Article
Active Site Hydrophobicity and the Convergent Evolution of Paraoxonase Activity in Structurally Divergent Enzymes: The Case of Serum Paraoxonase 1.
Journal of the American Chemical Society - 25 Jan 2017
Blaha-Nelson David, Krüger Dennis M, Szeler Klaudia, Ben-David Moshe, Kamerlin Shina Caroline Lynn
Abstract excerpt
Serum paraoxonase 1 (PON1) is a native lactonase capable of promiscuously hydrolyzing a broad range of substrates, including organophosphates, esters, and carbonates. Structurally, PON1 is a six-bladed β-propeller with a flexible loop (residues 70-81) covering the active site. This loop contains a functionally critical Tyr at position 71. We have performed detailed experimental and computational analyses of the...
Topics
- Aryldialkylphosphatase
- Binding Sites
- Biocatalysis
- Humans
- Hydrolysis
- Hydrophobic and Hydrophilic Interactions
- Lactones
- Molecular Dynamics Simulation
- Mutation
- Paraoxon