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Catalytic promiscuity in Pseudomonas aeruginosa arylsulfatase as an example of chemistry-driven protein evolution
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Computational and Systems Biology.
2012 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 586, no 11, 1622-1630 p.Article in journal (Refereed) Published
Abstract [en]

In recent years, it has become increasingly clear that many enzymes are catalytically "promiscuous". This can provide a springboard for protein evolution, allowing enzymes to acquire novel functionality without compromising their native activities. We present here a detailed study of Pseudomonas aeruginosa arylsulfatase (PAS), which catalyzes the hydrolysis of a number of chemically distinct substrates, with proficiencies comparable to that towards its native reaction. We demonstrate that the main driving force for the promiscuity is the ability to exploit the electrostatic preorganization of the active site for the native substrate, providing an example of chemistry-driven protein evolution.

Place, publisher, year, edition, pages
2012. Vol. 586, no 11, 1622-1630 p.
Keyword [en]
Enzyme catalysis, Empirical valence bond, Phosphoryl transfer, Sulfuryl transfer, Electrostatic reorganization
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-176203DOI: 10.1016/j.febslet.2012.04.012ISI: 000304472300010OAI: oai:DiVA.org:uu-176203DiVA: diva2:535316
Funder
Swedish Research Council, 2010-5026Swedish National Infrastructure for Computing (SNIC), 002/12-26
Available from: 2012-06-19 Created: 2012-06-18 Last updated: 2017-12-07Bibliographically approved

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