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EC Tree
IUBMB 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 beta-nicotinamide D-ribonucleotide. cf. EC 3.2.2.5, NAD+ glycohydrolase.
The taxonomic range for the selected organisms is: Homo sapiens The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
adp-ribosyl cyclase, adpr cyclase, nad(p)ase, nad(p)-glycohydrolase, bcd38, adp-ribosyl cyclase/cyclic adp-ribose hydrolase, nad(p)+ glycohydrolase,
more
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NAD(P)+ glycohydrolase
-
-
-
-
NAD(P)+-glycohydrolase
-
-
NAD(P)-glycohydrolase
-
-
-
-
nicotinamide adenine dinucleotide (phosphate) glycohydrolase
-
-
-
-
nicotinamide adenine dinucleotide (phosphate) nucleosidase
-
-
-
-
nucleosidase, nicotinamide adenine dinucleotide (phosphate)
-
-
-
-
triphosphopyridine nucleotidase
-
-
-
-
CD38
-
-
-
-
NAD(P) nucleosidase
-
-
-
-
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NAD+ + H2O = ADP-D-ribose + nicotinamide
reaction mechanism, overview
NAD+ + H2O = ADP-D-ribose + nicotinamide
also catalyses transfer of ADP-ribose(P) residues
-
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hydrolysis of N-glycosyl bond
-
-
-
-
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NAD+ glycohydrolase (cyclic ADP-ribose-forming)
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 beta-nicotinamide D-ribonucleotide. cf. EC 3.2.2.5, NAD+ glycohydrolase.
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cyclic ADP-ribose + H2O
ADP-D-ribose
-
-
-
?
NAD+
cyclic ADP-ribose + nicotinamide
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
1,N6-etheno NAD+ + H2O
epsilon-ADP-ribose + nicotinamide + H+
-
-
-
-
?
3-acetylpyridine + adenosine diphosphoribose
3-acetylpyridine adenine dinucleotide + phosphate
-
transglycosylation activity, very poor hydrolytic activity with this substrate
-
-
?
3-acetylpyridine adenine dinucleotide + H2O
?
-
-
-
-
?
3-acetylpyridine hypoxanthine dinucleotide + H2O
?
-
low activity
-
-
?
3-pyridine adenine dinucleotide + H2O
?
-
-
-
-
?
3-pyridinealdehyde hypoxanthine dinucleotide + H2O
?
alpha-NAD+ + H2O
?
-
-
-
-
?
beta-NAD+ + H2O
?
-
-
-
-
?
cyclic ADP-ribose + H2O
?
-
-
-
-
?
cyclic ADP-ribose + H2O
adenosine diphosphoribose + ?
-
i.e. ADPR activity
-
-
?
epsilon-NAD+ + H2O
?
-
-
-
-
?
epsilon-NADP+ + H2O
?
-
-
-
-
?
NAD+
cyclic ADP-ribose + nicotinamide
-
-
-
?
NAD+ + ?
cyclic ADP-ribose + ?
-
i.e. cADPR activity
-
-
?
NAD+ + H2O
ADP-ribose + nicotinamide
-
-
-
-
?
NADP+ + H2O
ADP-ribose-P + nicotinamide
-
80% activity compared to the activity with NAD+
-
-
?
NADP+ + H2O
nicotinamide + ADPribose-phosphate
NGD+ + H2O
cyclic GDP-ribose
-
-
-
-
?
NGD+ + H2O
GDP-ribose + nicotinamide
-
as effective as substrate as NAD+
-
-
?
nicotinamide 1,N6-ethenoadenine dinucleotide + H2O
?
-
i.e. epsilonNAD+, used for a fluorometric assay
-
-
?
nicotinamide guanine dinucleotide + H2O
?
-
-
-
-
?
nicotinamide-hypoxanthine dinucleotide + H2O
?
-
-
-
-
?
thio-NAD+ + H2O
?
-
-
-
-
?
additional information
?
-
NAD+ + H2O
ADP-D-ribose + nicotinamide
overall reaction
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
via a stepwise reaction mechanism
-
-
?
3-pyridinealdehyde hypoxanthine dinucleotide + H2O
?
-
-
-
-
?
3-pyridinealdehyde hypoxanthine dinucleotide + H2O
?
-
60% activity compared to the activity with NAD+
-
-
?
NADP+ + H2O
nicotinamide + ADPribose-phosphate
-
-
-
-
?
