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An efficient single-enzymatic cascade for asymmetric synthesis of chiral amines catalyzed by omega-transaminase
KTH, School of Biotechnology (BIO), Biochemistry.
KTH, School of Biotechnology (BIO), Biochemistry.ORCID iD: 0000-0003-3073-5641
KTH, School of Biotechnology (BIO), Biochemistry.ORCID iD: 0000-0002-9577-832X
2013 (English)In: Chemical Communications, ISSN 1359-7345, E-ISSN 1364-548X, Vol. 49, no 2, 161-163 p.Article in journal (Refereed) Published
Abstract [en]

An efficient single-enzymatic cascade approach for the asymmetric synthesis of chiral amines has been developed, which applies the amino donor 3-aminocyclohexa-1,5-dienecarboxylic acid spontaneously tautomerizing to reach reaction completion with excellent ee values.

Place, publisher, year, edition, pages
2013. Vol. 49, no 2, 161-163 p.
Keyword [en]
Optically-Active Amines, Amination, Coli
National Category
Biological Sciences Other Chemistry Topics
URN: urn:nbn:se:kth:diva-109597DOI: 10.1039/c2cc37232kISI: 000311938800014OAI: diva2:584380

QC 20130109

Available from: 2013-01-09 Created: 2013-01-08 Last updated: 2016-10-17Bibliographically approved
In thesis
1. Amine Transaminases in Biocatalytic Amine Synthesis
Open this publication in new window or tab >>Amine Transaminases in Biocatalytic Amine Synthesis
2016 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The use of enzymes, nature´s own catalysts, both isolated or as whole cells to perform chemical transformations is called biocatalysis. As a complement to classical chemical catalysis, biocatalysis can be an environmentally friendly and more economical option in the production and synthesis of chemicals. Research on the application of amine transaminases in synthesis of chiral amines have exploded over the last two decades and interest from the industry is increasing. Amine transaminases are promising catalysts due to their ability to perform reductive amination of ketones with excellent enantioselectivity.

For a process to be efficient, high substrate specificity of the applied enzyme is an important factor. A variant of Chromobacterium violaceum amine transaminase that was obtained through rational design has an increased specific activity toward (S)-1-phenylethylamine and a set of 4´-substituted acetophenones. This result makes this variant a promising catalyst for the asymmetric synthesis of similar amines.

Amine transaminase catalyzed asymmetric synthesis of amines generally suffers from unfavorable equilibrium. Two methods that include spontaneous tautomerization and biocatalytic amidation for equilibrium displacement have therefore been developed.

Efficient assays and screening methods are demanded for the discovery and development of novel amine transaminases. For this purpose, a sensitive fluorescence-based assay that holds promise as a high-throughput screening method was developed.

One of the major obstacles for application of enzymes in industrial processes is the instability of the enzyme toward harsh conditions. The stability of Chromobacterium violaceum amine transaminase was investigated and improved using co-solvents and other additives. Co-lyophilization with surfactants was also applied to improve the performance of the same enzyme in organic solvents.

Place, publisher, year, edition, pages
Stockholm: Henrik Land, 2016. 101 p.
TRITA-BIO-Report, ISSN 1654-2312 ; 2016:18
Amine Transaminase, Biocatalysis, Transamination, Reductive Amination, Enzyme, Enzyme Engineering, Equilibrium Displacement, Screening, Enzyme Stability
National Category
Biochemistry and Molecular Biology
Research subject
urn:nbn:se:kth:diva-194112 (URN)978-91-7729-164-0 (ISBN)
Public defence
2016-11-25, Kollegiesalen, Brinellvägen 8, Stockholm, 10:00 (English)

QC 20161017

Available from: 2016-10-17 Created: 2016-10-17 Last updated: 2016-10-17Bibliographically approved

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