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Cover Feature: Generation of Oxidoreductases with Dual Alcohol Dehydrogenase and Amine Dehydrogenase Activity (Chem. Eur. J. 10/2021)
Author(s) -
Tseliou Vasilis,
Schilder Don,
Masman Marcelo F.,
Knaus Tanja,
Mutti Francesco G.
Publication year - 2021
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202004194
Subject(s) - alcohol dehydrogenase , oxidative deamination , benzylamine , chemistry , amine gas treating , enzyme , alcohol , biochemistry , benzyl alcohol , deamination , dehydrogenase , stereochemistry , catalysis , organic chemistry
The catalytic promiscuity of LysEDH —which naturally catalyzes the oxidative deamination of l ‐lysine at the ϵ‐amino group—was harnessed to create variants that exhibited alcohol dehydrogenase (ADH) and amine dehydrogenase (AmDH) activities. These ADH and AmDH activities could be switched by changing the reaction conditions. The dual ADH‐AmDH activity (i.e., alcohol aminase) was applied to convert benzyl alcohol to benzylamine using a single enzyme. The artwork illustrates a “water lever” that represents the switch of the enzyme's activity from an AmDH to an ADH and vice versa. More information can be found in the Full Paper by F. G. Mutti et al. on page 3315.