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Literature summary extracted from

  • Esmaeeli, R.; Mehrnejad, F.; Mir-Derikvand, M.; Gopalpoor, N.
    Computational insights into pH-dependence of structure and dynamics of pyrazinamidase A comparison of wild type and mutants (2018), J. Cell. Biochem., 120, 2502-2514 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.B15 L85P naturally occuring mutation, resistant strain Mycobacterium tuberculosis
3.5.1.B15 additional information molecular dynamics simulations coupled with essential dynamics and binding pocket analysis at neutral (pH = 7) and acidic (pH = 4) ambient conditions, detailed overview. Computational insights into pH-dependence of structure and dynamics of pyrazinamidase, comparison of wild-type and mutant enzymes Mycobacterium tuberculosis
3.5.1.B15 V155G naturally occuring mutation, resistant strain Mycobacterium tuberculosis
3.5.1.B15 W68G naturally occuring mutation, resistant strain Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.B15 Fe2+ residues D49, H51, H57, H71 comprise a metal coordinating site coordinating an Fe2+ or Zn2+ cation Mycobacterium tuberculosis
3.5.1.B15 additional information Mn2+, Co2+, Sr2+, Ba2+, Fe3+, Mg2+, and Ca2+ cannot significantly change the activity and stability of PZase Mycobacterium tuberculosis
3.5.1.B15 Zn2+ residues D49, H51, H57, H71 comprise a metal coordinating site coordinating an Fe2+ or Zn2+ cation 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

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.B15 additional information
-
 computational insights into pH-dependence of structure and dynamics of pyrazinamidase, comparison of wild-type and mutant enzymes Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
3.5.1.B15 additional information computational insights into pH-dependence of structure and dynamics of pyrazinamidase, comparison of wild-type and mutant enzymes, molecular dynamics simulations using the wild-type structure, PDB ID 3PL1, detailed overview. The 51-71 flap region exhibits a drastic displacement leading to enlargement of binding cavity, especially at the lower pH. Residues D8, K96, and C138 comprise an active site Mycobacterium tuberculosis
3.5.1.B15 physiological function the mycobacterial enzyme pyrazinamidase (PZase), is the target of pyrazinamide (PZA), one of the first-line medications for treatment of tuberculosis. PZA is a prodrug catalyzed to its active form pyrazinoic acid (POA) by enzyme PZase. POA is pumped out of the cell slowly and converts to its conjugate acid form to easily diffuse inwards and accumulates Mycobacterium tuberculosis