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Literature summary for 3.5.1.B15 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
Search for more literature for 3.5.1.B15

Protein Variants

Protein Variants Comment Organism
L85P naturally occuring mutation, resistant strain Mycobacterium tuberculosis
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
V155G naturally occuring mutation, resistant strain Mycobacterium tuberculosis
W68G naturally occuring mutation, resistant strain Mycobacterium tuberculosis

Metals/Ions

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

pH Range

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

General Information

General Information Comment Organism
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
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