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Cover Picture: Structural Insights into the Recovery of Aldolase Activity in N-Acetylneuraminic Acid Lyase by Replacement of the Catalytically Active Lysine with γ-Thialysine by Using a Chemical Mutagenesis Strategy

DOI: 10.1002/cbic.201390008 DOI Help

Authors: Nicole Timms (University of Leeds) , Claire Windle (University of Leeds) , Anna Polyakova (University of Leeds) , James R. Ault (University of Leeds) , Chi Hung Trinh (Institute of Molecular and Cellular Biology, University of Leeds) , Arwen Pearson (University of Leeds) , Adam Nelson (University of Leeds) , Alan Berry (University of Leeds)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Chembiochem , VOL 14 (4) , PAGES 401 - 401

State: Published (Approved)
Published: March 2013
Diamond Proposal Number(s): 8367

Abstract: The cover picture shows an artist's impression of the substrate approaching the (?/?)8-barrel enzyme, N-acetylneuraminic acid lyase engineered to contain an unnatural amino acid in the active site. The unnatural amino acid, thialysine (highlighted), is introduced by chemical modification. On p. 474 ff., A. Berry et al. explain how X-ray structural studies and kinetic characterization show that the unnatural amino acid mimics the shape and positioning of the natural lysine at this site, but lower activity is regained because of the difference in the pKa of thialysine compared to lysine. The study opens the way to tailored novel enzymes containing unnatural amino acids.

Journal Keywords: Aldolases; Enzyme Catalysis; N-Acetylneuraminic Acid Lyase; Thialysine; Unnatural Amino Acids

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

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