Biology:NAD+ nucleosidase

From HandWiki
NAD+ nucleosidase
Identifiers
EC number3.2.2.5
CAS number9032-65-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a NAD+ nucleosidase (EC 3.2.2.5) is an enzyme that catalyzes the chemical reaction

NAD+ + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 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. Calcium Metabolism involves the regulation of the levels of calcium in the body. The role this calcium plays also includes providing enough calcium for bone mineralization. It serves as the basis for the structure and rigidity of bones. Calcium metabolism can lead to a variety of diseases which can involve renal function. High concentrations of calcium can lead to cell death or apoptosis.

References

Further reading

  • "[DPN- and TPN-specific nucleosidases in erythrocytes]". Biochimica et Biophysica Acta 18 (2): 296. October 1955. doi:10.1016/0006-3002(55)90076-7. PMID 13276383. 
  • "Nicotinamide adenine dinucleotide glycohydrolases and poly adenosine diphosphate ribose synthesis in rat liver". Biochemical and Biophysical Research Communications 32 (2): 143–9. July 1968. doi:10.1016/0006-291X(68)90360-4. PMID 5672131. 
  • "Nicotinamide adenine dinucleotide glycohydrolase from rat liver nuclei. Isolation and characterization of a new enzyme". The Journal of Biological Chemistry 250 (19): 7541–6. October 1975. doi:10.1016/S0021-9258(19)40852-1. PMID 240831. 
  • "Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities". Journal of Molecular Biology 316 (3): 711–23. February 2002. doi:10.1006/jmbi.2001.5386. PMID 11866528. 
  • "Rare diseases of phosphate and calcium metabolism: Crossing glances between nephrology and endocrinology". Annales d'Endocrinologie 82 (1): 30–35. February 2021. doi:10.1016/j.ando.2020.12.005. PMID 33316222.