A Novel Chimeric Amine Dehydrogenase Shows Altered Substrate Specificity Compared to Its Parent Enzymes

Overview

Journal Chem Commun (Camb)

Publisher Royal Society of Chemistry

Specialty Chemistry

Date 2014 Oct 28

PMID 25347124

Citations 23

Authors

Bettina R Bommarius

Martin Schurmann

Andreas S Bommarius

Affiliations

Soon will be listed here.

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.

Citing Articles

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Enzymatic Routes for Chiral Amine Synthesis: Protein Engineering and Process Optimization.

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High coenzyme affinity chimeric amine dehydrogenase based on domain engineering.

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One-Pot Biocatalytic Synthesis of Primary, Secondary, and Tertiary Amines with Two Stereocenters from α,β-Unsaturated Ketones Using Alkyl-Ammonium Formate.

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High-Yield Synthesis of Enantiopure 1,2-Amino Alcohols from l-Phenylalanine via Linear and Divergent Enzymatic Cascades.

Corrado M, Knaus T, Schwaneberg U, Mutti F Org Process Res Dev. 2022; 26(7):2085-2095.

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