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Retracing Enzyme Evolution in the ( βα ) 8 ‐Barrel Scaffold
Author(s) -
Stevenson James D.,
Lutz Stefan,
Benkovic Stephen J.
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20010518)40:10<1854::aid-anie1854>3.0.co;2-f
Subject(s) - scaffold , directed evolution , scaffold protein , barrel (horology) , enzyme , chemistry , protein engineering , catalysis , directed molecular evolution , nanotechnology , enzyme catalysis , combinatorial chemistry , biophysics , biochemistry , materials science , computer science , biology , signal transduction , database , mutant , gene , composite material
“Refitting” existing protein scaffolds to generate new enzymes with designed properties is a powerful tool in molecular evolution. Two recently published reports demonstrate the engineering of the ubiquitous ( βα ) 8 ‐barrel (see picture) scaffold to obtain new enzymatic catalysts with altered binding and catalytic properties. These are the first examples of the conversion of one enzyme's activity into that of another by using directed evolution.