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Issue 95, 2014
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A novel chimeric amine dehydrogenase shows altered substrate specificity compared to its parent enzymes

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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


Submitted
19 Aug 2014
Accepted
10 Oct 2014
First published
10 Oct 2014

Chem. Commun., 2014,50, 14953-14955
Article type
Communication

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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