NADP+ + H2O
nicotinamide + ADPribose-phosphate
-
-
-
?
additional information
?
-
-
the formation of an enzyme-ADP-ribosyl intermediary complex is common to all reaction pathways
-
-
?
additional information
?
-
-
enzyme is involved in the regulation of intracellular concentration of adenosine diphosphoribose
-
-
?
additional information
?
-
-
enzyme is multicatalytic, it also catalyzes the synthesis of cyclic ADP-ribose from NAD+ and the hydrolysis to adenosine diphosphoribose
-
-
?
additional information
?
-
-
CD38 is a multifunctional enzyme catalyzing the conversion of NAD(P)+ to three metabolites (cyclic ADP-ribose, nicotinic acid adenine dinucleotide phosphate and ADP-ribose)
-
-
?
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cyclic ADP-ribose + H2O
ADP-D-ribose
-
-
-
?
NAD+
cyclic ADP-ribose + nicotinamide
-
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
additional information
?
-
-
enzyme is involved in the regulation of intracellular concentration of adenosine diphosphoribose
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
overall reaction
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
via a stepwise reaction mechanism
-
-
?
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Cu2+
-
stimulation of cADPR activity
additional information
-
no effects by K+, Cd2+, Fe2+, Fe3+, and Mn2+
Ag+
-
50% inhibition of NADase and 300% activation of adenosine diphosphate cyclase
Ag+
-
at 2 mM 50% inhibition of NADase activity and 300% activation of ADPR activity
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1-[2-azido-2-deoxy-5-O-phosphono-D-threo-pentofuranosyl]-3-carbamoylpyridinium
inhibition of the NADase activity
1-[5-O-[(benzyloxy)(hydroxy)phosphoryl]-2-deoxy-2-fluoro-L-erythro-pentofuranosyl]-3-carbamoylpyridinium
inhibition of the NADase activity
1-[5-O-[butoxy(hydroxy)phosphoryl]-2-deoxy-2-fluoro-D-threo-pentofuranosyl]-3-carbamoylpyridinium
inhibition of the NADase activity
3-carbamoyl-1-[2-chloro-2-deoxy-5-O-phosphono-D-threo-pentofuranosyl]pyridinium
inhibition of the NADase activity
3-carbamoyl-1-[2-deoxy-2-fluoro-5-O-phosphono-D-threo-pentofuranosyl]pyridinium
inhibition of the NADase activity
3-carbamoyl-1-[2-deoxy-2-fluoro-5-O-phosphono-L-threo-pentofuranosyl]pyridinium
inhibition of the NADase activity
3-carbamoyl-1-[2-deoxy-2-fluoro-5-O-thiophosphono-L-erythro-pentofuranosyl]pyridinium
inhibition of the NADase activity
3-carbamoyl-1-[2-deoxy-2-fluoro-5-O-[(hexyloxy)(hydroxy)phosphoryl]-D-threo-pentofuranosyl]pyridinium
inhibition of the NADase activity
3-carbamoyl-1-[2-deoxy-2-fluoro-5-O-[hydroxy(2-phenylethoxy)phosphoryl]-L-erythro-pentofuranosyl]pyridinium
inhibition of the NADase activity
3-carbamoyl-1-[2-deoxy-2-fluoro-D-threo-pentofuranosyl]pyridinium
inhibition of the NADase activity
3-carbamoyl-1-[2-deoxy-5-O-(diethoxyphosphoryl)-2-fluoro-D-threo-pentofuranosyl]pyridinium
inhibition of the NADase activity
3-carbamoyl-1-[2-deoxy-5-O-[(ethenyloxy)(propoxy)phosphoryl]-2-fluoro-D-threo-pentofuranosyl]pyridinium
inhibition of the NADase activity
3-carbamoyl-1-[3-deoxy-3-fluoro-5-O-phosphono-L-threo-pentofuranosyl]pyridinium
inhibition of the NADase activity
arabinosyl-2'-fluoro-2'-deoxynicotinamide mononucleotide
inhibition of the NADase activity
5,7-dihydroxy-2-(3-hydroxy-4-methoxyphenyl)chromenium
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-
arabinosyl 2'-fluoro-2'-deoxy-NAD
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suicide substrate that inhibits CD38 ectoenzyme activity
additional information
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not inhibited by rac-taxifolin, rac-catechin, piceatannol, and trans-resveratrol
-
Ag+
-
50% inhibition of NADase and 300% activation of adenosine diphosphate cyclase
Ag+
-
at 2 mM 50% inhibition of NADase activity and 300% activation of cADPR activity
Cr3+
-
-
Cr3+
-
inhibition of NADase and adenosine diphosphate cyclase
Hg2+
-
complete inhibition at 2 mM
Hg2+
-
inhibition of NADase and adenosine diphosphate cyclase
Pb2+
-
complete inhibition at 2 mM
Pb2+
-
inhibition of NADase and adenosine diphosphate cyclase
Sn2+
-
complete inhibition at 2 mM
Sn2+
-
inhibition of NADase and adenosine diphosphate cyclase
Zn2+
-
-
Zn2+
-
inhibition of NADase and adenosine diphosphate cyclase
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Adenoma
The expression of messenger RNA for ADP-ribosyl cyclase in aldosterone-producing adenomas.
