The diversity of enzyme catalytic function is remarkable, particularly when one considers that ancestral life forms must have started with a much smaller ensemble of proteins. In this article, we discuss the evolution of the mandelate pathway in pseudomonads as an example of how catalytic diversity may have evolved. We suggest that existing enzymes that catalyse the chemistry needed to accomplish a transformation were recruited, followed by the evolution of specific binding.
|Original language||English (US)|
|Number of pages||5|
|Journal||Trends in Biochemical Sciences|
|State||Published - Oct 1993|
ASJC Scopus subject areas
- Molecular Biology