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Literature summary extracted from

  • Junaid, M.; Li, C.-D.; Li, J.; Khan, A.; Shujait Ali, S.; Jamal, S.B.; Saud, S.; Ali, A.; Wei, D.
    Structural insights of catalytic mechanism in mutant pyrazinamidase of Mycobacterium tuberculosis (2020), J. Biomol. Struct. Dyn., 39, 3172-3185.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.B15 D12A mutation affects regions Gln10-His43, Phe50-Gly75 and disturbs the communication among the catalytic triad residues Asp8, Lys98 and Cys138 and the oxyanion hole formation. The mutation destabilizes the interaction between Fe2+ ion and Asp49, His51, His57 and His71 Mycobacterium tuberculosis
3.5.1.B15 G97D/Q10P mutation affects regions Gln10-His43, Phe50-Gly75 and disturbs the communication among the catalytic triad residues Asp8, Lys98 and Cys138, and the mutation destabilizes the interaction between Fe2+ ion and Asp49, His51, His57 and His71 Mycobacterium tuberculosis
3.5.1.B15 Q10P mutation affects regions Gln10-His43, Phe50-Gly75 and disturbs the communication among the catalytic triad residues Asp8, Lys98 and Cys138, and the mutation destabilizes the interaction between Fe2+ ion and Asp49, His51, His57 and His71 Mycobacterium tuberculosis
3.5.1.19 D12A frequent mutations in multi-drug resistant Mycobacterium tuberculosis. The mutation increases the binding cavity, thereby destabilizing the binding of pyrazinamide in the cavity. The mutations strongly disturbs the communication among the catalytic triad (Asp8, Lys98 and Cys138). The mutation greatly disturbs the oxyanion hole formation. The mutations destabilizes the interaction between Fe2+ ion and Asp49, His51, His57 and His71 Mycobacterium tuberculosis
3.5.1.19 D12A mutation affects regions Gln10-His43, Phe50-Gly75 and disturbs the communication among the catalytic triad residues Asp8, Lys98 and Cys138 and the oxyanion hole formation. The mutation destabilizes the interaction between Fe2+ ion and Asp49, His51, His57 and His71 Mycobacterium tuberculosis
3.5.1.19 G97D frequent mutations in multi-drug resistant Mycobacterium tuberculosis. The mutation increases the binding cavity, thereby destabilizing the binding of pyrazinamide in the cavity. The mutation disturbs the oxyanion hole formation. The mutations destabilizes the interaction between Fe2+ ion and Asp49, His51, His57 and His71 Mycobacterium tuberculosis
3.5.1.19 G97D/Q10P mutation affects regions Gln10-His43, Phe50-Gly75 and disturbs the communication among the catalytic triad residues Asp8, Lys98 and Cys138, and the mutation destabilizes the interaction between Fe2+ ion and Asp49, His51, His57 and His71 Mycobacterium tuberculosis
3.5.1.19 Q10P frequent mutations in multi-drug resistant Mycobacterium tuberculosis. The mutation increases the binding cavity, thereby destabilizing the binding of pyrazinamide in the cavity. The mutations strongly disturbs the communication among the catalytic triad (Asp8, Lys98 and Cys138). The mutation disturbs the oxyanion hole formation. The mutations destabilizes the interaction between Fe2+ ion and Asp49, His51, His57 and His71 Mycobacterium tuberculosis
3.5.1.19 Q10P mutation affects regions Gln10-His43, Phe50-Gly75 and disturbs the communication among the catalytic triad residues Asp8, Lys98 and Cys138, and the mutation destabilizes the interaction between Fe2+ ion and Asp49, His51, His57 and His71 Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.19 Fe2+ Fe2+-dependent amidohydrolase Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.19 pyrazinamide + H2O Mycobacterium tuberculosis pyrazinamide is an essential first-line drug used in Mycobacterium tuberculosis treatment pyrazinoic acid + NH3
-
 ?
3.5.1.19 pyrazinamide + H2O Mycobacterium tuberculosis H37Rv pyrazinamide is an essential first-line drug used in Mycobacterium tuberculosis treatment pyrazinoic acid + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.B15 Mycobacterium tuberculosis I6XD65 cf. EC 3.5.1.19
-
3.5.1.B15 Mycobacterium tuberculosis H37Rv I6XD65 cf. EC 3.5.1.19
-
3.5.1.19 Mycobacterium tuberculosis I6XD65 cf. EC 3.5.1.B15
-
3.5.1.19 Mycobacterium tuberculosis I6XD65 i.e. nicotinamidase/pyrazinamidase
-
3.5.1.19 Mycobacterium tuberculosis H37Rv I6XD65 cf. EC 3.5.1.B15
-
3.5.1.19 Mycobacterium tuberculosis H37Rv I6XD65 i.e. nicotinamidase/pyrazinamidase
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.19 pyrazinamide + H2O pyrazinamide is an essential first-line drug used in Mycobacterium tuberculosis treatment Mycobacterium tuberculosis pyrazinoic acid + NH3
-
 ?
3.5.1.19 pyrazinamide + H2O
-
 Mycobacterium tuberculosis pyrazinoic acid + NH3
-
 ?
3.5.1.19 pyrazinamide + H2O pyrazinamide is an essential first-line drug used in Mycobacterium tuberculosis treatment Mycobacterium tuberculosis H37Rv pyrazinoic acid + NH3
-
 ?
3.5.1.19 pyrazinamide + H2O
-
 Mycobacterium tuberculosis H37Rv pyrazinoic acid + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.19 pyrazinamidase
-
 Mycobacterium tuberculosis
3.5.1.19 PZAse
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
3.5.1.19 drug target drug resistance mechanism against pyrazinamide due to mutations (Q10P, D12A and G97D) Mycobacterium tuberculosis