGNH2.

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Section: Discussionmentioning

confidence: 99%

Retracted: Chemoenzymatic Method for Enantioselective Synthesis of (R)‐2‐Phenylglycine and (R)‐2‐Phenylglycine Amide from Benzaldehyde and KCN Using Difference of Enzyme Affinity to the Enantiomers

Kawahara

Asano

2018

ChemCatChem

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“…Up to now most published enzymatic cascades involve mainly dehydrogenases, ketoreductases, transaminases, and amino acid dehydrogenases for the production of chiral alcohols,8 amines,9 amides,10 or amino acids 11. More recently, cytochrome P450 monooxygenases, enoate reductases and Baeyer–Villiger monooxygenases have also become candidates for the implementation in synthetic cascade reactions 12.…”

Section: Introductionmentioning

confidence: 99%

Two‐Step One‐Pot Synthesis of Pinoresinol from Eugenol in an Enzymatic Cascade

et al. 2015

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The phytoestrogen pinoresinol is a high‐value compound that has a protective effect against diverse health disorders, and thus is of interest for the pharmaceutical industry. Isolation of pinoresinol from plants suffers from low yields, and its chemical synthesis involves several work‐up steps. In this study we devised a novel two‐step one‐pot enzymatic cascade combining a vanillyl‐alcohol oxidase and a laccase for the production of pinoresinol from eugenol via the intermediate coniferyl alcohol. Along with the well‐characterized vanillyl‐alcohol oxidase from Penicillium simplicissimum used to catalyze the oxidation of eugenol, enzyme screening revealed three bacterial laccases that were appropriate for the synthesis of pinoresinol from coniferyl alcohol. The cascade was optimized regarding enzyme ratios, pH value, and the presence of organic solvents. Under optimized conditions, pinoresinol concentration achieved 4.4 mM (1.6 g l−1), and this compound was isolated and analyzed.

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“…[149] HNLs and NHases and have been extensively applied in the synthesis of pharmaceuticals and even bulk chemicals. [150] Indeed, the industrial production of acrylamide by NHasecatalyzed hydration of acrylonitrile dates back to the 1980s [151] and Rhodococcus rhodochrous J1 NHase currently accounts for the production of several hundred thousand tons per annum of acrylamidew orldwide. The main advantage of the NHase process, compared to the copper-catalyzed hydration that it replaced, is the near-perfect chemoselectivity (> 99.99 %).…”

Section: Scheme16 Synthesis Of Chiral Amines Using Amine Dehydrogenamentioning

confidence: 99%

Broadening the Scope of Biocatalysis in Sustainable Organic Synthesis

2019

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This Review is aimed at synthetic organic chemists who may be familiar with organometallic catalysis but have no experience with biocatalysis, and seeks to provide an answer to the perennial question: if it is so attractive, why wasn't it extensively used in the past? The development of biocatalysis in industrial organic synthesis is traced from the middle of the last century. Advances in molecular biology in the last two decades, in particular genome sequencing, gene synthesis and directed evolution of proteins, have enabled remarkable improvements in scope and substantially reduced biocatalyst development times and cost contributions. Additionally, improvements in biocatalyst recovery and reuse have been facilitated by developments in enzyme immobilization technologies. Biocatalysis has become eminently competitive with chemocatalysis and the biocatalytic production of important pharmaceutical intermediates, such as enantiopure alcohols and amines, has become mainstream organic synthesis. The synthetic space of biocatalysis has significantly expanded and is currently being extended even further to include new‐to‐nature biocatalytic reactions.

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Enzymatic cascade synthesis of (S)-2-hydroxycarboxylic amides and acids: Cascade reactions employing a hydroxynitrile lyase, nitrile-converting enzymes and an amidase

Cited by 26 publications

References 48 publications

Retracted: Chemoenzymatic Method for Enantioselective Synthesis of (R)‐2‐Phenylglycine and (R)‐2‐Phenylglycine Amide from Benzaldehyde and KCN Using Difference of Enzyme Affinity to the Enantiomers

Retracted: Chemoenzymatic Method for Enantioselective Synthesis of (R)‐2‐Phenylglycine and (R)‐2‐Phenylglycine Amide from Benzaldehyde and KCN Using Difference of Enzyme Affinity to the Enantiomers

Two‐Step One‐Pot Synthesis of Pinoresinol from Eugenol in an Enzymatic Cascade

Broadening the Scope of Biocatalysis in Sustainable Organic Synthesis

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