Premium
ATP Regeneration System in Chemoenzymatic Amide Bond Formation with Thermophilic CoA Ligase
Author(s) -
Lelièvre Chloé M.,
Balandras Mélanie,
Petit JeanLouis,
VergneVaxelaire Carine,
Zaparucha Anne
Publication year - 2020
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201901870
Subject(s) - amide , chemistry , dna ligase , thermophile , adenylate kinase , yield (engineering) , enzyme , coenzyme a , biochemistry , combinatorial chemistry , stereochemistry , materials science , reductase , metallurgy
CoA ligases are enzymes catalyzing the ATP‐dependent addition of coenzyme A to carboxylic acids in two steps through an adenylate intermediate. This intermediate can be diverted by a nucleophilic non enzymatic addition of amine to get the corresponding amide for synthetic purposes. To this end, we selected thermophilic CoA ligases to study the conversion of various carboxylic acids into their amide counterparts. To limit the use of ATP, we implemented an ATP regeneration system combining polyphosphate kinase 2 (PPK2 Class III) and inorganic pyrophosphatase. Suitability of this system was illustrated by the lab‐scale chemoenzymatic synthesis of N ‐methylbutyrylamide in 77 % yield using low enzyme loading and 5 % molar ATP.