Title

Cover Feature: Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity (Chem. Eur. J. 10/2021).

Authors

Tseliou, Vasilis; Schilder, Don; Masman, Marcelo F.; Knaus, Tanja; Mutti, Francesco G.

Abstract

Alcohol amination, alcohol dehydrogenases, amine dehydrogenases, biocatalysis, enzyme promiscuity Keywords: alcohol amination; alcohol dehydrogenases; amine dehydrogenases; biocatalysis; enzyme promiscuity EN alcohol amination alcohol dehydrogenases amine dehydrogenases biocatalysis enzyme promiscuity 3188 3188 1 02/17/21 20210215 NES 210215 B The catalytic promiscuity of LysEDH b - which naturally catalyzes the oxidative deamination of l-lysine at the -amino group - was harnessed to create variants that exhibited alcohol dehydrogenase (ADH) and amine dehydrogenase (AmDH) activities. The dual ADH-AmDH activity (i.e., alcohol aminase) was applied to convert benzyl alcohol to benzylamine using a single enzyme.

Subjects

ALCOHOL dehydrogenase; AMINES; OXIDOREDUCTASES; DEHYDROGENASES; BENZYL alcohol; BIOCATALYSIS

Publication

Chemistry - A European Journal, 2021, Vol 27, Issue 10, p3188

ISSN

0947-6539

Publication type

Academic Journal

DOI

10.1002/chem.202004194