title: Promiscuity and electrostatic flexibility in the alkaline phosphatase superfamily.
abstract: Catalytic promiscuity, that is, the ability of single enzymes to facilitate the turnover of multiple, chemically distinct substrates, is a widespread phenomenon that plays an important role in the evolution of enzyme function. Additionally, such pre-existing multifunctionality can be harnessed in artificial enzyme design. The members of the alkaline phosphatase superfamily have served extensively as both experimental and computational model systems for enhancing our understanding of catalytic promiscuity. In this Opinion, we present key recent computational studies into the catalytic activity of these highly promiscuous enzymes, highlighting the valuable insight they have provided into both the molecular basis for catalytic promiscuity in general, and its implications for the evolution of phosphatase activity.
authors.affiliation: Science for Life Laboratory, Department of Cell and Molecular Biology, Uppsala University, BMC Box 596, S-751 24 Uppsala, Sweden.
authors.forename: Anna
authors.initials: A
authors.lastname: Pabis
authors.affiliation: Science for Life Laboratory, Department of Cell and Molecular Biology, Uppsala University, BMC Box 596, S-751 24 Uppsala, Sweden. Electronic address: kamerlin@icm.uu.se.
authors.forename: Shina Caroline Lynn
authors.initials: SC
authors.lastname: Kamerlin
mesh_terms: D000469:Alkaline Phosphatase / Q000737:chemistry* / Q000378:metabolism; D002384:Catalysis; D020134:Catalytic Domain; D055672:Static Electricity; D013329:Structure-Activity Relationship
chemical_list: D000469:Alkaline Phosphatase