Issue 95, 2014
From the journal:

Chemical Communications

A novel chimeric amine dehydrogenase shows altered substrate specificity compared to its parent enzymes†

Bettina R. Bommarius,a   Martin Schürmannb  and  Andreas S. Bommarius*ac  

* Corresponding authors

a Georgia Institute of Technology, School of Chemical & Biomolecular Engineering, Parker H. Petit Building, 315 Ferst Drive, Atlanta, GA 30332-0100, USA
E-mail: andreas.bommarius@chbe.gatech.edu

b DSM Innovative Synthesis BV, PO Box 18, MD Geleen, Netherlands

c Georgia Institute of Technology, School of Chemistry and Biochemistry, 95 Atlantic Ave., Atlanta, GA 30332-0420, USA

Abstract

We created a novel chimeric amine dehydrogenase (AmDH) via domain shuffling of two parent AmDHs (‘L- and F-AmDH’), which in turn had been generated from leucine and phenylalanine DH, respectively. Unlike the parent proteins, the chimeric AmDH (‘cFL-AmDH’) catalyzes the amination of acetophenone to (R)-methylbenzylamine and adamantylmethylketone to adamantylethylamine.

Graphical abstract: A novel chimeric amine dehydrogenase shows altered substrate specificity compared to its parent enzymes

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Article information

DOI
https://doi.org/10.1039/C4CC06527A
Article type
Communication
Submitted
19 Aug 2014
Accepted
10 Oct 2014
First published
10 Oct 2014

Chem. Commun., 2014,50, 14953-14955

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A novel chimeric amine dehydrogenase shows altered substrate specificity compared to its parent enzymes

B. R. Bommarius, M. Schürmann and A. S. Bommarius, Chem. Commun., 2014, 50, 14953 DOI: 10.1039/C4CC06527A

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