Structural and mechanistic insights into Mycobacterium abscessus as-partate decarboxylase PanD and a pyrazinoic acid-derived inhibitor

• Main Authors: Saw, Wuan Geok, Leow, Chen Yen, Harikishore, Amaravadhi, Shin, Joon, Cole, Malcolm S., Aragaw, Wassihun Wedajo, Ragunathan, Priya, Hegde, Pooja, Aldrich, Courtney C., Dick, Thomas, Grüber, Gerhard
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2022
• Subjects: Science::Biological sciences::Biochemistry; Science::Biological sciences::Biophysics; Non-Tuberculous Mycobacteria; Mycobacterium Abscessus; Pyrazinamide; Pyrazinoic Acid; Coenzyme A; Aspartate Decarboxylase
• Online Access: https://hdl.handle.net/10356/163126
• Institution: Nanyang Technological University

Mycobacterium tuberculosis (Mtb) aspartate decarboxylase PanD is required for biosynthesis of the essential cofactor coenzyme A and targeted by the first line drug pyrazinamide (PZA). PZA is a prodrug that is converted by a bacterial amidase into its bioactive form pyrazinoic acid (POA). Employing s...