a nicotinamide prodrug. In Mycobacterium tuberculosis the enzyme converts the nicotinamide analogue prodrug pyrazinamide into the bacteriostatic pyrazinoic acid
a nicotinamide prodrug. In Mycobacterium tuberculosis the enzyme converts the nicotinamide analogue prodrug pyrazinamide into the bacteriostatic pyrazinoic acid
activates, best cation, the active site Cys159 is located at the N-terminus of a6 at one side of the active site with the Zn2+ ion positioned on the other side. The metal ion is bound tightly in the AbPncA active site
Zn2+ increases the kcat of the enzyme by about 19-fold. fold. Other divalent ions, including Mg2+, Mn2+, Ca2+, and Cd2+, do not increase the activity. A metal ion-binding site is revealed in the active site and confirmed by crystal structure of the enzyme in complex with Zn2+
the reaction product pyrazinoic acid inhibits Mycobacterium tuberculosis type I fatty acid synthase, represses mycolic acid biosynthesis, and appears to affect membrane energetics and acidification of the cytoplasm
protein conformational changes after ligand dissociation, molecular dynamics simulation methods are performed to investigate the unbinding process of nicotinamide using the enzyme's crystal structure. PDB ID 2WT9
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
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
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
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
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3.5.1.B15 pyrazinamidase
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