adenylate cyclase deficiency
An enzymatic alteration secondary to adenylyl cyclase deficiency in the cr-1 (crisp) mutant of Neurospora crassa: nicotinamide adenine dinucleotide (phosphate) glycohydrolase overproduction.
Anemia
Erythrocyte CD38 as a prognostic marker in cancer.
Brain Injuries
Perinatal hypoxic-ischemic brain injury affects the glutamatergic signal transduction coupled with neuronal ADP-ribosyl cyclase activity.
Cardiomegaly
Inhibition of ADP-ribosyl cyclase attenuates angiotensin II-induced cardiac hypertrophy.
Diabetic Nephropathies
Role of kidney ADP-ribosyl cyclase in diabetic nephropathy.
Glioma
Muscarinic receptor-mediated dual regulation of ADP-ribosyl cyclase in NG108-15 neuronal cell membranes.
Glioma
Signal transduction from bradykinin, angiotensin, adrenergic and muscarinic receptors to effector enzymes, including ADP-ribosyl cyclase.
Glioma
Subtype-specific coupling with ADP-ribosyl cyclase of metabotropic glutamate receptors in retina, cervical superior ganglion and NG108-15 cells.
Lupus Erythematosus, Systemic
CD38 polymorphisms in Spanish patients with systemic lupus erythematosus.
Multiple Myeloma
Daratumumab and Nanobody-Based Heavy Chain Antibodies Inhibit the ADPR Cyclase but not the NAD+ Hydrolase Activity of CD38-Expressing Multiple Myeloma Cells.
Myocardial Ischemia
Myocardial ischemia and reperfusion reduce the levels of cyclic ADP-ribose in rat myocardium.
Neoplasms
cADP-ribose/ryanodine channel/Ca2+-release signal transduction pathway in mesangial cells.
Neoplasms
CD38 and Regulation of the Immune Response Cells in Cancer.
Neoplasms
Changes in NAD/ADP-ribose metabolism in rectal cancer.
Neoplasms
Cyclic ADP-ribose as a potential second messenger for neuronal Ca2+ signaling.
Neoplasms
Erythrocyte CD38 as a prognostic marker in cancer.
Nervous System Diseases
Role of ADP-ribosyl cyclase in the pathogenesis of neurological disorders after coronary artery bypass surgery and experimental ischemia.
Neuroblastoma
Bradykinin activates ADP-ribosyl cyclase in neuroblastoma cells: intracellular concentration decrease in NAD and increase in cyclic ADP-ribose.
Neuroblastoma
Muscarinic receptor-mediated dual regulation of ADP-ribosyl cyclase in NG108-15 neuronal cell membranes.
Neuroblastoma
Signal transduction from bradykinin, angiotensin, adrenergic and muscarinic receptors to effector enzymes, including ADP-ribosyl cyclase.
Neuroblastoma
Subtype-specific coupling with ADP-ribosyl cyclase of metabotropic glutamate receptors in retina, cervical superior ganglion and NG108-15 cells.
Rectal Neoplasms
Changes in NAD/ADP-ribose metabolism in rectal cancer.
Tuberculosis
[NAD(P)-glycohydrolase in tuberculosis bacteria. A contribution to the mechanism of action INH]
Uterine Cervical Neoplasms
Increase of NAD glycohydrolase activity in uterine cervix cancers is caused by infiltration of lymphocytes.
Whooping Cough
Abscisic acid is an endogenous cytokine in human granulocytes with cyclic ADP-ribose as second messenger.
Whooping Cough
Abscisic acid is an endogenous stimulator of insulin release from human pancreatic islets with cyclic ADP ribose as second messenger.
