Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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
-
?

Organism

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
-
-

Substrates and Products (Substrate)

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
-
?

Synonyms

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

General Information

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