| Entry |
|
| Name |
nicotinamide-nucleotide amidase;
NMN deamidase;
nicotinamide mononucleotide deamidase;
nicotinamide mononucleotide amidohydrolase |
| Class |
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
 |
| Sysname |
nicotinamide-D-ribonucleotide amidohydrolase |
| Reaction(IUBMB) |
beta-nicotinamide D-ribonucleotide + H2O = beta-nicotinate
D-ribonucleotide + NH3 [RN:R02322] |
| Reaction(KEGG) |
R02322;
(other) R06134
 |
| Substrate |
beta-nicotinamide D-ribonucleotide [CPD:C00455];
H2O [CPD:C00001] |
| Product |
beta-nicotinate D-ribonucleotide [CPD:C01185];
NH3 [CPD:C00014] |
| Comment |
Also acts more slowly on beta-nicotinamide D-ribonucleoside. |
| Pathway |
PATH: ec00760 Nicotinate and nicotinamide metabolism |
Reference Authors Title
Journal Organism
|
1 [PMID:4144084]
Imai T.
Purification and properties of nicotinamide mononucleotide
amidohydrolase from Azotobacter vinelandii.
J. Biochem. (Tokyo). 73 (1973) 139-53.
Azotobacter vinelandii [GN:avn] |
| Other DBs |
ExplorEnz - The Enzyme Database: 3.5.1.42
IUBMB Enzyme Nomenclature: 3.5.1.42
ExPASy - ENZYME nomenclature database: 3.5.1.42
BRENDA, the Enzyme Database: 3.5.1.42
CAS: 37355-58-1 |