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Information on EC 3.2.2.6 - ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
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3.2.2.6 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolaseIUBMB 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.
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Word Map
- 3.2.2.6
-
cadpr
-
ryanodine
- aplysia
- inositol
-
ca2+-mobilizing
-
ectoenzyme
-
naadp
- gdp-ribose
-
urchin
- californica
- beta-nad+
- nadase
- diphosphoribose
-
ca2+-induced
-
ca2+-releasing
-
calcium-mobilizing
-
trisphosphate
- oxytocin
-
8-br-cadpr
-
anti-cd38
-
8-bromo-cadpr
-
cadpr-mediated
-
ryanodine-sensitive
-
cadpr-induced
-
cd38-deficient
- ngd+
- nad+-glycohydrolase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
+
=
+
+
Synonyms
ADP-ribosyl cyclase, ADPR cyclase, bCD38, CD38, CD38/NAD+ glycohydrolase, NAD(P) nucleosidase, NAD(P)+ glycohydrolase, NAD(P)+-glycohydrolase, NAD(P)-glycohydrolase, NAD(P)ase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CD38
NAD(P) nucleosidase
NAD(P)+ glycohydrolase
-
-
-
-
NAD(P)-glycohydrolase
-
-
-
-
NAD(P)ase
-
-
-
-
NADase
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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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclic ADP-ribose + H2O = ADP-D-ribose
(1b)
-
-
-
NAD+ = cyclic ADP-ribose + nicotinamide
(1a)
-
-
-
NAD+ + H2O = ADP-D-ribose + nicotinamide
also catalyses transfer of ADP-ribose(P) residues
-
NAD+ + H2O = ADP-D-ribose + nicotinamide
(overall reaction)
-
-
-
NAD+ + H2O = ADP-D-ribose + nicotinamide
structure-function analysis and reaction mechanism, overview. The nicotinamide-ribosyl bond of NAD+ is cleaved via a dissociative process with a late transition state, leading to a ribooxocarbenium ion reaction intermediate stabilized by the side-chain of invariant Glu218. This rate-determining step is followed by two nucleophilic reactions in competition: (i) an intermolecular pathway involving a rapid trapping from the b-face of this intermediate by a water molecule (NAD+ glycohydrolase activity) or by competing neutral nucleophiles such as pyridines (transglycosidation reactions) or alcohols (e.g., methanolysis), and (ii) an intramolecular reaction between N1 of the adenine ring and C19 (anomeric carbon) of the oxocarbenium ion leading to the formation of cyclic ADP-ribose (ADP-ribosyl cyclase activity). This latter reaction represents a kinetically minor step relative to solvolysis
NAD+ + H2O = ADP-D-ribose + nicotinamide
substrate binding with a crucial role of Glu218, which orients the substrate for cleavage by interacting with the N-ribosyl 2'-OH group of NAD+, stepwise ordered uni-bi kinetic mechanism, overview. Residues Trp118, Glu138, Asp147, Trp181 stabilize the ribooxocarbenium ion-like transition state mostly by electrostatic interactions
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
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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CAS REGISTRY NUMBER
COMMENTARY
9025-46-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-acetylpyridine + adenosine diphosphoribose
3-acetylpyridine adenine dinucleotide + phosphate
-
transglycosylation activity, very poor hydrolytic activity with this substrate
-
-
?
cyclic ADP-ribose + H2O
adenosine diphosphoribose + ?
-
i.e. ADPR activity
-
-
?
NAD+ + H2O
cyclic ADP-ribose + nicotinamide + H+
-
the cyclization and hydrolysis of NAD(P)+ occur optimally at physiological pH
-
-
?
NADP+ + H2O
ADP-ribose-P + nicotinamide
-
80% activity compared to the activity with NAD+
-
-
?
NADP+ + nicotinic acid
nicotinic acid adenine dinucleotide phosphate
-
this reaction occurs only in acidic pH
-
-
?
nicotinamide 1,N6-ethenoadenine dinucleotide + H2O
?
-
i.e. epsilonNAD+, used for a fluorometric assay
-
-
?
3-pyridinealdehyde hypoxanthine dinucleotide + H2O
?
-
60% activity compared to the activity with NAD+
-
-
?
beta-NAD+ + H2O
?
-
beta-NAD+ and NADP+ are hydrolyzed at equal rates
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
bovine CD38/NAD+ glycohydrolase catalyzes the hydrolysis of NAD+ to nicotinamide and ADP-ribose and the formation of cyclic ADP-ribose via a stepwise reaction mechanism
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
via a stepwise reaction mechanism
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
overall reaction
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
via a stepwise reaction mechanism
-
-
?
additional information
?
