We thank TSB, CoEBio3, and BBSRC for PhD studentships to C.C., M.W., and M.G. We thank Prof. Christopher T. Walsh (Harvard) for AdmH and Prof. Nicholas J. Turner (Manchester) for RgPAL expression plasmids.
Thermal Bifunctionality of Bacterial Phenylalanine Aminomutase and Ammonia Lyase Enzymes†
Article first published online: 27 MAR 2012
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 51, Issue 18, pages 4344–4348, April 27, 2012
How to Cite
Chesters, C., Wilding, M., Goodall, M. and Micklefield, J. (2012), Thermal Bifunctionality of Bacterial Phenylalanine Aminomutase and Ammonia Lyase Enzymes . Angew. Chem. Int. Ed., 51: 4344–4348. doi: 10.1002/anie.201200669
- Issue published online: 24 APR 2012
- Article first published online: 27 MAR 2012
- Manuscript Received: 24 JAN 2012
- ammonia lyases;
- enzyme catalysis;
- β-amino acids
Enzymatic thermal switch: The bacterial 4-methylideneimidazol-5-one (MIO) dependent enzymes AdmH and EncP are shown to display remarkable thermal bifunctionality: they act as mutases (blue graph) at lower temperatures but with lyase (red graph) activity predominant at higher temperatures. This temperature-dependent switch in enzyme class also explains how these two similar enzymes can fulfill different catalytic functions in secondary metabolisms.