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Cover Feature: Tuning the Product Spectrum of a Glycoside Hydrolase Enzyme by a Combination of Site‐Directed Mutagenesis and Tyrosine‐Specific Chemical Modification (Chem. Eur. J. 26/2019)
Author(s) -
Ertl Julia,
OrtizSoto Maria Elena,
Le Thien Anh,
Bechold Julian,
Shan Junwen,
Teßmar Jörg,
Engels Bernd,
Seibel Jürgen
Publication year - 2019
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201901004
Subject(s) - bioconjugation , tyrosine , chemical modification , biocatalysis , chemistry , mutagenesis , enzyme , glycoside hydrolase , cover (algebra) , site directed mutagenesis , product (mathematics) , biochemistry , active site , protein engineering , combinatorial chemistry , stereochemistry , mutation , engineering , gene , mathematics , reaction mechanism , mechanical engineering , geometry , mutant , catalysis
Selective chemical modification of proteins is a powerful tool for the rational design of enzymes. This work shows a combination of genetic and chemical engineering of a biocatalyst by conducting a tyrosine‐specific modification at introduced tyrosine residues. This method enables a systematic tuning of the enzymes’ functionalities and allows control of the product synthesis. Depending on the selected position for the bioconjugation, completely different product spectra are obtained. More information can be found in the Full Paper by J. Seibel et al. on page 6533.