Mechanistic analysis elucidating the relationship between Lys96 mutation in Mycobacterium tuberculosis pyrazinamidase enzyme and pyrazinamide susceptibility

BMC Genomics. 2015;16 Suppl 2(Suppl 2):S14. doi: 10.1186/1471-2164-16-S2-S14. Epub 2015 Jan 21.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases / chemistry
  • Amidohydrolases / genetics*
  • Amidohydrolases / metabolism
  • Antitubercular Agents / chemistry
  • Antitubercular Agents / metabolism
  • Antitubercular Agents / pharmacology
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Drug Resistance, Bacterial / genetics
  • Hydrophobic and Hydrophilic Interactions
  • Ligands
  • Lysine / chemistry
  • Lysine / genetics*
  • Lysine / metabolism
  • Molecular Docking Simulation
  • Molecular Dynamics Simulation
  • Mutation*
  • Mycobacterium tuberculosis / drug effects*
  • Mycobacterium tuberculosis / enzymology
  • Mycobacterium tuberculosis / genetics
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Pyrazinamide / chemistry
  • Pyrazinamide / metabolism
  • Pyrazinamide / pharmacology*

Substances

  • Antitubercular Agents
  • Bacterial Proteins
  • Ligands
  • Pyrazinamide
  • Amidohydrolases
  • PncA protein, Mycobacterium tuberculosis
  • Lysine