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Literature summary extracted from

  • Rueda, D.; Sheen, P.; Gilman, R.H.; Bueno, C.; Santos, M.; Pando-Robles, V.; Batista, C.V.; Zimic, M.
    Nicotinamidase/pyrazinamidase of Mycobacterium tuberculosis forms homo-dimers stabilized by disulfide bonds (2014), Tuberculosis, 94, 644-648.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.B15 gene pncA, DNA and amino acid sequence determination and analysis, recombinant enzyme expression in Escherichia coli strain BL21(DE3)pLysS Mycobacterium tuberculosis
3.5.1.19 gene pncA, DNA and amino acid sequence determination and analysis, recombinant enzyme expression in Escherichia coli strain BL21(DE3)pLysS Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.B15 39700
-
 dimeric enzyme, gel filtration Mycobacterium tuberculosis
3.5.1.19 39700
-
 dimeric enzyme, gel filtration 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 nicotinamide + H2O Mycobacterium tuberculosis
-
 nicotinate + NH3
-
 ?
3.5.1.B15 nicotinamide + H2O Mycobacterium tuberculosis H37Rv
-
 nicotinate + NH3
-
 ?
3.5.1.B15 pyrazinamide + H2O Mycobacterium tuberculosis
-
 pyrazinoic acid + NH3
-
 ?
3.5.1.B15 pyrazinamide + H2O Mycobacterium tuberculosis H37Rv
-
 pyrazinoic acid + NH3
-
 ?
3.5.1.19 nicotinamide + H2O Mycobacterium tuberculosis
-
 nicotinate + NH3
-
 ?
3.5.1.19 nicotinamide + H2O Mycobacterium tuberculosis H37Rv
-
 nicotinate + NH3
-
 ?
3.5.1.19 pyrazinamide + H2O Mycobacterium tuberculosis
-
 pyrazinoic acid + NH3
-
 ?
3.5.1.19 pyrazinamide + H2O Mycobacterium tuberculosis H37Rv
-
 pyrazinoic acid + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.B15 Mycobacterium tuberculosis I6XD65 gene pncA
-
3.5.1.B15 Mycobacterium tuberculosis H37Rv I6XD65 gene pncA
-
3.5.1.19 Mycobacterium tuberculosis I6XD65 gene pncA
-
3.5.1.19 Mycobacterium tuberculosis H37Rv I6XD65 gene pncA
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.B15 recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and gel filtration Mycobacterium tuberculosis
3.5.1.19 recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and gel filtration Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.B15 nicotinamide + H2O
-
 Mycobacterium tuberculosis nicotinate + NH3
-
 ?
3.5.1.B15 nicotinamide + H2O
-
 Mycobacterium tuberculosis H37Rv nicotinate + NH3
-
 ?
3.5.1.B15 pyrazinamide + H2O
-
 Mycobacterium tuberculosis pyrazinoic acid + NH3
-
 ?
3.5.1.B15 pyrazinamide + H2O
-
 Mycobacterium tuberculosis H37Rv pyrazinoic acid + NH3
-
 ?
3.5.1.19 nicotinamide + H2O
-
 Mycobacterium tuberculosis nicotinate + NH3
-
 ?
3.5.1.19 nicotinamide + H2O
-
 Mycobacterium tuberculosis H37Rv nicotinate + NH3
-
 ?
3.5.1.19 pyrazinamide + H2O
-
 Mycobacterium tuberculosis pyrazinoic acid + NH3
-
 ?
3.5.1.19 pyrazinamide + H2O
-
 Mycobacterium tuberculosis H37Rv pyrazinoic acid + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.B15 homodimer 2 * 20500-20700, about, recombinant enzyme, SDS-PAGE and mass spectrometry. Homodimers show a slightly lower specific enzyme activity compared to monomers. Enzyme dimers are dissociated into monomers in response to reducing conditions, disulfide bonds C72-C138 and C138-C138 stabilize the quaternary structure of the enzyme homodimer, quarternary structure analysis, structural model of enzyme homodimer, overview Mycobacterium tuberculosis
3.5.1.B15 monomer 1 * 20500-20700, about, recombinant enzyme, SDS-PAGE and mass spectrometry. Homodimers show a slightly lower specific enzyme activity compared to monomers. Enzyme dimers are dissociated into monomers in response to reducing conditions, disulfide bonds C72-C138 and C138-C138 stabilize the quaternary structure of the enzyme homodimer, quarternary structure analysis, overview Mycobacterium tuberculosis
3.5.1.19 homodimer 2 * 20500-20700, about, recombinant enzyme, SDS-PAGE and mass spectrometry. Homodimers show a slightly lower specific enzyme activity compared to monomers. Enzyme dimers are dissociated into monomers in response to reducing conditions, disulfide bonds C72-C138 and C138-C138 stabilize the quaternary structure of the enzyme homodimer, quarternary structure analysis, structural model of enzyme homodimer, overview Mycobacterium tuberculosis
3.5.1.19 monomer 1 * 20500-20700, about, recombinant enzyme, SDS-PAGE and mass spectrometry. Homodimers show a slightly lower specific enzyme activity compared to monomers. Enzyme dimers are dissociated into monomers in response to reducing conditions, disulfide bonds C72-C138 and C138-C138 stabilize the quaternary structure of the enzyme homodimer, quarternary structure analysis, overview Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
3.5.1.B15 More cf. EC 3.5.1.19 Mycobacterium tuberculosis
3.5.1.B15 nicotinamidase/pyrazinamidase
-
 Mycobacterium tuberculosis
3.5.1.B15 PZAse
-
 Mycobacterium tuberculosis
3.5.1.19 nicotinamidase/pyrazinamidase
-
 Mycobacterium tuberculosis
3.5.1.19 PZAse
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
3.5.1.B15 additional information structural modeling of the enzyme homodimer, docking study and molecular dynamics simulations, overview Mycobacterium tuberculosis
3.5.1.19 additional information structural modeling of the enzyme homodimer, docking study and molecular dynamics simulations, overview Mycobacterium tuberculosis