EC Number   |
General Information |
Reference |
|---|
   3.5.1.B15 | malfunction |
Mycobacterium bovis 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 |
| 3.5.1.B15 | malfunction |
Mycobacterium kansasii 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 |
| 3.5.1.B15 | malfunction |
Mycobacterium marinum 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 |
| 3.5.1.B15 | malfunction |
Mycobacterium smegmatis 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 |
| 3.5.1.B15 | malfunction |
pyrazinamide (PZA)-resistance in Mycobacterium tuberculosis strains is caused by point mutations in the PZase enzyme which is the activator of the prodrug pyrazinoic acid (PZA) |
-, 757007 |
| 3.5.1.B15 | malfunction |
the major cause of PZA-resistance is associated with mutations in the pncA gene. Several novel mutations including V131F, Q141P, R154T, A170P, and V180F in the pncA gene of PZA-resistant isolates are detectetd during PZA drug susceptibility testing followed by pncA gene sequencing. Molecular mechanism of PZA-resistance, molecular dynamics |
757258 |
| 3.5.1.B15 | malfunction |
the residues of flap region of enzyme mutant K96R acquire more flexibility in mutant form of protein and thus move away from the active site. This leads to weak binding of the drug to the target residues which might interfere with the activation of the drug to functional form thereby giving rise to drug resistant bacterial strains |
-, 756295 |
| 3.5.1.B15 | metabolism |
in Mycobacterium tuberculosis the enzyme converts the nicotinamide analogue prodrug pyrazinamide into the bacteriostatic pyrazinoic acid |
710862 |
| 3.5.1.B15 | metabolism |
pyrazinamide (PZA), a derivative of nicotinamide is one of the most imperative first-line drug treatments against tuberculosis. PZA is significantly used in MDR tuberculosis in combination with isoniazid, rifampicin and ethambutol in regimens. The most potent action of the drug is against the semi-dormant bacilli in an acidic environment, which cannot be treated with most other drugs and thus helps in shortening the chemotherapy period |
-, 756295 |
| 3.5.1.B15 | more |
catalytic Cys138 |
-, 757008 |