Whooping Cough
Recombinant human serotonin 5A receptors stably expressed in C6 glioma cells couple to multiple signal transduction pathways.
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0.851
3-acetylpyridine adenine dinucleotide
-
-
0.224
cyclic ADP-ribose
-
-
0.033
nicotinamide 1,N6-ethenoadenine dinucleotide
-
pH 7.0, 28°C
0.0016
nicotinamide guanine dinucleotide
-
-
0.026
NAD+
-
-
0.026
NAD+
-
pH 7.0, 28°C
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0.0321
5,7-dihydroxy-2-(3-hydroxy-4-methoxyphenyl)chromenium
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0218
cyanidin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0146
delphinidin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0703
fisetinidin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0063
kuromanin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0082
luteolin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.006
luteolinidin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.017
malvidin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0248
myricetin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0163
pelargonidin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0209
peonidin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0392
petunidin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0486
quercetagetin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0142
quercetagetinidin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0379
quercetin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
0.0379
robinetin
Homo sapiens
-
at 37°C in 10 mM potassium phosphate buffer, pH 7.4, containing 0.05% (w/v) emulphogene
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0.02
-
partially purified enzyme, ADPR activity
0.113
-
partially purified enzyme, cADPR activity
2.205
-
partially purified enzyme, NADase activity
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7
-
-
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38 - 50
-
inactive above 50°C
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6.4 - 6.6
isoelectric focusing
4.9
-
isoelectric focusing
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-
UniProt
brenda
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surface antigen CD38
brenda
-
brenda
-
activity is 4times higher in Burkitt's lymphoma-derived cell lines than in nonmalignant control lines
brenda
-
-
brenda
-
the enzyme is the leucocyte antigen CD38
brenda
-
-
brenda
additional information
no enzyme expression in K-562 cells
brenda
-
brenda
the enzymeis induced by retinoic acid, no activity in untreated cells
brenda
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surface antigen CD38
-
brenda
CD38 is a type II transmembrane protein
brenda
CD38 is predominately on the plasma membrane of Raji and retinoic acid-treated HL-60 cells
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
CD38 is a type II membrane protein with an extracellular C-terminal enzymatic domain with NADase/NADPase and ADPR cyclase activity and a short cytoplasmic N-terminal tail
brenda
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malfunction
ablation of the CD38 gene in mice causes multiple physiological defects, including impaired oxytocin release, that result in altered social behavior
physiological function
-
leukocyte antigen CD38 expression is an early marker of all-trans retinoic acid-stimulated differentiation in the leukemic cell line HL-60 where CD38 promotes induced myeloid maturation when overexpressed. The ability of CD38 to propel all-trans retinoic acid-induced myeloid differentiation and G1/0 arrest is unimpaired by loss of its ectoenzymeactivity
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+
physiological function
the enzyme is a signaling enzyme responsible for catalyzing the synthesis of cyclic ADP ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate, both are universal Ca2+ messenger molecules
physiological function
senescent cells do not have high expression of CD38. The senescent associated secretory phenotype factors secreted by senescent cells induce CD38 mRNA and protein expression and increase CD38-NADase activity in non-senescent cells such as endothelial cells or bone marrow derived macrophages
additional information
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
additional information
structure-function relationship anaysis, overview. Covalent intermediates are formed with the catalytic residue, Glu226
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CD38_HUMAN
300
1
34328
Swiss-Prot
other Location (Reliability: 5 )
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39000
1 * 39000, SDS-PAGE
additional information
-
native enzyme shows high molecular weight and elutes in the void volumes from a Superose 12 gel filtration column
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monomer
1 * 39000, SDS-PAGE
oligomer
-
x * 45000, SDS-PAGE
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glycoprotein
N-glycosylation sites are N100, N164, N209, and N219
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N100D
site-directed mutagenesis, N-glycoylation at the site is abolished
N164D
site-directed mutagenesis, N-glycoylation at the site is abolished
N209D
site-directed mutagenesis, N-glycoylation at the site is abolished
N219D
site-directed mutagenesis, N-glycoylation at the site is abolished
E226Q
-
the mutation cripples enzymatic activity
E226D
site-directed mutagenesis, inactive catalytic site mutant
E226D
site-directed mutagenesis, catalytic mutant
E226Q
site-directed mutagenesis, inactive catalytic site mutant
E226Q
site-directed mutagenesis, catalytic mutant
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38
-
half-life: about 1 day
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50% inactivation at 2 M urea
-
SDS, even at micromolar concentration, leads to complete inactivation of the enzyme
-
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20°C, lyophilized enzyme, 90% remaining activity after 6 months
-
4°C to -196°C, 10 mM Tris-HCl, pH 8.0, 0.1% Triton X-100, at least 1 month, stable
-
4°C, -20°C, -80°C or -196°C, pH 8.0, 0.1% Triton X-100, 10 mM Tris-HCl, stable for at least 1 month
-
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native enzyme 480fold from serum by ammonium sulfate fractionation, affinity chromatography, gel filtration, and isoelectric focusing, and again gel filtration, to homogeneity
partially from spleen microsomal membranes after solubilization with Triton X-100, chromatography methods, 133fold
-
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the soluble ecto-domain of human CD38 is expressed in Pichia pastoris
-
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enzyme induction by retinoic acid in HL-60 cells
no induction of CD38 mRNA by senescence itself. Cytokines and chemokines expressed by senescent cells induce CD38 expression in macrophages
0.001 mM ATRA induces CD38 expression
-
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80% renaturation of urea and SDS denatured enzyme by treatment with Triton X-100 in a 20:1 v/w ratio with SDS
-
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Skala, H.; Lenoir, G.M.; Pichard, A.L.; Vuillaume, M.; Dreyfus, J.C.
