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Exploiting Protein Symmetry To Design Light-Controllable Enzyme Inhibitors

Reisinger, Bernd, Kuzmanovic, Natascha, Löffler, Patrick, Merkl, Rainer, König, Burkhard and Sterner, Reinhard (2014) Exploiting Protein Symmetry To Design Light-Controllable Enzyme Inhibitors. Angewandte Chemie International Edition 53, pp. 595-598.

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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.


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Item type:Article
Date:2014
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Chemistry and Pharmacy > Institut für Organische Chemie > Lehrstuhl Prof. Dr. Burkhard König
Projects:GRK 1910, Graduiertenkolleg "Medicinal Chemistry of Selective GPCR Ligands"
Identification Number:
ValueType
10.1002/anie.201307207DOI
Keywords:biosynthesis · enzyme catalysis · enzyme inhibitors · molecular switches · photochromism
Dewey Decimal Classification:500 Science > 540 Chemistry & allied sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:29759
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