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Literature summary for 3.5.1.B15 extracted from

  • Khan, M.T.; Malik, S.I.
    Structural dynamics behind variants in pyrazinamidase and pyrazinamide resistance (2020), J. Biomol. Struct. Dyn., 38, 3003-3017.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis A0A2Z5CVM9
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
PncA
-
 Mycobacterium tuberculosis
PZAse
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
malfunction the major cause of PZA-resistance is associated with mutations in the pncA gene. Several novel mutations including V131F, Q141P, R154T, A170P, and V180F in the pncA gene of PZA-resistant isolates are detectetd during PZA drug susceptibility testing followed by pncA gene sequencing. Molecular mechanism of PZA-resistance, molecular dynamics Mycobacterium tuberculosis
additional information wild-type and mutant PZase structures in apo and complex with pyrazinamide (PZA) are subjected to structure analysis by molecular dynamics simulations Mycobacterium tuberculosis
physiological function pyrazinamide (PZA) is an important component of first-line anti-tuberculosis (anti-TB) drugs. The anti-TB agent is activated into an active form, pyrazinoic acid, by Mycobacterium tuberculosis (MTB) pncA gene encoding pyrazinamidase (PZase) Mycobacterium tuberculosis