Reisinger, Bernd and Kuzmanovic, Natascha and Loeffler, Patrick and Merkl, Rainer and Koenig, Burkhard and Sterner, Reinhard (2014) Exploiting Protein Symmetry To Design Light-Controllable Enzyme Inhibitors. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 53 (2). pp. 595-598. ISSN 1433-7851, 1521-3773
Full text not available from this repository. (Request a copy)Abstract
The activity of the metabolic branch-point enzyme PriA from Mycobacterium tuberculosis (mtPriA) can be controlled reversibly by light. Two-pronged inhibitors based on the dithienylethene scaffold were designed utilizing mtPriA's natural rotational symmetry. Switching from the flexible, ring-open to the rigid, ring-closed isomer reduces inhibition activity by one order of magnitude.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MYCOBACTERIUM-TUBERCULOSIS; TRYPTOPHAN BIOSYNTHESIS; PHOSPHATE SYNTHASE; EVOLUTION; HISTIDINE; SPECIFICITY; ISOMERASE; TOOLS; FOLD; biosynthesis; enzyme catalysis; enzyme inhibitors; molecular switches; photochromism |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Rainer Merkl Chemistry and Pharmacy > Institut für Organische Chemie > Lehrstuhl Prof. Dr. Burkhard König |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 28 Nov 2019 10:35 |
| Last Modified: | 28 Nov 2019 10:35 |
| URI: | https://pred.uni-regensburg.de/id/eprint/10833 |
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