ExplorEnz: EC 3.2.2.6

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3.2.2.6

Accepted name:

ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

Reaction:

NAD⁺ + H₂O = ADP-D-ribose + nicotinamide (overall reaction)
(1a) NAD⁺ = cyclic ADP-ribose + nicotinamide
(1b) cyclic ADP-ribose + H₂O = ADP-D-ribose

For diagram of cyclic ADP-ribose biosynthesis, click here

Glossary:

ADP-D-ribose = adenosine 5′-(5-deoxy-D-ribofuranos-5-yl diphosphate)
cyclic ADP-ribose = N¹-(β-D-ribosyl)adenosine 5′(P1),5′′(P2)-cyclic diphosphate

Other name(s):

NAD⁺ nucleosidase; NADase (ambiguous); DPNase (ambiguous); DPN hydrolase (ambiguous); NAD hydrolase (ambiguous); nicotinamide adenine dinucleotide nucleosidase (ambiguous); NAD glycohydrolase (misleading); NAD nucleosidase (ambiguous); nicotinamide adenine dinucleotide glycohydrolase (misleading); CD38 (gene name); BST1 (gene name)

Systematic name:

NAD⁺ glycohydrolase (cyclic ADP-ribose-forming)

Comments:

This multiunctional enzyme acts on NAD⁺, catalysing both the synthesis and hydrolysis of cyclic ADP-ribose, a calcium messenger that can mobilize intracellular Ca²⁺ stores and activate Ca²⁺ influx to regulate a wide range of physiological processes. In addition, the enzyme also catalyses EC 2.4.99.20, 2′-phospho-ADP-ribosyl cyclase/2′-phospho-cyclic-ADP-ribose transferase. It is also able to act on β-nicotinamide D-ribonucleotide. cf. EC 3.2.2.5, NAD⁺ glycohydrolase.

Links to other databases:

BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9032-65-9

References:

1.	Imai, T. Purification and characterization of a pyridine nucleotide glycohydrolase from rabbit spleen. J. Biochem. 106 (1989) 928–937. [PMID: 2613697]
2.	Howard, M., Grimaldi, J.C., Bazan, J.F., Lund, F.E., Santos-Argumedo, L., Parkhouse, R.M., Walseth, T.F. and Lee, H.C. Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38. Science 262 (1993) 1056–1059. [DOI] [PMID: 8235624]
3.	Takasawa, S., Tohgo, A., Noguchi, N., Koguma, T., Nata, K., Sugimoto, T., Yonekura, H. and Okamoto, H. Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP. J. Biol. Chem. 268 (1993) 26052–26054. [PMID: 8253715]
4.	Tohgo, A., Takasawa, S., Noguchi, N., Koguma, T., Nata, K., Sugimoto, T., Furuya, Y., Yonekura, H. and Okamoto, H. Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis by CD38. J. Biol. Chem. 269 (1994) 28555–28557. [PMID: 7961800]
5.	Fryxell, K.B., O'Donoghue, K., Graeff, R.M., Lee, H.C. and Branton, W.D. Functional expression of soluble forms of human CD38 in Escherichia coli and Pichia pastoris. Protein Expr. Purif. 6 (1995) 329–336. [DOI] [PMID: 7663169]
6.	Yamamoto-Katayama, S., Ariyoshi, M., Ishihara, K., Hirano, T., Jingami, H. and Morikawa, K. Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities. J. Mol. Biol. 316 (2002) 711–723. [DOI] [PMID: 11866528]
7.	Liu, Q., Kriksunov, I.A., Graeff, R., Munshi, C., Lee, H.C. and Hao, Q. Crystal structure of human CD38 extracellular domain. Structure 13 (2005) 1331–1339. [DOI] [PMID: 16154090]

[EC 3.2.2.6 created 1961, modified 2004, modified 2014, modified 2018]