투고논문


JKMRS Volume 22, No 4, pp 144, Characterization of pH-dependen...
2018년 12월 20일 / 조회수: 588

Characterization of pH-dependent structural properties of hydrolase PncA using NMR


Jong-Jae Yi1,ǂ, Won-Je Kim2,ǂ, Jin-Kyu Rhee3, Jongsoo Lim4, Bong-Jin Lee2, and Woo Sung Son1,*


1 College of pharmacy and Institute of Pharmaceutical Sciences, CHA University, 120 Haeyong-ro, Pocheon-si, Gyeonggi-do 11160, Republic of Korea
2 College of pharmacy, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 08826, Republic of Korea
3 Department of Food Science and Engineering, Ewha Womans University, 52 Ewhayeodae-gil, Seodaemun-gu, Seoul 03760, Republic of Korea
4 Discovery Technology Team, Dong-A ST Research Institute, 21 Geumhwa-ro 105beon-gil, Yongin-si, Gyeonggi-do 17073, Republic of Korea


Received Dec 06, 2018; Revised Dec 15, 2018; Accepted Dec 17, 2018


Abstract

Catalytic enzyme Pyrazinamidase (PncA) from Mycobacterium tuberculosis can hydrolyze substrate pyrazinamide (PZA) to pyrazoic acid (POA) as active form of compound. Using NMR spectroscopy, pH-dependent catalytic properties were monitored including metal binding mode during converting PZA to POA. There seems to be a conformational change through zinc binding in active site from the perturbation of peak intensities in series of 2D HSQC spectra the conformation changes through zinc binding.


ǂ These authors contributed equally.
* Address correspondence to: Woo Sung Son, College of Pharmacy and Institute of Pharmaceutical Sciences, CHA University, 120 Haeryong-ro, Pocheon-si, Gyeonggi-do 11160, Republic of Korea, Tel: 82-31-850-9398; Fax: 82-31-850-9398; E-mail: wson@cha.ac.kr

첨부파일 11-JKMRS_SonWS_2.pdf