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 2PGJ
External Links
Method X-RAY DIFFRACTION
Organism Pichia
Primary Citation
Catalysis-associated Conformational Changes Revealed by Human CD38 Complexed with a Non-hydrolyzable Substrate Analog
Liu, Q., Kriksunov, I.A., Moreau, C., Graeff, R., Potter, B.V., Lee, H.C., Hao, Q.
J.Biol.Chem.