Abstract
The directed evolution of ancestral -resurrected- enzymes can give a new twist in protein engineering approaches towards more versatile and robust biocatalysts.
Highlights
On the twenty-fifth anniversary of the invention of directed molecular evolution, few can doubt the power of this revolutionary method to engineer useful biomolecules at the service of mankind
There are two main currents of opinion regarding this controversial issue: (i) those who believe that the properties of the resurrected enzymes are mostly due to the accumulation of consensus/ancestor mutations, such that similar properties could be achieved by introducing such mutations into their modern counterparts; and (ii) those who believe that the properties of the resurrected enzymes are not exclusively dependent on the set of consensus/ancestor mutations but rather, they reflect the broad differences in protein sequence with respect to the extant enzymes (Cole and Gaucher, 2011; Risso et al, 2014)
While this debate remains open, paleoenzymologists are harnessing resurrected enzymes to decipher some of the principles of natural protein evolution, just as directed evolution has sometimes done with modern enzymes (Bloom and Arnold, 2009)
Summary
On the twenty-fifth anniversary of the invention of directed molecular evolution, few can doubt the power of this revolutionary method to engineer useful biomolecules at the service of mankind. Enzyme reconstruction and resurrection has recently emerged as an approach to rapidly obtain potential biocatalysts. Using phylogenetic analysis and ancestral inference algorithms, versions of ancient enzymes are being rapidly recreated.
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