Elevated NAD(P) glycohydrolase activity: a possible enzymatic marker for malignancy in Burkitt's lymphoma cells
Blood
60
912-917
1982
Homo sapiens
brenda
Orsomando, G.; Polzonetti, V.; Natalini, P.
NAD(P)+-glycohydrolase from human spleen: a multicatalytic enzyme
Comp. Biochem. Physiol. B
126
89-98
2000
Homo sapiens
brenda
Berthelier, V.; Tixier, J.M.; Muller-Steffner, H.; Schuber, F.; Deterre, P.
Human CD38 is an authentic NAD(P)+ glycohydrolase
Biochem. J.
330
1383-1390
1998
Homo sapiens
-
brenda
Kellenberger, E.; Kuhn, I.; Schuber, F.; Muller-Steffner, H.
Flavonoids as inhibitors of human CD38
Bioorg. Med. Chem. Lett.
21
3939-3942
2011
Homo sapiens
brenda
Congleton, J.; Jiang, H.; Malavasi, F.; Lin, H.; Yen, A.
ATRA-induced HL-60 myeloid leukemia cell differentiation depends on the CD38 cytosolic tail needed for membrane localization, but CD38 enzymatic activity is unnecessary
Exp. Cell Res.
317
910-919
2011
Homo sapiens
brenda
Jiang, H.; Sherwood, R.; Zhang, S.; Zhu, X.; Liu, Q.; Graeff, R.; Kriksunov, I.A.; Lee, H.C.; Hao, Q.; Lin, H.
Identification of ADP-ribosylation sites of CD38 mutants by precursor ion scanning mass spectrometry
Anal. Biochem.
433
218-226
2013
Homo sapiens (P28907)
brenda
Kwong, A.; Chen, Z.; Zhang, H.; Leung, F.; Lam, C.; Ting, K.; Zhang, L.; Hao, Q.; Zhang, L.; Lee, H.
Catalysis-based inhibitors of the calcium signaling function of CD38
Biochemistry
51
555-564
2012
Homo sapiens (P28907), Mus musculus (P56528), Rattus norvegicus
brenda
Shrimp, J.H.; Hu, J.; Dong, M.; Wang, B.S.; MacDonald, R.; Jiang, H.; Hao, Q.; Yen, A.; Lin, H.
Revealing CD38 cellular localization using a cell permeable, mechanism-based fluorescent small-molecule probe
J. Am. Chem. Soc.
136
5656-5663
2014
Homo sapiens (P28907)
brenda
Coskun, O.; Nurten, R.
Purification of NAD+ glycohydrolase from human serum
Oncol. Lett.
6
227-231
2013
Homo sapiens (P28907)
brenda
Chini, C.; Hogan, K.A.; Warner, G.M.; Tarrago, M.G.; Peclat, T.R.; Tchkonia, T.; Kirkland, J.L.; Chini, E.
The NADase CD38 is induced by factors secreted from senescent cells providing a potential link between senescence and age-related cellular NAD+ decline
Biochem. Biophys. Res. Commun.
513
486-493
2019
Homo sapiens (P28907)
brenda
Transporter Classification Database (TCDB):
8.A.23.1.11