Nicotinamide-nucleotide amidase
| nicotinamide-nucleotide amidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.1.42 | ||||||||
| CAS number | 37355-58-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a nicotinamide-nucleotide amidase (EC 3.5.1.42) is an enzyme that catalyzes the chemical reaction
- beta-nicotinamide D-ribonucleotide + H2O beta-nicotinate D-ribonucleotide + NH3
Thus, the two substrates of this enzyme are beta-nicotinamide D-ribonucleotide and H2O, whereas its two products are beta-nicotinate D-ribonucleotide and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is nicotinamide-D-ribonucleotide amidohydrolase. Other names in common use include NMN deamidase, nicotinamide mononucleotide deamidase, and nicotinamide mononucleotide amidohydrolase. This enzyme participates in nicotinate and nicotinamide metabolism.
References
- Imai T (January 1973). "Purification and properties of nicotinamide mononucleotide amidohydrolase from Azotobacter vinelandii". J. Biochem. Tokyo. 73 (1): 139&ndash, 53. PMID 4144084.
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