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Promiscuity and electrostatic flexibility in the alkaline phosphatase superfamily
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology.
2016 (English)In: Current opinion in structural biology, ISSN 0959-440X, E-ISSN 1879-033X, Vol. 37, 14-21 p.Article in journal (Refereed) Published
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Abstract [en]

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.
National Category
Biochemistry and Molecular Biology Cell Biology
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URN: urn:nbn:se:uu:diva-297375DOI: 10.1016/j.sbi.2015.11.008ISI: 000375163000005PubMedID: 26716576OAI: oai:DiVA.org:uu-297375DiVA: diva2:941666
Funder
EU, FP7, Seventh Framework Programme, 306474
Available from: 2016-06-22 Created: 2016-06-22 Last updated: 2017-11-28Bibliographically approved

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Pabis, AnnaKamerlin, Shina Caroline Lynn

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