-
the enzyme catalyses the hydrolysis of NAD+ into nicotinamide and ADP-ribose and the formation of cyclic ADP-ribose (cADPR)
-
-
?
additional information
?
-
-
the enzyme catalyses the hydrolysis of NAD+ into nicotinamide and ADP-ribose and the formation of cyclic ADP-ribose (cADPR)
-
-
?
additional information
?
-
selectivity in favor of methanolysis by wild-type enzyme and mutant E138A. 1'-Azido ADP-ribose is the reaction product obtained in the presence of azide. the ADP-ribosyl cyclase activity of wild-type bCD38 isminimal
-
-
?
additional information
?
-
-
selectivity in favor of methanolysis by wild-type enzyme and mutant E138A. 1'-Azido ADP-ribose is the reaction product obtained in the presence of azide. the ADP-ribosyl cyclase activity of wild-type bCD38 isminimal
-
-
?
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)
-
-
?
additional information
?
-
CD38 is a NAD+-dependent, multifunctional ectoenzyme that cannot only generate cyclic ADP-ribose from NAD+ but also hydrolyze cyclic ADP-ribose to ADP-ribose and transport cyclic ADP-ribose into cells
-
-
?
additional information
?
-
-
enzyme may be induced by presence of protein in the culture medium. Low concentrations of sucrose or glucose, 0.1%, casamino acids or some amino acids such as Met, Cys, Phe and Trp strongly repress enzyme synthesis
-
-
?
additional information
?
-
-
synthesis of nicotinate adenine dinucleotide phosphate by exchange of nicotinamide for nicotinic acid
-
-
?
additional information
?
-
frog CD38 enzyme shows NAD+ glycohydrolase, ADP-ribosyl cyclase, and cyclic ADP-ribosyl hydrolase activities
-
-
?
additional information
?
-
-
frog CD38 enzyme shows NAD+ glycohydrolase, ADP-ribosyl cyclase, and cyclic ADP-ribosyl hydrolase activities
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + H2O
ADP-D-ribose + nicotinamide
bovine CD38/NAD+ glycohydrolase catalyzes the hydrolysis of NAD+ to nicotinamide and ADP-ribose and the formation of cyclic ADP-ribose via a stepwise reaction mechanism
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
overall reaction
-
-
?
NAD+ + H2O
ADP-D-ribose + nicotinamide
via a stepwise reaction mechanism
-
-
?
additional information
?
-
the enzyme catalyses the hydrolysis of NAD+ into nicotinamide and ADP-ribose and the formation of cyclic ADP-ribose (cADPR)
-
-
?
additional information
?
-
-
the enzyme catalyses the hydrolysis of NAD+ into nicotinamide and ADP-ribose and the formation of cyclic ADP-ribose (cADPR)
-
-
?
additional information
?
-
-
enzyme is involved in the regulation of intracellular concentration of adenosine diphosphoribose
-
-
?
additional information
?
-
CD38 is a NAD+-dependent, multifunctional ectoenzyme that cannot only generate cyclic ADP-ribose from NAD+ but also hydrolyze cyclic ADP-ribose to ADP-ribose and transport cyclic ADP-ribose into cells
-
-
?
additional information
?
-
-
enzyme may be induced by presence of protein in the culture medium. Low concentrations of sucrose or glucose, 0.1%, casamino acids or some amino acids such as Met, Cys, Phe and Trp strongly repress enzyme synthesis
-
-
?
additional information
?
-
frog CD38 enzyme shows NAD+ glycohydrolase, ADP-ribosyl cyclase, and cyclic ADP-ribosyl hydrolase activities
-
-
?
additional information
?
