Promiscuity and electrostatic flexibility in the alkaline phosphatase superfamily
2016 (English)In: Current opinion in structural biology, ISSN 0959-440X, E-ISSN 1879-033X, Vol. 37, 14-21 p.Article in journal (Refereed) PublishedText
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.
Place, publisher, year, edition, pages
2016. Vol. 37, 14-21 p.
Biochemistry and Molecular Biology Cell Biology
IdentifiersURN: urn:nbn:se:uu:diva-297375DOI: 10.1016/j.sbi.2015.11.008ISI: 000375163000005PubMedID: 26716576OAI: oai:DiVA.org:uu-297375DiVA: diva2:941666
FunderEU, FP7, Seventh Framework Programme, 306474