Changing the Regioselectivity of the Tryptophan 7-Halogenase PrnA by Site-Directed Mutagenesis


  • We thank Paul Vogel for the preparation of purified HisPrnAF103A, Dr. Ingmar Bauer for LC–MS analysis, and Dr. Margit Gruner for recording the 1H NMR spectra.


original image

Creating more space in the active site of the tryptophan 7-halogenase PrnA by exchanging the large amino acid phenylalanine for the smaller alanine makes it possible for the substrate to bind in different orientations (see picture; yellow PrnA, blue PrnAF103A variant). This results in halogenation of the differently bound substrate in the 5-position of the indole ring.