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Establishing wild-type levels of catalytic activity on natural and artificial (βα)8-barrel protein scaffolds

Titelangaben

Claren, Jörg ; Malisi, Christoph ; Höcker, Birte ; Sterner, Reinhard:
Establishing wild-type levels of catalytic activity on natural and artificial (βα)8-barrel protein scaffolds.
In: Proceedings of the National Academy of Sciences of the United States of America. Bd. 106 (2009) Heft 10 . - S. 3704-3709.
ISSN 1091-6490
DOI: https://doi.org/10.1073/pnas.0810342106

Abstract

The generation of high levels of new catalytic activities on natural and artificial protein scaffolds is a major goal of enzyme engineering. Here, we used random mutagenesis and selection in vivo to establish a sugar isomerisation reaction on both a natural (beta alpha)(8)-barrel enzyme and a catalytically inert chimeric (beta alpha)(8)-barrel scaffold, which was generated by the recombination of 2 (beta alpha)(4)-half barrels. The best evolved variants show turnover numbers and substrate affinities that are similar to those of wild-type enzymes catalyzing the same reaction. The determination of the crystal structure of the most proficient variant allowed us to model the substrate sugar in the novel active site and to elucidate the mechanistic basis of the newly established activity. The results demonstrate that natural and inert artificial protein scaffolds can be converted into highly proficient enzymes in the laboratory, and provide insights into the mechanisms of enzyme evolution.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Institutionen der Universität: Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie > Lehrstuhl Biochemie III - Proteindesign - Univ.-Prof. Dr. Birte Höcker
Fakultäten
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie
Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Chemie > Lehrstuhl Biochemie
Titel an der UBT entstanden: Nein
Themengebiete aus DDC: 500 Naturwissenschaften und Mathematik > 500 Naturwissenschaften
500 Naturwissenschaften und Mathematik > 570 Biowissenschaften; Biologie
Eingestellt am: 27 Jan 2021 07:13
Letzte Änderung: 05 Sep 2022 07:42
URI: https://eref.uni-bayreuth.de/id/eprint/62428