One-pot one-step deracemization of amines using ω-transaminases

Shin, Giyoung; Mathew, Sam; Shon, Minsu; Kim, Byung‐Gee; Yun, Hyungdon

doi:10.1039/c3cc43348j

Cited by 61 publications

(46 citation statements)

References 28 publications

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“…Each enantiomer was separated by these analytical conditions except a6 and a12. A quantitative chiral analysis of a6 and a12 was performed using a C18 symmetry column (Waters, Milford, MA, USA) with a Waters HPLC system at 254 nm after the derivatization of the sample with GITC [33]. The separation of each enantiomer of a6 and a12 was achieved through isocratic elution with a mixture of 50% methanol and 50% water (0.1% TFA) at a flow rate of 1.0 mL min −1 .…”

Section: Analysis Of Aminesmentioning

confidence: 99%

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The Kinetic Resolution of Racemic Amines Using a Whole-Cell Biocatalyst Co-Expressing Amine Dehydrogenase and NADH Oxidase

et al. 2017

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Amine dehydrogenase (AmDH) possesses tremendous potential for the synthesis of chiral amines because AmDH catalyzes the asymmetric reductive amination of ketone with high enatioselectivity. Although a reductive application of AmDH is favored in practice, the oxidative route is interesting as well for the preparation of chiral amines. Here, the kinetic resolution of racemic amines using AmDH was first extensively studied, and the AmDH reaction was combined with an NADH oxidase (Nox) to regenerate NAD + and to drive the reaction forward. When the kinetic resolution was carried out with 10 mM rac-2-aminoheptane and 5 mM rac-α-methylbenzylamine (α-MBA) using purified enzymes, the enantiomeric excess (ee) values were less than 26% due to the product inhibition of AmDH by ketone and the inhibition of Nox by the substrate amine. The use of a whole-cell biocatalyst co-expressing AmDH and Nox apparently reduces the substrate and product inhibition, and/or it increases the stability of the enzymes. Fifty millimoles (50 mM) rac-2-aminoheptane and 20 mM rac-α-MBA were successfully resolved into the (S)-form with >99% ee using whole cells. The present study demonstrates the potential of a whole-cell biocatalyst co-expressing AmDH and Nox for the kinetic resolution of racemic amines.

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Section: Analysis Of Aminesmentioning

confidence: 99%

“…The conversion and ee analysis of amines were performed by HPLC using a Crownpak CR (Daicel Co., Osaka, Japan) column at 210 nm with elution with a perchloric acid solution of pH 1.5 (0.6 mL min −1 ) [33]. Each enantiomer was separated by these analytical conditions except a6 and a12.…”

Section: Analysis Of Aminesmentioning

confidence: 99%

The Kinetic Resolution of Racemic Amines Using a Whole-Cell Biocatalyst Co-Expressing Amine Dehydrogenase and NADH Oxidase

et al. 2017

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“…Yun and co-workers have recently used this approach in a one-pot one-step fashion to deracemize aromatic primary amines, using . [104] This method enabled the synthesis of the (R)-antipodes in good conversions (70-99%) and excellent ee values (up to >99%). The key of this strategy was the use of an amino acceptor (α-ketoglutaric acid), that was not a good substrate for the second TA.…”

Section: Using Two Transaminasesmentioning

confidence: 98%

“…Deracemization of racemic primary amines using two stereocomplementary TAs. [104] Using an oxidase and a dehydrogenase…”

Section: Using Two Transaminasesmentioning

confidence: 99%

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

Díaz‐Rodríguez¹,

Lavandera

Gotor³

2015

CGC

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Abstract. In recent years the usefulness of enzymatic systems to obtain a single stereoisomerically pure compound starting from a racemate has been expanded. Moreover, current advances in protein engineering, molecular biology and modeling tools are the basis to improve the catalytic properties of enzymes to face novel synthetic challenges. Also, medium engineering and novel immobilization methods of (bio)catalysts are enhancing the productivity of biocatalytic processes making them suitable for being scalable. The development of multienzymatic protocols and the combination of enzymes with other catalysts are providing a wide range of synthetic possibilities that are expanding the scope of these transformations even at industrial scale. Herein we will describe an overview of recent (chemo)enzymatic deracemizations, focusing on the strategy employed (dynamic kinetic resolution, stereoinversion, cyclic deracemization or enantioconvergent process), the type of substrate (e.g., alcohols, amines, carboxylic acid derivatives or carbonylic compounds), and the biocatalyst(s) used.

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“…v-TA belongs to a class of TAs that reversibly transfers an amino group from an amino donor to the non-alpha position of the amino acceptor and yield an a-keto acid, facilitated by a coenzyme pyridoxal 5 0 -phosphate hydrate PLP [4]. Enantiomerically pure amines can be produced via three reaction schemes using v-TA: (i) asymmetric synthesis from prochiral ketones, (ii) kinetic resolution and (iii) deracemization [4,16]. In principle, both enantiomers of a given amine can be obtained with a single enantioslective v-TA having, for instance, (S)-enaniopreference.…”

Section: Introductionmentioning

confidence: 99%

Kinetic resolution of amines by (R)-selective omega-transaminase from Mycobacterium vanbaalenii

Shin

Mathew

Yun

2015

Journal of Industrial and Engineering Chemistry

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One-pot one-step deracemization of amines using ω-transaminases

Abstract: In this study, we developed a one-pot one-step deracemization method for the production of various enantiomerically pure amines using two opposite enantioselective ω-TAs. Using this method, various aromatic amines were successfully converted to their (R)-forms (>99%) with good conversion.

Cited by 61 publications

References 28 publications

The Kinetic Resolution of Racemic Amines Using a Whole-Cell Biocatalyst Co-Expressing Amine Dehydrogenase and NADH Oxidase

The Kinetic Resolution of Racemic Amines Using a Whole-Cell Biocatalyst Co-Expressing Amine Dehydrogenase and NADH Oxidase

Why Leave a Job Half Done? Recent Progress in Enzymatic Deracemizations

Kinetic resolution of amines by (R)-selective omega-transaminase from Mycobacterium vanbaalenii

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