3.5.1.B15	dimer	-	710862	
3.5.1.B15	dimer or tetramer	the structure of BsPncA consists of an alpha/beta domain and a subdomain. The subdomain of BsPncA has a different conformation compared to PncA enzymes from other organisms. The B-factor analysis reveals a rigid structure of the alpha/beta domain, while the subdomain is highly flexible. Both dimers and tetramers are observed in BsPncA protein crystals, but only dimers are observed in solution	752683	
3.5.1.B15	homodimer	-	-, 727053	
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	-, 735324	
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	-, 735324	
3.5.1.B15	additional information	enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)	-, 757474	
3.5.1.B15	additional information	PZase consists of six parallel beta-sheets surrounded by alpha-helices. The metal binding site contains iron (Fe2+ ion) in coordination with one aspartate (Asp49) and three histidines residues (His51, His57, and His71), while Asp8, Lys96, and Cys138 form the catalytic triad	-, 757293