EC Number   |
Subunits |
Reference |
|---|
   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 | More |
enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1) |
-, 757474 |
| 3.5.1.B15 | More |
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 |
