Studying the evolutionary potential of ancestral aryl sulfatases in the alkaline phosphatase family with droplet microfluidics.

ABSTRACT: Characterizing the dynamics and functional shifts during protein evolution is essential, both for understanding protein evolution and for rationalizing efficient strategies for e.g. enzymes with desired and effective functions. Most proteins organize in families, sets of divergent sequences which share a common ancestor and have a similar structural fold. Here, we study aryl sulfatases, a subfamily of the large and evolutionary old alkaline phosphatase superfamily. We demonstrate how ultrahigh-throughput droplet microfluidics can be used for studying aryl sulfatases and their computationally reconstructed putative common ancestors. We compare the evolvability and robustness of three ancestors and three extant aryl sulfatases which all exhibit catalytic promiscuity towards a range of

SUBMITTER: Eenink BDG 

PROVIDER: S-EPMC12917725 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature