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IUBMB CommentsThis multiunctional enzyme catalyses 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 Ca2+ stores and activate Ca2+ influx to regulate a wide range of physiological processes. In addition, the enzyme also catalyses EC 3.2.2.6, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
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2'-phospho-cyclic ADP-ribose + nicotinate = nicotinate-adenine dinucleotide phosphate
NADP+ + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide
NADP+ = 2'-phospho-cyclic ADP-ribose + nicotinamide
2'-phospho-cyclic ADP-ribose + nicotinate = nicotinate-adenine dinucleotide phosphate
reaction 1 b
2'-phospho-cyclic ADP-ribose + nicotinate = nicotinate-adenine dinucleotide phosphate
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NADP+ + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide
overall reaction. The multifunctional enzyme catalyses both the removal of nicotinamide from NADP+, forming 2'-phospho-cyclic ADP-ribose, and the addition of nicotinate to the cyclic product, forming nicotinic acid-adenine dinucleotide phosphate, a calcium messenger that can mobilize intracellular Ca2+ stores and activate Ca2+ influx to regulate a wide range of physiological processes
NADP+ + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide
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NADP+ = 2'-phospho-cyclic ADP-ribose + nicotinamide
reaction 1a
NADP+ = 2'-phospho-cyclic ADP-ribose + nicotinamide
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2'-phospho-cyclic ADP-ribose + nicotinate
nicotinate-adenine dinucleotide phosphate
NADP+
2'-phospho-cyclic ADP-ribose + nicotinamide
NADP+ + nicotinate
nicotinate-adenine dinucleotide phosphate + nicotinamide
NGDP+
2'-phospho-cyclic GDP-ribose + nicotinamide
additional information
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2'-phospho-cyclic ADP-ribose + nicotinate
nicotinate-adenine dinucleotide phosphate
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2'-phospho-cyclic ADP-ribose + nicotinate
nicotinate-adenine dinucleotide phosphate
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enzyme shows a higher NAADP+-producing activity at pH 5.0 than at pH 7.4. At pH 5.0 the formation of NAADP+ is even more predominant than cADPRP hydrolysis, reaction of EC 3.2.2.6
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2'-phospho-cyclic ADP-ribose + nicotinate
nicotinate-adenine dinucleotide phosphate
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enzyme shows a higher NAADP+-producing activity at pH 5.0 than at pH 7.4. At pH 5.0 the formation of NAADP+ is even more predominant than cADPRP hydrolysis, reaction of EC 3.2.2.6
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2'-phospho-cyclic ADP-ribose + nicotinate
nicotinate-adenine dinucleotide phosphate
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2'-phospho-cyclic ADP-ribose + nicotinate
nicotinate-adenine dinucleotide phosphate
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the synthesis of nicotinate-adenine dinucleotide phosphate from 2'-phospho-cyclic ADP-ribose is as efficient as the hydrolysis of the cyclic nucleotide at pH 5.0, reaction of EC 3.2.2.6, while at pH 7.4 the hydrolase activity is predominant
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2'-phospho-cyclic ADP-ribose + nicotinate
nicotinate-adenine dinucleotide phosphate
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2'-phospho-cyclic ADP-ribose + nicotinate
nicotinate-adenine dinucleotide phosphate
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2'-phospho-cyclic ADP-ribose + nicotinate
nicotinate-adenine dinucleotide phosphate
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NADP+
2'-phospho-cyclic ADP-ribose + nicotinamide
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NADP+
2'-phospho-cyclic ADP-ribose + nicotinamide
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NADP+
2'-phospho-cyclic ADP-ribose + nicotinamide
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NADP+
2'-phospho-cyclic ADP-ribose + nicotinamide
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NADP+ + nicotinate
nicotinate-adenine dinucleotide phosphate + nicotinamide
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nicotinic acid-adenine dinucleotide phosphate i.e. NAADP+
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NADP+ + nicotinate
nicotinate-adenine dinucleotide phosphate + nicotinamide
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this multiunctional enzyme catalyses both the removal of nicotinamide from NADP+, forming 2'-phospho-cyclic ADP-ribose, and the addition of nicotinate to the cyclic product, forming nicotinic acid-adenine dinucleotide phosphate, a calcium messenger that can mobilize intracellular Ca2+ stores and activate Ca2+ influx to regulate a wide range of physiological processes
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NADP+ + nicotinate
nicotinate-adenine dinucleotide phosphate + nicotinamide
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nicotinic acid-adenine dinucleotide phosphate i.e. NAADP+
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NADP+ + nicotinate
nicotinate-adenine dinucleotide phosphate + nicotinamide
this multifunctional enzyme catalyses both the removal of nicotinamide from NADP+, forming 2'-phospho-cyclic ADP-ribose, and the addition of nicotinate to the cyclic product, forming nicotinic acid-adenine dinucleotide phosphate, a calcium messenger that can mobilize intracellular Ca2+ stores and activate Ca2+ influx to regulate a wide range of physiological processes
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NGDP+
2'-phospho-cyclic GDP-ribose + nicotinamide
enzyme cyclizes nicotinamide guanine dinucleotide to produce a fluorescent product, cyclic GDP-ribose, which has a site of cyclization different from cADPR
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NGDP+
2'-phospho-cyclic GDP-ribose + nicotinamide
enzyme cyclizes nicotinamide guanine dinucleotide to produce a fluorescent product, cyclic GDP-ribose, which has a site of cyclization different from cADPR
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NGDP+
2'-phospho-cyclic GDP-ribose + nicotinamide
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additional information
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enzyme is more efficient in catalyzing the removal of the nicotinamide moiety than in the base-exchange reaction
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additional information
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enzymes cyclizes NAD to cADPR. In the presence of nicotinic acid, it catalyzes a base exchange reaction resulting in the synthesis of nicotinate-adenine dinucleotide phosphate from NADP+. The switch between these two modes of catalysis is regulated by pH
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additional information
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in the absence of nicotinic acid or at neutral pH, isoform CD38 converts NADP+ to ADP-ribose 2'-phosphate, which is the hydrolysis product of cyclic ADPribose 2'-phosphate, reaction of EC 3.2.2.6
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additional information
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enzyme is more efficient in catalyzing the removal of the nicotinamide moiety than in the base-exchange reaction
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additional information
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enzyme is more efficient in catalyzing the removal of the nicotinamide moiety than in the base-exchange reaction
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additional information
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enzymes cyclizes NAD to cADPR. In the presence of nicotinic acid, it catalyzes a base exchange reaction resulting in the synthesis of nicotinate-adenine dinucleotide phosphate from NADP+. The switch between these two modes of catalysis is regulated by pH
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additional information
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the switch of the catalysis to the exchange reaction requires acidic pH and nicotinic acid. In the absence of nicotinic acid or at neutral pH, the cyclase converts NADP+ to cyclic ADP-ribose 2'-phosphate
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additional information
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the cyclization reaction to form cADPr and cGDPr as well as the base-exchange reaction to form nicotinic acid adenine dinucleotide phosphate are strictly dependent on pH. Although the formation of cyclic GDP-ribose is optimized at pH 6, the synthesis of nicotinic acid adenine dinucleotide phosphate is most pronounced at a pH below 5. Nicotinic acid has virtually no influence on the cyclization reaction, but increases the affinity of NADP at an acidic pH and has the opposite effect at alkaline pH
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NADP+ + nicotinate
nicotinate-adenine dinucleotide phosphate + nicotinamide
NADP+ + nicotinate
nicotinate-adenine dinucleotide phosphate + nicotinamide
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this multiunctional enzyme catalyses both the removal of nicotinamide from NADP+, forming 2'-phospho-cyclic ADP-ribose, and the addition of nicotinate to the cyclic product, forming nicotinic acid-adenine dinucleotide phosphate, a calcium messenger that can mobilize intracellular Ca2+ stores and activate Ca2+ influx to regulate a wide range of physiological processes
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NADP+ + nicotinate
