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Literature summary for 3.5.1.B15 extracted from
- Crystal structure of the nicotinamidase/pyrazinamidase PncA from Bacillus subtilis (2018), Biochem. Biophys. Res. Commun., 503, 2906-2911 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| determination and analysis of the crystal structure of substrate-free PncA from Bacillus subtilis (BsPncA) at 2.0 A resolution | Bacillus subtilis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyrazinamide + H2O | Bacillus subtilis | - |
pyrazinoic acid + NH3 | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pyrazinamide + H2O | - |
Bacillus subtilis | pyrazinoic acid + NH3 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| 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 | Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BsPncA | - |
Bacillus subtilis |
| More | cf. EC 3.5.1.19 | Bacillus subtilis |
| nicotinamidase/pyrazinamidase | - |
Bacillus subtilis |
| PncA | - |
Bacillus subtilis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the nicotinamidase/pyrazinamidase PncA is a member of a large family of hydrolase enzymes that catalyze the deamination of nicotinamide to nicotinic acid | Bacillus subtilis |
| physiological function | nicotinamidase/pyrazinamidase PncA catalyzes the deamination of nicotinamide to nicotinic acid (EC 3.5.1.19). PncA also functions as a pyrazinamidase in a wide variety of eubacteria and is an essential coenzyme in many cellular redox reactions in living systems | Bacillus subtilis |
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Release 2023.1 (January 2023)
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