-
-
frog CD38 enzyme shows NAD+ glycohydrolase, ADP-ribosyl cyclase, and cyclic ADP-ribosyl hydrolase activities
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ag+
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-[5-O-[(benzyloxy)(hydroxy)phosphoryl]-2-deoxy-2-fluoro-L-erythro-pentofuranosyl]-3-carbamoylpyridinium
1-[5-O-[butoxy(hydroxy)phosphoryl]-2-deoxy-2-fluoro-D-threo-pentofuranosyl]-3-carbamoylpyridinium
2'-deoxy-2'-beta-D-fluororibofuranoside NAD+
non-covalent complex of the inhibitor formed with enzyme mutant E218Q, PDB ID: 3ghh, and with wild-type enzyme, PDB ID: 3kou
3-carbamoyl-1-[2-deoxy-2-fluoro-5-O-[(hexyloxy)(hydroxy)phosphoryl]-D-threo-pentofuranosyl]pyridinium
3-carbamoyl-1-[2-deoxy-2-fluoro-5-O-[hydroxy(2-phenylethoxy)phosphoryl]-L-erythro-pentofuranosyl]pyridinium
3-carbamoyl-1-[2-deoxy-5-O-(diethoxyphosphoryl)-2-fluoro-D-threo-pentofuranosyl]pyridinium
3-carbamoyl-1-[2-deoxy-5-O-[(ethenyloxy)(propoxy)phosphoryl]-2-fluoro-D-threo-pentofuranosyl]pyridinium
Ag+
-
50% inhibition of NADase and 300% activation of adenosine diphosphate cyclase; at 2 mM 50% inhibition of NADase activity and 300% activation of cADPR activity
arabinosyl 2'-fluoro-2'-deoxy-NAD
-
suicide substrate that inhibits CD38 ectoenzyme activity
Pb2+
-
complete inhibition at 2 mM; inhibition of NADase and adenosine diphosphate cyclase
Sn2+
-
complete inhibition at 2 mM; inhibition of NADase and adenosine diphosphate cyclase
1-[2-azido-2-deoxy-5-O-phosphono-D-threo-pentofuranosyl]-3-carbamoylpyridinium
inhibition of the NADase activity
1-[2-azido-2-deoxy-5-O-phosphono-D-threo-pentofuranosyl]-3-carbamoylpyridinium
inhibition of the NADase activity
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-[(benzyloxy)(hydroxy)phosphoryl]-2-deoxy-2-fluoro-L-erythro-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
1-[5-O-[butoxy(hydroxy)phosphoryl]-2-deoxy-2-fluoro-D-threo-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-chloro-2-deoxy-5-O-phosphono-D-threo-pentofuranosyl]pyridinium
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-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-phosphono-L-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-thiophosphono-L-erythro-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-[(hexyloxy)(hydroxy)phosphoryl]-D-threo-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-5-O-[hydroxy(2-phenylethoxy)phosphoryl]-L-erythro-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-2-fluoro-D-threo-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-(diethoxyphosphoryl)-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-[2-deoxy-5-O-[(ethenyloxy)(propoxy)phosphoryl]-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
3-carbamoyl-1-[3-deoxy-3-fluoro-5-O-phosphono-L-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
arabinosyl-2'-fluoro-2'-deoxynicotinamide mononucleotide
inhibition of the NADase activity
arabinosyl-2'-fluoro-2'-deoxynicotinamide mononucleotide
-
inhibition of the NADase activity
Hg2+
-
complete inhibition at 2 mM; inhibition of NADase and adenosine diphosphate cyclase
additional information
-
not inhibited by rac-taxifolin, rac-catechin, piceatannol, and trans-resveratrol
-
additional information
-
NADase inhibitor from Pseudomonas putida KB1
-
additional information
-
high resistance to inhibition by nicotinamide
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
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.
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.
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.
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0604
NAD+-glycohydrolase activityin crude cell extract, pH 7.4, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity is 4times higher in Burkitt's lymphoma-derived cell lines than in nonmalignant control lines
brenda
additional information
the enzymeis induced by retinoic acid, no activity in untreated cells
brenda
additional information
the enzyme is ubiquitously expressed in various tissues
brenda
additional information
-
the enzyme is ubiquitously expressed in various tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
CD38 is predominately on the plasma membrane of Raji and retinoic acid-treated HL-60 cells
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
most frog enzyme (81%) is distributed in the membrane fraction (5% in mitochondrial fraction and 14% in microsomal fraction)
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the CD38-cADPR signaling system is conserved during vertebrate evolution, phylogenetic tree
malfunction
physiological function
additional information
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
malfunction
-
ablation of the CD38 gene in mice causes multiple physiological defects, including impaired oxytocin release, that result in altered social behavior
malfunction
ablation of the CD38 gene in mice causes multiple physiological defects, including impaired oxytocin release, that result in altered social behavior
malfunction
ablation of the CD38 gene in mice causes multiple physiological defects, including impaired oxytocin release, that result in altered social behavior
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
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 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
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
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
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
the enzyme is CD38-cADPR signaling system in frog cells
physiological function
in cultured macrophages, lipopolysaccharide LPS can upregulate CD38 expression in time- and dose-dependent manner. Knocking down or blockade of CD38 in macrophages inhibits LPS-induced macrophage M1 polarization accompanied by diminished NF-kappaB signaling activation. In a mouse model with LPS-induced acute kidney injury, blocking CD38 with quercetin significantly relieves kidney dysfunction, kidney pathological changes as well as inflammatory cell accumulation
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
invariant glutamate 218 identified is the catalytic residue of the enzyme, Structure homology modelling, overview
