Application | Comment | Organism |
---|---|---|
drug development | while nicotinamidases are widespread in nature they are not occuring within mammals and present a potential drug target. The enzymes can be used in the activation of tuberculosis prodrugs such as pyrazinamide | Streptococcus pneumoniae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | zinc-dependent enzyme | Streptococcus pneumoniae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
nicotinamide + H2O | Streptococcus pneumoniae | - |
nicotinate + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptococcus pneumoniae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
nicotinamide + H2O = nicotinate + NH3 | catalytic mechanism in two stages: (i) formation of a tetrahedral thioester enzyme-substrate intermediate (with the sulfur of Cys136 nucleophilically attacks the nicotinamidase substrate's carbonyl carbon while concomitantly the Cys136-SH thiol proton is transferred onto the substrate's amide group nitrogen) and (ii) hydrolysis of the thioester bond to give the products, overview. The catalytic triad comprises Lys103, Asp9, and Cys136, substrate binding and roles of active site residues of the enzyme from Streptococcus pneumoniae. The active site Lys103 likely plays a role in stabilizing the thiolate of Cys136 during the reaction | Streptococcus pneumoniae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nicotinamide + H2O | - |
Streptococcus pneumoniae | nicotinate + NH3 | - |
? | |
pyrazinamide + H2O | - |
Streptococcus pneumoniae | pyrazinoic acid + NH3 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
NIC | - |
Streptococcus pneumoniae |
nicotinamidase | - |
Streptococcus pneumoniae |
SpNic | - |
Streptococcus pneumoniae |
General Information | Comment | Organism |
---|---|---|
evolution | nicotinamidases are a family of peptide hydrolases that generally contain a Zn2+ ion | Streptococcus pneumoniae |
metabolism | nicotinamidase is a key enzyme in NAD+ metabolism | Streptococcus pneumoniae |
additional information | catalytic mechanism, substrate binding and roles of active site residues, quantum mechanics/molecular mechanics methods and modeling, overview. The polar protein environment has a significant effect in stabilizing reaction intermediates and in particular transition states | Streptococcus pneumoniae |