EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.B15 | Co2+ | activates, and reactivates the metal-depleted PZase, and facilitates the deprotonation of coordinates water molecules to generate a nucleophile that catalyzes the enzymatic reaction | Mycobacterium tuberculosis | |
3.5.1.B15 | Fe2+ | activates, cannot reactivate the metal-depleted PZase, but facilitates the deprotonation of coordinated water molecules to generate a nucleophile that catalyzes the enzymatic reaction | Mycobacterium tuberculosis | |
3.5.1.B15 | Mn2+ | activates, and reactivates the metal-depleted PZase | Mycobacterium tuberculosis | |
3.5.1.B15 | additional information | PZase is a metalloenzyme, metal binding structure, overview. The metal coordination site of the enzyme is able to coordinate various divalent metal cofactors. Effects of metal-ion replacement on pyrazinamidase activity, quantum mechanics calculations and simulations, metal-ligand (residue) binding energy and atomic partial charges in the presence of various ions, overview. Co2+, Mn2+, and Zn2+ are able to reactivate metal-depleted PZase, while Cu2+, Fe2+, and Mg2+ cannot restore activity. The coordination of Ni2+, Co2+, or Fe2+ to PZase facilitates the deprotonation of coordinated water molecules to generate a nucleophile that catalyzes the enzymatic reaction | Mycobacterium tuberculosis | |
3.5.1.B15 | Ni2+ | activates, and facilitates the deprotonation of coordinates water molecules to generate a nucleophile that catalyzes the enzymatic reaction | Mycobacterium tuberculosis | |
3.5.1.B15 | Zn2+ | activates, and reactivates the metal-depleted PZase | Mycobacterium tuberculosis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.B15 | pyrazinamide + H2O | Mycobacterium tuberculosis | - |
pyrazinoic acid + NH3 | - |
? | |
3.5.1.B15 | pyrazinamide + H2O | Mycobacterium tuberculosis H37Rv | - |
pyrazinoic acid + NH3 | - |
? | |
3.5.1.B15 | pyrazinamide + H2O | Mycobacterium tuberculosis ATCC 25618 | - |
pyrazinoic acid + NH3 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.B15 | Mycobacterium tuberculosis | I6XD65 | - |
- |
3.5.1.B15 | Mycobacterium tuberculosis ATCC 25618 | I6XD65 | - |
- |
3.5.1.B15 | Mycobacterium tuberculosis H37Rv | I6XD65 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.B15 | pyrazinamide + H2O | - |
Mycobacterium tuberculosis | pyrazinoic acid + NH3 | - |
? | |
3.5.1.B15 | pyrazinamide + H2O | - |
Mycobacterium tuberculosis H37Rv | pyrazinoic acid + NH3 | - |
? | |
3.5.1.B15 | pyrazinamide + H2O | - |
Mycobacterium tuberculosis ATCC 25618 | pyrazinoic acid + NH3 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.B15 | PncA | - |
Mycobacterium tuberculosis |
3.5.1.B15 | PZAse | - |
Mycobacterium tuberculosis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.1.B15 | additional information | the coordination of metal cofactors Ni2+, Co2+, or Fe2+ to PZase facilitates the deprotonation of coordinates water molecules to generate a nucleophile that catalyzes the enzymatic reaction | Mycobacterium tuberculosis |
3.5.1.B15 | physiological function | pyrazinamidase (PZase), a metalloenzyme, is responsible for acidic modification of pyrazinamide (PZA), a drug used in tuberculosis treatment | Mycobacterium tuberculosis |