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Results 1 - 10 of 45 > >>
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.B15evolution the nicotinamidase/pyrazinamidase PncA is a member of a large family of hydrolase enzymes that catalyze the deamination of nicotinamide to nicotinic acid 752683
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.B15malfunction a nonfunctional PZase in resistant strains allows the mycobacterium to survive in the presence of pyrazinamide. Alternative or complementary mechanism of resistance may exist 755800
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.B15malfunction analysis of mutations in pyrazinamidase and effects of the mutations at the metal coordination site and conformational changes in PZase binding cavity on the enzyme activity, quantum mechanical calculations, overview. Iron shows weak binding with the metal coordination site of the mutant proteins due to alteration in electron transfer mechanism. The binding cavity of the mutant PZase has undergone major conformational changes as the volume of pocket increased due to bulky R-chains of mutated amino acids. These conformational changes lead to weak binding of the drug at binding cavity of PZase and reduce the drug activation mechanism leading to increased drug resistance in the bacterial strains. The template structure used is the tertiary structure of pyrazinamidase from Mycobacterium tuberculosis, PDB ID 3PL1 -, 757448
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.B15malfunction cumulative effect of mutations and iron substitution -, 756516
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.B15malfunction estimation of pyrazinamidase activity using a cell-free in vitro synthesis of pncA and its association with pyrazinamide susceptibility in Mycobacterium tuberculosis, mutant phenotypes, overview -, 757008
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.B15malfunction identification and multiple analyses to unveil different mechanisms of resistance of PZase mutants L19R, R140H, and E144K, overview. The native PZase protein docking score is the maximum, showing strong binding affinity in comparison with mutants. Molecular dynamics simulations explore the effect of the variants on the biological function of PZase. Hydrogen bonding, metal ion Fe2+ deviation, and fluctuation also seem to be affected because of the mutations L19R, R140H, and E144K. The mutant variants play a significant role in PZA resistance, altering the overall activity of native PZase, including metal ion Fe2+ displacement and free energy -, 757293
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.B15malfunction mechanisms of the pyrazinamide (PZA) resistance of three pyrazinamidase mutants N11K, P69T, and D126N. In general, pyrazinoic acid (PZA) resistance is caused by three genes pncA, rpsA, and panD. Among them, the pncA gene contributes 72-99% to the resistance. The binding pocket analysis shows that mutations N11K and P69T decrease the volume of the active site and hinder the correct orientation of PZA drug in the active site. Moreover, the Patchdock score is low as compared to wild-type showing the disturbance of shape complementarity between enzyme PZase and PZA drug. These mutations N11K, P69T, and D126N disturb the position of the Fe2+ ion. Among the mutations, D126N allosterically disturbs the position of the Fe2+ ion. The mutations decrease the binding affinity toward the PZA drug -, 757305
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.B15malfunction mutations in the pncA gene cause pyrazinamide (PZA) resistance in Mycobacterium tuberculosis -, 758499
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.B15malfunction Mycobacterium abscessus is resistant to pyrazinamide due to the random mutations in the primary sequences of the pyrazinamidase. In silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium -, 757474
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.B15malfunction Mycobacterium avium is resistant to pyrazinamide due to the random mutations in the primary sequences of the pyrazinamidase. In silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium 757474
Results 1 - 10 of 45 > >>