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Literature summary extracted from

  • Pitaloka, D.A.E.; Arfan, A.; Ramadhan, D.S.F.; Chaidir, L.
    Insights from the molecular mechanism of pyrazinamide to mutated pyrazinamidase linked to the pncA gene in clinical isolates of Mycobacterium tuberculosis (2024), J. Biomol. Struct. Dyn., 42, 759-765.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.B15 A171V mutation has no effect on the complex's stability Mycobacterium tuberculosis
3.5.1.B15 H82R mutation affects the coordination state of the Fe2+ ion, changing the flexibility, stability, and fluctuation, which leads to an unstable complex and dissociation of PZA from the PZAse binding site Mycobacterium tuberculosis
3.5.1.B15 P62L mutation has no effect on the complex's stability Mycobacterium tuberculosis
3.5.1.B15 S66P mutation affects the coordination state of the Fe2+ ion, changing the flexibility, stability, and fluctuation, which leads to an unstable complex and dissociation of PZA from the PZAse binding site Mycobacterium tuberculosis
3.5.1.B15 T87M mutation affects the coordination state of the Fe2+ ion, changing the flexibility, stability, and fluctuation, which leads to an unstable complex and dissociation of PZA from the PZAse binding site Mycobacterium tuberculosis
3.5.1.19 A171V mutation has no effect on the complex's stability Mycobacterium tuberculosis
3.5.1.19 H82R mutation affects the coordination state of the Fe2+ ion, changing the flexibility, stability, and fluctuation, which leads to an unstable complex and dissociation of PZA from the PZAse binding site Mycobacterium tuberculosis
3.5.1.19 P62L mutation has no effect on the complex's stability Mycobacterium tuberculosis
3.5.1.19 S66P mutation affects the coordination state of the Fe2+ ion, changing the flexibility, stability, and fluctuation, which leads to an unstable complex and dissociation of PZA from the PZAse binding site Mycobacterium tuberculosis
3.5.1.19 T87M mutation affects the coordination state of the Fe2+ ion, changing the flexibility, stability, and fluctuation, which leads to an unstable complex and dissociation of PZA from the PZAse binding site Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.B15 Fe2+
-
 Mycobacterium tuberculosis
3.5.1.19 Fe2+
-
 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.B15 Mycobacterium tuberculosis I6XD65 cf. EC 3.5.1.19
-
3.5.1.B15 Mycobacterium tuberculosis H37Rv I6XD65 cf. EC 3.5.1.19
-
3.5.1.19 Mycobacterium tuberculosis I6XD65 i.e. nicotinamidase/pyrazinamidase
-
3.5.1.19 Mycobacterium tuberculosis H37Rv I6XD65 i.e. nicotinamidase/pyrazinamidase
-

Synonyms

EC Number Synonyms Comment Organism
3.5.1.B15 PncA
-
 Mycobacterium tuberculosis
3.5.1.19 PncA
-
 Mycobacterium tuberculosis