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Literature summary for 3.5.1.B15 extracted from

  • Khadem-Maaref, M.; Mehrnejad, F.; Phirouznia, A.
    Effects of metal-ion replacement on pyrazinamidase activity a quantum mechanical study (2017), J. Mol. Graph. Model., 73, 24-29 .
    View publication on PubMed
Search for more literature for 3.5.1.B15

Metals/Ions

Metals/Ions Comment Organism Structure
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
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
Mn2+ activates, and reactivates the metal-depleted PZase Mycobacterium tuberculosis
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
Ni2+ activates, and facilitates the deprotonation of coordinates water molecules to generate a nucleophile that catalyzes the enzymatic reaction Mycobacterium tuberculosis
Zn2+ activates, and reactivates the metal-depleted PZase Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyrazinamide + H2O Mycobacterium tuberculosis
-
 pyrazinoic acid + NH3
-
 ?
pyrazinamide + H2O Mycobacterium tuberculosis H37Rv
-
 pyrazinoic acid + NH3
-
 ?
pyrazinamide + H2O Mycobacterium tuberculosis ATCC 25618
-
 pyrazinoic acid + NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis I6XD65
-
-
Mycobacterium tuberculosis ATCC 25618 I6XD65
-
-
Mycobacterium tuberculosis H37Rv I6XD65
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyrazinamide + H2O
-
 Mycobacterium tuberculosis pyrazinoic acid + NH3
-
 ?
pyrazinamide + H2O
-
 Mycobacterium tuberculosis H37Rv pyrazinoic acid + NH3
-
 ?
pyrazinamide + H2O
-
 Mycobacterium tuberculosis ATCC 25618 pyrazinoic acid + NH3
-
 ?

Synonyms

Synonyms Comment Organism
PncA
-
 Mycobacterium tuberculosis
PZAse
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
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
physiological function pyrazinamidase (PZase), a metalloenzyme, is responsible for acidic modification of pyrazinamide (PZA), a drug used in tuberculosis treatment Mycobacterium tuberculosis