Funded by the BBSRC [BBS/B/14434], The Wellcome Trust [082596 and 083481] and EC Seventh Framework Programme (FP7/2007-2013). We thank Lorna Eades of the University of Edinburgh, Mark Agacan, the Diamond Synchrotron Radiation Facility and the European Synchrotron Radiation facility for support.
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Communication
Specificity and Mechanism of Acinetobacter baumanii Nicotinamidase: Implications for Activation of the Front-Line Tuberculosis Drug Pyrazinamide†
Article first published online: 26 OCT 2009
DOI: 10.1002/anie.200903407
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Issue
Angewandte Chemie International Edition
Volume 48, Issue 48, pages 9176–9179, November 16, 2009
Additional Information
How to Cite
Fyfe, P., Rao, V., Zemla, A., Cameron, S. and Hunter, W. (2009), Specificity and Mechanism of Acinetobacter baumanii Nicotinamidase: Implications for Activation of the Front-Line Tuberculosis Drug Pyrazinamide. Angewandte Chemie International Edition, 48: 9176–9179. doi: 10.1002/anie.200903407
- †
Publication History
- Issue published online: 11 NOV 2009
- Article first published online: 26 OCT 2009
- Manuscript Revised: 24 AUG 2009
- Manuscript Received: 23 JUN 2009
Funded by
- BBSRC. Grant Number: BBS/B/14434
- The Wellcome Trust. Grant Numbers: 082596, 083481
- EC Seventh Framework Programme. Grant Number: FP7/2007-2013
Keywords:
- drug discovery;
- enzymes;
- mechanisms;
- tuberculosis;
- zinc
Graphical Abstract
TB or not TB active: The high-resolution crystal structures (see picture) of the zinc-containing metalloenzyme nicotinamidase in complex with nicotinic acid and pyrazinoic acid reveal new aspects of enzyme mechanism that help to explain the activation of a front-line anti-tuberculosis (TB) drug.