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Benzo[d]thiazole-2-carboxamides as New anti-TB Chemotypes Inhibiting Mycobacterial ATP Phosphoribosyl Transferase (HisG) - Supplementary Material

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posted on 2022-11-29, 09:50 authored by Tejas M. Dhameliya, Rishu Tiwari, Arkaprabha Banerjee, Sahaj Pancholia, Dharmarajan Sriram, Dulal Panda, Asit K. Chakraborti

Figure 1. Role of ATP-PRTase enzyme in the first step of cycle of biosynthesis of L-Histidine.

Figure 2. The SDS-PAGE (sodium dodecyl-sulfate polyacrylamide gel electrophoresis) profile of purified recombinant ATPPRTase

from the complexed mixture of proteins.

Figure 3. The plots of velocity of enzymatic reaction versus concentration of ATP (A) and PRPP (B). The Michaelis-Menten constant

for PRPP and ATP were observed with values of 72 ± 15 and 238 ± 28 μM, respectively with the value of Vmax of 5.1 ± 1.3 μM min-.

Figure 4.Plots of % enzyme inhibitions versus selected benzo[d]thiazol-2-carboxamides (1-4).

Table 1. Comparison of binding energies to stabilize ATP-PRTase.

Figure 5. Compound 1n (A) and 2a (B) interacting with the catalytic residues at the binding site of ATP-PRTase (A).

Figure 6. The 2-dimensional interactions of 1n (A) and 2a (B) with ATP-PRTase represented through LigPlot+.[1]

Figure 7. The schematic plots for (a) RMSD-P, (b) RMSD-L, (c) RMSF, (d) RoG, (e) SASA and (f) HB for the complex of ATPPRTase

with 1n.

Figure 8. The schematic plots for (a) RMSD-P, (b) RMSD-L, (c) RMSF, (d) RoG, (e) SASA and (f) HB for the complex of ATPPRTase

with 2a.



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