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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyrazinamide + H2O | Bacillus subtilis | - |
pyrazinoic acid + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyrazinamide + H2O | - |
Bacillus subtilis | pyrazinoic acid + NH3 | - |
? |
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 | Comment | Organism |
---|---|---|
BsPncA | - |
Bacillus subtilis |
More | cf. EC 3.5.1.19 | Bacillus subtilis |
nicotinamidase/pyrazinamidase | - |
Bacillus subtilis |
PncA | - |
Bacillus subtilis |
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 |