Article
Adaptive laboratory evolution recruits the promiscuity of succinate semialdehyde dehydrogenase to repair different metabolic deficiencies.
Nature communications - 15 Oct 2024
He Hai, Gómez-Coronado Paul A, Zarzycki Jan, Barthel Sebastian, Kahnt Jörg, Claus Peter, Klein Moritz, Klose Melanie, de Crécy-Lagard Valérie, Schindler Daniel, Paczia Nicole, Glatter Timo, Erb Tobias J
Abstract excerpt
Promiscuous enzymes often serve as the starting point for the evolution of novel functions. Yet, the extent to which the promiscuity of an individual enzyme can be harnessed several times independently for different purposes during evolution is poorly reported. Here, we present a case study illustrating how NAD(P)+-dependent succinate semialdehyde dehydrogenase of Escherichia coli (Sad) is independently recruited...
Topics
- Succinate-Semialdehyde Dehydrogenase
- Escherichia coli
- Pyridoxal Phosphate
- Directed Molecular Evolution
- Catalytic Domain
- Glycolysis
- Escherichia coli Proteins
- Mutation
- Evolution, Molecular