EC 3.2.2.6 - ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase

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IntEnz Enzyme Nomenclature
EC 3.2.2.6

Names

Accepted name:
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Other names:
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)

Reactions

Comments:

This multiunctional enzyme catalyses 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. cf. It is also able to act on β-nicotinamide D-ribonucleotide. EC 3.2.2.5, NAD+ glycohydrolase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050135 , GO:0061809
CAS Registry Number: 9025-46-1
UniProtKB/Swiss-Prot: (184) [show] [UniProt]

References

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

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