Special Issue "Catalyzed Synthesis of Chiral Amines"

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Catalysis in Organic and Polymer Chemistry".

Deadline for manuscript submissions: 31 December 2019.

Special Issue Editors

Guest Editor
Prof. Hyungdon Yun Website E-Mail
Department of Systems Biotechnology, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul 05029, Korea
Interests: enzyme engineering; biocatalysis and biotransformation; synthetic biology; unnatural amino acid mutagenesis
Guest Editor
Dr. Mahesh D. Patil Website E-Mail
Department of Systems Biotechnology, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul 05029, Korea
Interests: biocatalysis and biotransformations; bioprocess technology; downstream processing; enzyme immobilization

Special Issue Information

Dear Colleagues,

Chiral amines are valuable constituents of many important pharmaceutical compounds or their intermediates. It is estimated that nearly 50% of pharmaceutical drugs contain chiral amine scaffolds in their structures. The requisite amines are scarce in nature, and their industrial production mainly relies on the metal-catalysed, traditional organic synthesis. On the other hand, tremendous advancements in biocatalytic methods for chiral amines have been achieved during the last decades. Enzyme catalysis provides green and selective tools for the enantioselective synthesis of chiral amines.

This Special Issue aims to cover recent updates and novel trends in the synthesis of chiral amines. We invite the scientific community to submit their contributions in the form of original research papers and review articles that provide new insights and emphasize aspects of fundamental and applied research areas.

Contributions should be related, but not limited, to the following:

  • Green synthesis of chiral amines
  • Discovery of novel bicayalysts and/or engineering of known biocatalysts
  • Development and application of novel immobilized biocatalysts
  • Design and construction of new whole-cell biocatalysts
  • Novel catalytic reactions for the synthesis of chiral amines.

Prof. Hyungdon Yun
Dr. Mahesh D. Patil
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Chiral amines
  • Biocatalysis
  • Whole-cell biotransformations
  • Immobilized enzymes
  • Protein engineering
  • Catalysis
  • Synthetic biology
  • Cascade reactions

Published Papers (1 paper)

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Research

Open AccessArticle
Kinetic Resolution of Racemic Amines to Enantiopure (S)-amines by a Biocatalytic Cascade Employing Amine Dehydrogenase and Alanine Dehydrogenase
Catalysts 2019, 9(7), 600; https://doi.org/10.3390/catal9070600 - 12 Jul 2019
Abstract
Amine dehydrogenases (AmDHs) efficiently catalyze the NAD(P)H-dependent asymmetric reductive amination of prochiral carbonyl substrates with high enantioselectivity. AmDH-catalyzed oxidative deamination can also be used for the kinetic resolution of racemic amines to obtain enantiopure amines. In the present study, kinetic resolution was carried [...] Read more.
Amine dehydrogenases (AmDHs) efficiently catalyze the NAD(P)H-dependent asymmetric reductive amination of prochiral carbonyl substrates with high enantioselectivity. AmDH-catalyzed oxidative deamination can also be used for the kinetic resolution of racemic amines to obtain enantiopure amines. In the present study, kinetic resolution was carried out using a coupled-enzyme cascade consisting of AmDH and alanine dehydrogenase (AlaDH). AlaDH efficiently catalyzed the conversion of pyruvate to alanine, thus recycling the nicotinamide cofactors and driving the reaction forward. The ee values obtained for the kinetic resolution of 25 and 50 mM rac-α-methylbenzylamine using the purified enzymatic systems were only 54 and 43%, respectively. The use of whole-cells apparently reduced the substrate/product inhibition, and the use of only 30 and 40 mgDCW/mL of whole-cells co-expressing AmDH and AlaDH efficiently resolved 100 mM of rac-2-aminoheptane and rac-α-methylbenzylamine into the corresponding enantiopure (S)-amines. Furthermore, the applicability of the reaction protocol demonstrated herein was also successfully tested for the efficient kinetic resolution of wide range of racemic amines. Full article
(This article belongs to the Special Issue Catalyzed Synthesis of Chiral Amines)
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