Article
Intracellular complexities of acquiring a new enzymatic function revealed by mass-randomisation of active-site residues.
eLife - 13 Nov 2020
Hall Kelsi R, Robins Katherine J, Williams Elsie M, Rich Michelle H, Calcott Mark J, Copp Janine N, Little Rory F, Schwörer Ralf, Evans Gary B, Patrick Wayne M, Ackerley David F
Abstract excerpt
Selection for a promiscuous enzyme activity provides substantial opportunity for competition between endogenous and newly-encountered substrates to influence the evolutionary trajectory, an aspect that is often overlooked in laboratory directed evolution studies. We selected the Escherichia coli nitro/quinone reductase NfsA for chloramphenicol detoxification by simultaneously randomising eight active-site...
Topics
- Catalytic Domain
- Chloramphenicol
- Escherichia coli
- Escherichia coli Proteins
- Evolution, Molecular
- Inactivation, Metabolic
- Mutation
- Nitroreductases
- Protein Conformation
- Structure-Activity Relationship