NAD+ glycohydrolase
From Wikipedia the free encyclopedia
| NAD+ glycohydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifiers | |||||||||
| EC no. | 3.2.2.5 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
In enzymology, a NAD+ glycohydrolase (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. Unlike ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase (EC 3.2.2.6), which catalyzes the same reaction, this reaction does not proceed through a cyclic ADP-ribose.[1][2]
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 NAD+ nucleosidase, 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[edit]
- Mosca, Melodie (2021). "Rare diseases of phosphate and calcium metabolism: Crossingglances between nephrology and endocrinology Rare pathologies of calcium and phosphorus: crossed views between nephrology and endocrinology". Annales d'Endocrinologie. 82 (1): 30–35. doi:10.1016/j.ando.2020.12.005. PMID 33316222. S2CID 229174185.
- Putney, J. W. P. (2019). Calcium Metabolism. Access Science. https://www.accessscience.com/content/calcium-metabolism/103100
- ^ "ENZYME - 3.2.2.5 NAD(+) glycohydrolase". enzyme.expasy.org. Retrieved 2022-07-11.
- ^ "ENZYME - 3.2.2.6 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase". enzyme.expasy.org. Retrieved 2022-07-11.
Further reading[edit]
- Hofmann EC, Rapoport S (October 1955). "[DPN- and TPN-specific nucleosidases in erythrocytes]". Biochimica et Biophysica 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 (July 1968). "Nicotinamide adenine dinucleotide glycohydrolases and poly adenosine diphosphate ribose synthesis in rat liver". Biochemical and Biophysical Research Communications. 32 (2): 143–9. doi:10.1016/0006-291X(68)90360-4. PMID 5672131.
- Ueda K, Fukushima M, Okayama H, Hayaishi O (October 1975). "Nicotinamide adenine dinucleotide glycohydrolase from rat liver nuclei. Isolation and characterization of a new enzyme". The Journal of Biological Chemistry. 250 (19): 7541–6. doi:10.1016/S0021-9258(19)40852-1. PMID 240831.
- Yamamoto-Katayama S, Ariyoshi M, Ishihara K, Hirano T, Jingami H, Morikawa K (February 2002). "Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities". Journal of Molecular Biology. 316 (3): 711–23. doi:10.1006/jmbi.2001.5386. PMID 11866528.
- Mosca M, Bernardor J, Lemoine S, Bertholet-Thomas A, Bacchetta J (February 2021). "Rare diseases of phosphate and calcium metabolism: Crossing glances between nephrology and endocrinology". Annales d'Endocrinologie. 82 (1): 30–35. doi:10.1016/j.ando.2020.12.005. PMID 33316222. S2CID 229174185.
.svg){kind=small} | This biochemistry article is a stub. You can help Wikipedia by expanding it. |