additional information
-
invariant glutamate 218 identified is the catalytic residue of the enzyme, Structure homology modelling, overview
additional information
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
additional information
-
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
additional information
-
structure-function relationship anaysis, overview. Covalent intermediates are formed with the catalytic residue, Glu226
additional information
structure-function relationship anaysis, overview. Covalent intermediates are formed with the catalytic residue, Glu226
additional information
structure-function relationship anaysis, overview. Covalent intermediates are formed with the catalytic residue, Glu226
Show AA Sequence and Transmembrane Helices (2753 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
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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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mono N-glycosylated forms of soluble enzyme ecto-domain (residues 32-278) and catalytic residue mutant Glu218Gln, in apo state or bound to 2'-fluorinated NAD+ derivatives aFNAD or rFNAD, hanging drop vapour diffusion method, from 20-30% PEG 4000, 50-250 mM ammonium sulfate and 100 mM sodium cacodylate, sodium acetate or MES, pH 6.0-6.5, room temperature, soaking of crystals in 1-3 mM ligand solution, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement
enzyme in complex with inhibitors, hanging drop vapor diffusion method, mixing of 10 mg/ml protein in 20 mM HEPES with 5 mm ligands, with reservoir solution containing 0.1 M sodium acetate, pH 4.0, 0.2 M ammonium acetate, 3% 2-propanol, and 15% PEG 10000, X-ray diffraction structure determination and analysis, molecular replacement
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D147A
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
E138A
site-directed mutagenesis, the mutation causes a modest increase in the rate of NAD+ transformation which is proportional to its concentration. At 4.0 M, the rate increase is about 1.2fold and the formation of beta-1'-O-methyl ADP-ribose amounts to about 80% of the total reaction products. The observed selectivity in favor of methanolysis is similar to that of wild-type enzyme. The ADP-ribosyl cyclase activity of E138A mutant is more affected by the competing nucleophile, i.e. formation of ADP-ribose and cADPR are reduced by 75% and 90% respectively at 4.0 M methanol, the mutant shows an increase in ADP cyclization and higly reduced overall activity compared to the wild-type enzyme
E138Q
site-directed mutagenesis, in the presence of methanol, mutant E138Q efficiently catalyzes the formation of beta-1'-O-methyl ADP-ribose. But in contrast with mutant E138A, and like the wild-type enzyme, solvolysis does not affect the overall turnover rate of NAD+ indicating that the formation of the E.ADP-ribosyl intermediate is still rate limiting
E218A
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
E218Q
K120A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R216A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S185A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W118A
site-directed mutagenesis, the mutant shows a decrease of the catalytic rate compared to the wild-type enzyme
W118A/W181A
site-directed mutagenesis, the mutant shows a decrease of the catalytic rate which is 16fold lower than the product of the effects of the two single mutations
W118F
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
W118H
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
W168A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W181A
site-directed mutagenesis, the mutant shows a decrease of the catalytic rate and a reduced sensitivity to nicotinamide inhibition compared to the wild-type enzyme
W181F
site-directed mutagenesis, the mutant shows a decrease in activity and an increase in ADP cyclization compared to the wild-type enzyme
E226D
E226Q
additional information
E218Q
site-directed mutagenesis, catalytic site mutant, crystal structure analysis, almost inactive mutant
E218Q
site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme
additional information
construction of CD38/NAD+ glycohydrolase truncated for the first 31 amino acids that encompass the transmembrane and short intracellular domains
additional information
-
construction of CD38/NAD+ glycohydrolase truncated for the first 31 amino acids that encompass the transmembrane and short intracellular domains
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
-
60% loss of activity after 30 min, 80% loss of activity after 1 h
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
SDS, even at micromolar concentration, leads to complete inactivation of the enzyme
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 480fold from serum by ammonium sulfate fractionation, affinity chromatography, gel filtration, and isoelectric focusing, and again gel filtration, to homogeneity
partial
partially from spleen microsomal membranes after solubilization with Triton X-100, chromatography methods, 133fold
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cd38, eight exons, DNA and amino acid sequence determination and analysis, sequence comparison to the human enzyme, phylogenetic tree, expression in COS-7 cells
recombinant expression of bovine CD38/NAD+ glycohydrolase truncated for the first 31 amino acids that encompass the transmembrane and short intracellular domains in Pichia pastoris. The construct comprises a DNA fragment encoding the ecto-domain in the expression plasmid pPICZaA in frame with the yeast alpha-factor secretion signal sequence under the transcriptional control of the AOX1 promoter and keeping its original stop codon
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in cultured macrophages, lipopolysaccharide LPS can upregulate CD38 expression in time- and dose-dependent manner
no induction of CD38 mRNA by senescence itself. Cytokines and chemokines expressed by senescent cells induce CD38 expression in macrophages
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamasaki, N.; Mori, I.; Takakuwa, M.
