Cloned (Comment) | Organism |
---|---|
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] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
39700 | - |
dimeric enzyme, gel filtration | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
nicotinamide + H2O | Mycobacterium tuberculosis | - |
nicotinate + NH3 | - |
? | |
nicotinamide + H2O | Mycobacterium tuberculosis H37Rv | - |
nicotinate + NH3 | - |
? | |
pyrazinamide + H2O | Mycobacterium tuberculosis | - |
pyrazinoic acid + NH3 | - |
? | |
pyrazinamide + H2O | Mycobacterium tuberculosis H37Rv | - |
pyrazinoic acid + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | I6XD65 | gene pncA | - |
Mycobacterium tuberculosis H37Rv | I6XD65 | gene pncA | - |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and gel filtration | Mycobacterium tuberculosis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nicotinamide + H2O | - |
Mycobacterium tuberculosis | nicotinate + NH3 | - |
? | |
nicotinamide + H2O | - |
Mycobacterium tuberculosis H37Rv | nicotinate + NH3 | - |
? | |
pyrazinamide + H2O | - |
Mycobacterium tuberculosis | pyrazinoic acid + NH3 | - |
? | |
pyrazinamide + H2O | - |
Mycobacterium tuberculosis H37Rv | pyrazinoic acid + NH3 | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 |
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 | Comment | Organism |
---|---|---|
nicotinamidase/pyrazinamidase | - |
Mycobacterium tuberculosis |
PZAse | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
additional information | structural modeling of the enzyme homodimer, docking study and molecular dynamics simulations, overview | Mycobacterium tuberculosis |