Cover Feature: Expanding the Substrate Scope of Native Amine Dehydrogenases through In Silico Structural Exploration and Targeted Protein Engineering (ChemCatChem 22/2022)

The Cover Feature shows the active site of an amine dehydrogenase (AmDH), an enzyme which catalyzes the transformation of ketones into chiral amines.  The protein has been modified by protein engineering, creating a variant that can synthesizee longer amines than the wild‐type. In their Research Art...

Full description

Saved in:
Bibliographic Details
Published in:ChemCatChem 2022-11, Vol.14 (22), p.n/a
Main Authors: Ducrot, Laurine, Bennett, Megan, André‐Leroux, Gwenaëlle, Elisée, Eddy, Marynberg, Sacha, Fossey‐Jouenne, Aurélie, Zaparucha, Anne, Grogan, Gideon, Vergne‐Vaxelaire, Carine
Format: Article
Language:English
Subjects:
molecular dynamics
native amine dehydrogenases
protein engineering
reductive amination
structural biodiversity
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The Cover Feature shows the active site of an amine dehydrogenase (AmDH), an enzyme which catalyzes the transformation of ketones into chiral amines.  The protein has been modified by protein engineering, creating a variant that can synthesizee longer amines than the wild‐type. In their Research Article, C. Vergne‐Vaxelaire and co‐workers explain how, inspired by natural sequence biodiversity, the key amino acids of different enzymes active sites have been selected and then mutated into less bulky residues, successfully leading to variants that are able to transform unprecedented bulky aldehydes and ketones into amines.  The improved performance of the variants has been investigated using both X‐ray crystal structures and molecular studies, helping to inform further engineering of these important sustainable tools for amine synthesis. The credit for the picture belongs to Kim‐Beverly Ajavon and Laurine Ducrot. More information can be found in the Research Article by C. Vergne‐Vaxelaire and co‐workers.
ISSN:1867-3880
1867-3899
DOI:10.1002/cctc.202201257