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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 (ChemBioChem 4/2013)
Author(s) -
Timms Nicole,
Windle Claire L.,
Polyakova Anna,
Ault James R.,
Trinh Chi H.,
Pearson Arwen R.,
Nelson Adam,
Berry Alan
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201390008
Subject(s) - lyase , aldolase a , chemistry , mutagenesis , biochemistry , active site , lysine , enzyme , cover (algebra) , site directed mutagenesis , combinatorial chemistry , stereochemistry , amino acid , mutation , mutant , gene , mechanical engineering , engineering
The cover picture shows an artist's impression of the substrate approaching the (β/α) 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 p K a of thialysine compared to lysine. The study opens the way to tailored novel enzymes containing unnatural amino acids.