Sperl, Josef M. and Rohweder, Bettina and Rajendran, Chitra and Sterner, Reinhard (2013) Establishing catalytic activity on an artificial (beta alpha)(8)-barrel protein designed from identical half-barrels. FEBS LETTERS, 587 (17). pp. 2798-2805. ISSN 0014-5793,
Full text not available from this repository. (Request a copy)Abstract
It has been postulated that the ubiquitous (beta alpha)(8)-barrel enzyme fold has evolved by duplication and fusion of an ancestral (beta alpha)(4)-half-barrel. We have previously reconstructed this process in the laboratory by fusing two copies of the C-terminal half-barrel HisF-C of imidazole glycerol phosphate synthase (HisF). The resulting construct HisF-CC was stepwise stabilized to Sym1 and Sym2, which are extremely robust but catalytically inert proteins. Here, we report on the generation of a circular permutant of Sym2 and the establishment of a sugar isomerization reaction on its scaffold. Our results demonstrate that duplication and mutagenesis of (beta alpha)(4)-half-barrels can readily lead to a stable and catalytically active (beta alpha)(8)-barrel enzyme. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PHOSPHORIBOSYL ANTHRANILATE ISOMERASE; DIFFERENT METABOLIC PATHWAYS; COMPUTATIONAL DESIGN; TRYPTOPHAN BIOSYNTHESIS; THERMOTOGA-MARITIMA; DIRECTED EVOLUTION; PHOSPHATE SYNTHASE; MOLECULAR-GRAPHICS; RANDOM MUTAGENESIS; ENZYME EVOLUTION; Artificial enzyme; Enzyme design; Enzyme evolution; (beta alpha)(8)-Barrel |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 31 Mar 2020 13:58 |
| Last Modified: | 31 Mar 2020 13:58 |
| URI: | https://pred.uni-regensburg.de/id/eprint/16053 |
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