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Identification of Enzymatic Catalysis of PncA using 1H-NMR

  • Yi, Jong-Jae (College of Pharmacy, CHA University) ;
  • Kim, Won-Je (College of Pharmacy, Seoul National University) ;
  • Rhee, Jin-Kyu (Department of Food Science and Engineering, Ewha Womans University) ;
  • Lim, Jongsoo (Discovery Technology Team, Dong-A ST Research Institute) ;
  • Lee, Bong-Jin (College of Pharmacy, Seoul National University) ;
  • Son, Woo Sung (College of Pharmacy, CHA University)
  • Received : 2017.07.18
  • Accepted : 2017.07.30
  • Published : 2017.09.20

Abstract

Pyrazinamidase (PncA) from Mycobacterium tuberculosis is the hydrolytic enzyme (hydrolase) that can hydrolyze substrate PZA to active form pyrazoic acid (POA). To investigate hydrolytic reaction of M. tuberculosis PncA, 1D NMR spectra were monitored at various molar ratios of PncA and PZA. The line-width of PZA was changed as PncA was added into PZA with different molar ratios. These results suggested that determination of PncA enzymatic activity could potentially serve as an indirect measure of PZA susceptibility.

Keywords

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