KEGG   ENZYME: 3.2.2.14
Entry
EC 3.2.2.14                 Enzyme                                 
Name
NMN nucleosidase;
NMNase;
nicotinamide mononucleotide nucleosidase;
nicotinamide mononucleotidase;
NMN glycohydrolase;
NMNGhase
Class
Hydrolases;
Glycosylases;
Hydrolysing N-glycosyl compounds
Sysname
nicotinamide-nucleotide phosphoribohydrolase
Reaction(IUBMB)
beta-nicotinamide D-ribonucleotide + H2O = D-ribose 5-phosphate + nicotinamide [RN:R01270]
Reaction(KEGG)
R01270
Substrate
beta-nicotinamide D-ribonucleotide [CPD:C00455];
H2O [CPD:C00001]
Product
D-ribose 5-phosphate [CPD:C00117];
nicotinamide [CPD:C00153]
Comment
The enzyme is thought to participate in an NAD+-salvage pathway. In eukaryotic organisms this activity has been attributed to EC 3.2.2.6, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
History
EC 3.2.2.14 created 1976, modified 2018
Pathway
ec00760  Nicotinate and nicotinamide metabolism
Reference
1  [PMID:4342726]
  Authors
Andreoli AJ, Okita TW, Bloom R, Grover TA.
  Title
The pyridine nucleotide cycle: presence of a nicotinamide mononucleotide-specific glycohydrolase in Escherichia coli.
  Journal
Biochem Biophys Res Commun 49:264-9 (1972)
DOI:10.1016/0006-291X(72)90039-3
Reference
2  [PMID:457634]
  Authors
Imai T
  Title
Isolation and properties of a glycohydrolase specific for nicotinamide mononucleotide from Azotobacter vinelandii.
  Journal
J Biochem 85:887-99 (1979)
DOI:10.1093/oxfordjournals.jbchem.a132420
Reference
3  [PMID:3571198]
  Authors
Imai T
  Title
Properties of allosteric nicotinamide mononucleotide glycohydrolase from Azotobacter vinelandii: activation and inhibition.
  Journal
J Biochem 101:163-73 (1987)
DOI:10.1093/oxfordjournals.jbchem.a121887
Other DBs
ExplorEnz - The Enzyme Database: 3.2.2.14
IUBMB Enzyme Nomenclature: 3.2.2.14
ExPASy - ENZYME nomenclature database: 3.2.2.14
BRENDA, the Enzyme Database: 3.2.2.14
CAS: 37237-49-3

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