투고논문

Identification of Enzymatic Catalysis of PncA using ¹H-NMR

Jong-Jae Yi^1,ǂ, Won-Je Kim^2,ǂ, Jin-Kyu Rhee³, Jongsoo Lim⁴, Bong-Jin Lee², and Woo Sung Son^1,*

¹College of Pharmacy, CHA University, 120 Haeyong-ro, Pocheon-si, Gyeonggi-do, 11160, Republic of Korea

²College of Pharmacy, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul, 08826, Republic of Korea

³Department of Food Science and Engineering, Ewha Womans University, 52 Ewhayeodae-gil, Seodaemun-gu, Seoul, 03760, Republic of Korea

⁴Discovery Technology Team, Dong-A ST Research Institute, 21 Geumhwa-ro 105beon-gil, Yongin-si, Gyeonggi-do, 17073, Republic of Korea

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.