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Selection of a promiscuous minimalist cAMP phosphodiesterase from a library of de novo designed proteins

Biology

Selection of a promiscuous minimalist cAMP phosphodiesterase from a library of de novo designed proteins

J. D. Schnettler, M. S. Wang, et al.

This groundbreaking research by J. David Schnettler and colleagues delves into how new enzyme functions can emerge from unevolved sequences. Utilizing ultrahigh-throughput droplet microfluidics, the study screens an impressive library of over one million proteins, uncovering that significant sequence changes can lead to the acquisition of activity in a newly characterized manganese-dependent metalloenzyme.

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