NAD+ nucleosidase
| NAD+ nucleosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.2.2.5 | ||||||||
| CAS number | 9032-65-9 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a NAD+ nucleosidase (EC 3.2.2.5) is an enzyme that catalyzes the chemical reaction
- NAD+ + H2O ADP-ribose + nicotinamide
Thus, the two substrates of this enzyme are NAD+ and H2O, whereas its two products are ADP-ribose and nicotinamide.
This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is NAD+ glycohydrolase. Other names in common use include NADase, DPNase, DPN hydrolase, NAD hydrolase, diphosphopyridine nucleosidase, nicotinamide adenine dinucleotide nucleosidase, NAD glycohydrolase, NAD nucleosidase, and nicotinamide adenine dinucleotide glycohydrolase. This enzyme participates in nicotinate and nicotinamide metabolism and calcium signaling pathway.
Structural studies
As of late 2007, 25 structures have been solved for this class of enzymes, with PDB accession codes 1ISF, 1ISG, 1ISH, 1ISI, 1ISJ, 1ISM, 1LBE, 1R0S, 1R12, 1R15, 1R16, 1YH3, 1ZVM, 2EF1, 2HCT, 2I65, 2I66, 2I67, 2O3Q, 2O3R, 2O3S, 2O3T, 2O3U, 2PGJ, and 2PGL.
References
- HOFMANN EC, RAPOPORT S (1955). "[DPN- and TPN-specific nucleosidases in erythrocytes.]". Biochim. Biophys. Acta. 18 (2): 296. doi:10.1016/0006-3002(55)90076-7. PMID 13276383.
- Nakazawa K, Ueda K, Honjo T, Yoshihara K, Nishizuka Y, Hayaishi O (1968). "Nicotinamide adenine dinucleotide glycohydrolases and poly adenosine diphosphate ribose synthesis in rat liver". Biochem. Biophys. Res. Commun. 32 (2): 143–9. doi:10.1016/0006-291X(68)90360-4. PMID 5672131.
- Ueda K, Fukushima M, Okayama H, Hayaishi O (1975). "Nicotinamide adenine dinucleotide glycohydrolase from rat liver nuclei. Isolation and characterization of a new enzyme". J. Biol. Chem. 250 (19): 7541–6. PMID 240831.
- Morikawa K; Ariyoshi, M; Ishihara, K; Hirano, T; Jingami, H; Morikawa, K (2002). "Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities". J. Mol. Biol. 316 (3): 711–23. doi:10.1006/jmbi.2001.5386. PMID 11866528.