CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

Enzyme Information

3.2.2.6
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
based on mapping to UniProt P28907
NAD(+) + H(2)O = ADP-D-ribose + nicotinamide.
-!- This multiunctional enzyme catalyzes both the synthesis and hydrolysis of cyclic ADP-ribose, a calcium messenger that can mobilize intracellular Ca(2+) stores and activate Ca(2+) influx to regulate a wide range of physiological processes. -!- In addition, the enzyme also catalyzes EC 2.4.99.20. -!- It is also able to act on beta-nicotinamide D-ribonucleotide. -!- Cf. EC 3.2.2.5.
2.4.99.20
2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase.
based on mapping to UniProt P28907
NADP(+) + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide.
-!- This multiunctional enzyme catalyzes both the removal of nicotinamide from NADP(+), forming 2'-phospho-cyclic ADP-ribose, and the addition of nicotinate to the cyclic product, forming NAADP(+), a calcium messenger that can mobilize intracellular Ca(2+) stores and activate Ca(2+) influx to regulate a wide range of physiological processes. -!- In addition, the enzyme also catalyzes EC 3.2.2.6.

UniProtKB Entries (1)

P28907
CD38_HUMAN
Homo sapiens
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1

PDB Structure

PDB 4XJS
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Discovery of 4-Amino-8-quinoline Carboxamides as Novel, Submicromolar Inhibitors of NAD-Hydrolyzing Enzyme CD38.
Becherer, J.D., Boros, E.E., Carpenter, T.Y., Cowan, D.J., Deaton, D.N., Haffner, C.D., Jeune, M.R., Kaldor, I.W., Poole, J.C., Preugschat, F., Rheault, T.R., Schulte, C.A., Shearer, B.G., Shearer, T.W., Shewchuk, L.M., Smalley, T.L., Stewart, E.L., Stuart, J.D., Ulrich, J.C.
J.Med.Chem.
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