Specificity and mechanism of Acinetobacter baumanii nicotinamidase: implications for activation of the front-line tuberculosis drug pyrazinamide

Paul K. Fyfe, Vincenzo A. Rao, Aleksandra Zemla, Scott Cameron, William N. Hunter

Research output: Contribution to journalArticlepeer-review

46 Citations (Scopus)

Abstract

TB or not TB active: The high-resolution crystal structures (see picture) of the zinccontaining 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.

Original languageEnglish
Pages (from-to)9176-9179
Number of pages4
JournalAngewandte Chemie - International Edition
Volume48
Issue number48
Early online date26 Oct 2009
DOIs
Publication statusPublished - 16 Nov 2009
Externally publishedYes

Keywords

  • Drug discovery
  • Enzymes
  • Mechanisms
  • Tuberculosis
  • Zinc

Fingerprint

Dive into the research topics of 'Specificity and mechanism of Acinetobacter baumanii nicotinamidase: implications for activation of the front-line tuberculosis drug pyrazinamide'. Together they form a unique fingerprint.

Cite this