The IPB has once again been recognized for its exemplary actions in terms of equal opportunity-oriented personnel and organizational policies and has received the TOTAL E-QUALITY certification for the…
The Plant Science Student Conference (PSSC) has been organised by students from the two Leibniz institutes, IPK and IPB, every year for the last 20 years. In this interview, Christina Wäsch (IPK) and…
Bräuer, L.; Brandt, W.; Schulze, D.; Zakharova, S.; Wessjohann, L.;A Structural Model of the Membrane-Bound Aromatic Prenyltransferase UbiA from E. coliChemBioChem9982-992(2008)DOI: 10.1002/cbic.200700575
We report the first reasonable model for the active site of the membrane‐bound aromatic prenyltransferase UbiA, derived from structural—not sequence—similarity to a terpene synthase, with the aid of threading, site‐directed mutagenesis, and substrate selectivities. The high similarity of the active fold of UbiA‐transferase to that of 5‐epi‐aristolochene synthase (Nictotiana tabacum ), despite a low homology, allows a hypothesis on a convergent evolution of these enzymes to be formed.