Exploiting Protein Symmetry To Design Light‐Controllable Enzyme Inhibitors

Bernd Reisinger, Natascha Kuzmanovic, Patrick Löffler, Rainer Merkl, Burkhard König, Reinhard Sterner

Angewandte Chemie International Edition · 2013 · 68 citations · 18 references

Concepts

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.

References

18