EC Number |
General Information |
Reference |
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3.2.2.6 | evolution |
the CD38-cADPR signaling system is conserved during vertebrate evolution, phylogenetic tree |
732501 |
3.2.2.6 | malfunction |
ablation of the CD38 gene in mice causes multiple physiological defects, including impaired oxytocin release, that result in altered social behavior |
731296 |
3.2.2.6 | malfunction |
CD38 knockout mice manifest multiple defects relating to Ca2+ signaling, including that of insulin secretion, hormonal signaling in pancreatic acinar cells, migration of dendritic cell precursors, bone resorption, airway responsiveness, alpha-adrenoceptor signaling in aorta, cardiac hypertrophy, susceptibility to bacterial infection, as well as social behavior in mice through modulation of oxytocin secretion |
716910 |
3.2.2.6 | malfunction |
CD38 reductions lead to microglial apoptosis. inhibition of CD38/cADPR-dependent signaling by CD38 silencing or 8-bromo-cADPR, a ryanodine receptor antagonist, produced significant ATP release from BV2 microglia. Cx43 small interfering RNA and Cx43 hemichannel blocker 18-alpha-glycyrrhetinic acid completely prevented the CD38 silencing or 8-bromo-cADPR-induced ATP release. Prevention of the ATP release might also be due to P2X7 receptor antagonists. Key role of ATP release in the microglial apoptosis induced by decreased CD38/cADPR-dependent signaling, overview |
731882 |
3.2.2.6 | more |
D226/Q226 and K129 residues of the two CD38 enzyme are the ADP-ribosylation sites. 6-Alkyne-F-araNAD, 6-alkyne-NAD, and Rh-N3 are used in the labeling reactions of CD38 wild-type and mutants, overview |
731119 |
3.2.2.6 | more |
invariant glutamate 218 identified is the catalytic residue of the enzyme, Structure homology modelling, overview |
732691 |
3.2.2.6 | more |
structure-function analysis, overview. The enzyme catalyzes the formation of beta-1'-O-methyl ADP-ribose in presence of methanol, solvolysis does not affect the overall turnover rate of NAD+ by the wild-type enzyme. Precise role of key conserved active site residues Trp118, Glu138, Asp147, Trp181 and Glu218, effects of experiments with neutral (methanol) and ionic (azide, formate) nucleophiles. Binding of 2'-fluorinated analogs of NAD+ and trappping of the reaction intermediate, detailed overview. Catalytic residue Glu138 is part of the TLEDTL signature domain, Asp147 is a highly conserved residue in the enzyme and is important for the catalytic parameters. Cooperative contribution of Trp118 and Trp181 to catalysis |
731357 |
3.2.2.6 | more |
structure-function relationship anaysis, overview. Covalent intermediates are formed with the catalytic residue, Glu226 |
731296 |
3.2.2.6 | physiological function |
CD38 is an ectoenzyme that consumes NAD+ to produce cyclic ADP-ribose, a potent agonist of ryanodine receptors. Basal CD38/cyclic ADP-ribose-dependent signaling plays a key role in ATP release, which mediates basal survival of microglia, overview |
731882 |
3.2.2.6 | physiological function |
CD38 is an NAD+-metabolizing enzyme in mammals, a type II transmembrane protein that converts NAD+ primarily to adenosine diphosphate ribose and a small amount of cyclic adenosine diphosphate ribose. The major enzymatic function of the enzyme is to hydrolyze extracellular rather than intracellular NAD+ |
731987 |