Purification and some properties of NAD(P)+ glycohydrolase from Saccharomyces cerevisiae
J. Ferment. Technol.
60
131-137
1982
Saccharomyces cerevisiae
-
brenda
Mather, I.H.; Knight, M.
A heat-stable nicotinamide-adenine dinucleotide glycohydrolase from Pseudomonas putida KB1. Partial purification and some properties of the enzyme and an inhibitory protein
Biochem. J.
129
141-152
1972
Pseudomonas putida KB1
brenda
Broeker, M.; Schindelmeiser, J.; Pape, H.
A nicotinamide adenine dinucleotide (phosphate) glycohydrolase [NAD(P)ase, EC 3.2.2.6] from Streptomyces griseus
FEMS Microbiol. Lett.
6
245-247
1979
Streptomyces griseus
-
brenda
Jorge, J.A.; Terenzi, H.F.
Carbon source regulation of nicotinamide adenine dinucleotide (phosphate) glycohydrolase in Neurospora crassa: induction and repression of enzyme synthesis
J. Gen. Microbiol.
130
1563-1568
1984
Neurospora crassa
brenda
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
Artman, M.; Frankl, G.
Nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate splitting enzyme(s) of sheep and rabbit erythrocytes: their effect on the growth of Haemophilus
Can. J. Microbiol.
28
696-702
1982
Oryctolagus cuniculus, Ovis aries
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
Chini, E.N.; Dousa, T.P.
Enzymatic synthesis and degradation of nicotinate adenine dinucleotide phosphate (NAADP), a Ca2+-releasing agonist, in rat tissues
Biochem. Biophys. Res. Commun.
209
167-174
1995
Rattus norvegicus
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
Lee, H.C.
Cyclic ADP-ribose and NAADP: fraternal twin messengers for calcium signaling
Sci. China Life Sci.
54
699-711
2011
Mus musculus
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
Rattus norvegicus, Homo sapiens (P28907), Mus musculus (P56528)
brenda
Kuhn, I.; Kellenberger, E.; Cakir-Kiefer, C.; Muller-Steffner, H.; Schuber, F.
Probing the catalytic mechanism of bovine CD38/NAD+ glycohydrolase by site directed mutagenesis of key active site residues
Biochim. Biophys. Acta
1844
1317-1331
2014
Bos taurus (Q9TTF5), Bos taurus
brenda
Ma, Y.; Cao, W.; Wang, L.; Jiang, J.; Nie, H.; Wang, B.; Wei, X.; Ying, W.
Basal CD38/cyclic ADP-ribose-dependent signaling mediates ATP release and survival of microglia by modulating connexin 43 hemichannels
Glia
62
943-955
2014
Mus musculus (P56528)
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
Ikeda, T.; Takasawa, S.; Noguchi, N.; Nata, K.; Yamauchi, A.; Takahashi, I.; Yoshikawa, T.; Sugawara, A.; Yonekura, H.; Okamoto, H.
Identification of a major enzyme for the synthesis and hydrolysis of cyclic ADP-ribose in amphibian cells and evolutional conservation of the enzyme from human to invertebrate
Mol. Cell. Biochem.
366
69-80
2012
Xenopus laevis (H7C831), Xenopus laevis
brenda
Coskun, O.; Nurten, R.
Purification of NAD+ glycohydrolase from human serum
Oncol. Lett.
6
227-231
2013
Homo sapiens (P28907)
brenda
Egea, P.F.; Muller-Steffner, H.; Kuhn, I.; Cakir-Kiefer, C.; Oppenheimer, N.J.; Stroud, R.M.; Kellenberger, E.; Schuber, F.
Insights into the mechanism of bovine CD38/NAD+ glycohydrolase from the X-ray structures of its Michaelis complex and covalently-trapped intermediates
PLoS ONE
7
e34918
2012
Bos taurus (Q9TTF5), Bos taurus
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
Shu, B.; Feng, Y.; Gui, Y.; Lu, Q.; Wei, W.; Xue, X.; Sun, X.; He, W.; Yang, J.; Dai, C.
Blockade of CD38 diminishes lipopolysaccharide-induced macrophage classical activation and acute kidney injury involving NF-kappaB signaling suppression
Cell. Signal.
42
249-258
2018
Mus musculus (P56528), Mus musculus
brenda
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