This work was supported by the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie. We thank Dr. M. Spraul, Bruker Analytische MeBtechnik GmbH, Rheinstetten/Karlsruhe for the 600 MHz H NMR spectrum. Dr. H. Röttele for the 13C NMR spectrum of the adduct, Dr. M. Lenz for the urocanase overproducing E. coli strain, and Ms. J. Herman for her assistance in numerous enzyme isolations.
Article first published online: 22 DEC 2003
Copyright © 1994 by VCH Verlagsgesellschaft mbH, Germany
Angewandte Chemie International Edition in English
Volume 33, Issue 12, pages 1279–1280, June 6, 1994
How to Cite
Schubert, C., Zhao, Y., Shin, J.-H. and Rétey, J. (1994), On the Mechanism of the Urocanase Reaction: Confirmation of the Structure of the NAD+-Inhibitor Adduct by Direct 13C-13C Coupling. Angew. Chem. Int. Ed. Engl., 33: 1279–1280. doi: 10.1002/anie.199412791
Dedicated to Professor Joachim Knappe on the occasion of his 65th birthday
- Issue published online: 22 DEC 2003
- Article first published online: 22 DEC 2003
- Manuscript Received: 3 FEB 1994
NAD+ functions not as a redox reagent but as an electrophile in the second step in the degradation of histidine. In this as yet unique enzymatic reaction, water is added to urocanic acid (1), leading to the formation of 2. The proposed mechanism has now been substantiated by NMR spectroscopic results on the 13C-labeled adduct 3. R = ADP-ribosyl, • = 13C.