Active Site Hydrophobicity and the Convergent Evolution of Paraoxonase Activity in Structurally Divergent Enzymes: The Case of Serum Paraoxonase 1
Author:
Affiliation:
1. Science for Life Laboratory, Department of Cell and Molecular Biology, Uppsala University, S-751 24 Uppsala, Sweden
2. Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel
Funder
European Research Council
Royal Swedish Academy of Sciences
Knut och Alice Wallenbergs Stiftelse
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
http://pubs.acs.org/doi/pdf/10.1021/jacs.6b10801
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1. Enzyme Promiscuity: A Mechanistic and Evolutionary Perspective
2. An evolutionary biochemist's perspective on promiscuity
3. Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer
4. Structure−Reactivity Studies of Serum Paraoxonase PON1 Suggest that Its Native Activity Is Lactonase
5. Enhanced stereoselective hydrolysis of toxic organophosphates by directly evolved variants of mammalian serum paraoxonase
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