Dem IPB wird erneut ein beispielhaftes Handeln im Sinne einer chancengleichheitsorientierten Personal- und Organisationspolitik bescheinigt. Das Institut erhält zum 6. Mal in Folge das TOTAL E-QUALITY…
Die Plant Science Student Conference (PSSC) wird seit 20 Jahren im jährlichen Wechsel von Studierenden der beiden Leibniz-Institute IPK und IPB organisiert. Im Interview erläutern Christina Wäsch…
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.
Publikation
Wasternack, C.; Feussner, I.;Multifunctional Enzymes in Oxylipin MetabolismChemBioChem92373-2375(2008)DOI: 10.1002/cbic.200800582
For the first time a member of the CYP74 enzyme subfamily (9‐AOS) from tomato has been shown by chemical and analytical approaches to catalyze multiple reactions. These multifunctional properties of 9‐AOS from the oxylipin‐forming lipoxygenase (LOX) pathway raise several new questions on lipid‐derived signaling.