Abstract
The EBG system of E. coli has served as a model for the evolution of novel functions. This paper reviews the experimental evolution of the catabolism of ß-galactoside sugars in strains of E. coli that carry deletions of the classical lacZ ß-galactosidase gene. Evolution of the ebgA encoded Ebg ß-galactosidase for an expanded substrate range, evolution of the ebgR encoded Ebg repressor for sensitivity to an expanded range of inducers, the amino acid replacements responsible for those changes, and the evolutionary potential of the system are discussed. The EBG system has also served as a model for studying the detailed catalytic consequences of experimental evolution at the physical-chemical level. The analysis of free-energy profiles for the wildtype and all of the various evolved Ebg enzymes has permitted rejection of the Albery-Knowles hypothesis that relates likely changes in free-energy profiles to evolutionary change.
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Hall, B.G. (2003). The EBG system of E. coli: origin and evolution of a novel ß-galactosidase for the metabolism of lactose. In: Long, M. (eds) Origin and Evolution of New Gene Functions. Contemporary Issues in Genetics and Evolution, vol 10. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-0229-5_5
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DOI: https://doi.org/10.1007/978-94-010-0229-5_5
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