Ribosomal protein S1 and Aspartate decarboxylase (RpsA/PanD)

Ribosomal protein S1 (RpsA) and Aspartate decarboxylase (PanD) are two distinct but functionally significant proteins in Mycobacterium tuberculosis that serve as the primary molecular targets for the essential anti-tuberculosis drug pyrazinamide (PZA) (Shi et al., 2011; Zhang et al., 2013). RpsA is a vital component of the 30S ribosomal subunit involved in translation initiation and the trans-translation process, which is critical for rescuing stalled ribosomes under stress conditions (Shi et al., 2011). PanD is an enzyme that catalyzes the decarboxylation of L-aspartate to produce beta-alanine, a key precursor for the biosynthesis of pantothenate (vitamin B5) and Coenzyme A (Zhang et al., 2013; Gopal et al., 2016). The active form of pyrazinamide, pyrazinoic acid (POA), binds to the C-terminus of RpsA to inhibit trans-translation and to PanD to disrupt the synthesis of essential metabolic cofactors (Shi et al., 2011;}

Other names

RpsAPanD30S ribosomal protein S1L-aspartate 1-decarboxylaseADCAspartate 1-decarboxylase

Inhibition of trans-translation via binding to the C-terminus of RpsA and inhibition of beta-alanine biosynthesis via binding to PanD (Shi et al., 2011; Zhang et al., 2013).