nicotinate-adenine dinucleotide phosphate + nicotinamide
this multifunctional enzyme catalyses both the removal of nicotinamide from NADP+, forming 2'-phospho-cyclic ADP-ribose, and the addition of nicotinate to the cyclic product, forming nicotinic acid-adenine dinucleotide phosphate, a calcium messenger that can mobilize intracellular Ca2+ stores and activate Ca2+ influx to regulate a wide range of physiological processes
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0.00027
Cu2+
Oryctolagus cuniculus
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formation of cGDPr, pH 7.4, temperature not specified in the publication
0.0054
NAD+
Oryctolagus cuniculus
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formation of cGDPr, pH 7.4, temperature not specified in the publication
0.0013
NADP+
Oryctolagus cuniculus
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formation of cGDPr, pH 7.4, temperature not specified in the publication
0.7
nicotinamide
Oryctolagus cuniculus
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cyclization reaction, pH 7.4, temperature not specified in the publication
0.0023
Zn2+
Oryctolagus cuniculus
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formation of cGDPr, pH 7.4, temperature not specified in the publication
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malfunction
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generation of CD38(-/-) knockout mice of determine the role of this enzyme
physiological function
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the enzyme is involved in synthesis of nicotinic acid-adenine dinucleotide phosphate, a calcium messenger that can mobilize intracellular Ca2+ stores and activate Ca2+ influx to regulate a wide range of physiological processes
physiological function
the enzyme is involved in synthesis of nicotinic acid-adenine dinucleotide phosphate, a calcium messenger that can mobilize intracellular Ca2+ stores and activate Ca2+ influx to regulate a wide range of physiological processes
physiological function
calcium signaling messengers nicotinate-adenine dinucleotide phosphate and 2'-phospho-cyclic ADP-ribose are not produced when lymphokine-activated killer cells prepared from CD38 knock-out mice are treated with interleukin IL-8. Application of 2'-phospho-cyclic ADP-ribose to lymphikine-activated killer cells induces nicotinate-adenine dinucleotide phosphate production, whereas nicotinate-adenine dinucleotide phosphate fails to increase intracellular 2'-phospho-cyclic ADP-ribose levels. IL-8-induced nicotinate-adenine dinucleotide phosphate production is mediated by CD38 activation through the actions of cAMP/Epac/protein kinaseA/Rap1 in lymphokine-activated killer cells and nicotinate-adenine dinucleotide phosphate plays a key role in Ca2+ signaling of IL-8-induced lymphokine-activated killer cell migration.
physiological function
gene silencing of CD38 does not inhibit NAADP synthesis in intact Jurkat T cells. In vitro, both NAADP formation by base-exchange and degradation to 2-phospho adenosine diphosphoribose are efficiently decreased. Thus in vivo CD38 appears to be a NAADP degrading rather than a NAADP forming enzyme
physiological function
gene silencing of CD38 does not inhibit NAADP synthesis in thymus or spleen obtained from CD38 knock out mice
physiological function
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L-thyroxine modifies nephrotoxicity by regulating the apoptotic pathway. Possible role of CD38/ADP-ribosyl cyclase mediated calcium mobilization
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Chini, E.N.; Chini, C.C.; Kato, I.; Takasawa, S.; Okamoto, H.
CD38 is the major enzyme responsible for synthesis of nicotinic acid-adenine dinucleotide phosphate in mammalian tissues
Biochem. J.
362
125-130
2002
Mus musculus, Rattus norvegicus (Q64244)
brenda
Lee, H.C.; Graeff, R.M.; Walseth, T.F.
ADP-ribosyl cyclase and CD38. Multi-functional enzymes in Ca+2 signaling
Adv. Exp. Med. Biol.
419
411-419
1997
Homo sapiens (P28907), Aplysia californica (P29241)
brenda
Moreschi, I.; Bruzzone, S.; Melone, L.; De Flora, A.; Zocchi, E.
NAADP+ synthesis from cADPRP and nicotinic acid by ADP-ribosyl cyclases
Biochem. Biophys. Res. Commun.
345
573-580
2006
Axinella polypoides, Homo sapiens (P28907), Aplysia californica (P29241)
brenda
Bacher, I.; Zidar, A.; Kratzel, M.; Hohenegger, M.
Channelling of substrate promiscuity of the skeletal-muscle ADP-ribosyl cyclase isoform
Biochem. J.
381
147-154
2004
Oryctolagus cuniculus
brenda
Schmid, F.; Bruhn, S.; Weber, K.; Mittruecker, H.W.; Guse, A.H.
CD38: a NAADP degrading enzyme
FEBS Lett.
585
3544-3548
2011
Homo sapiens (P28907), Mus musculus (P56528)
brenda
Aarhus, R.; Graeff, R.M.; Dickey, D.M.; Walseth, T.F.; Lee, H.C.
ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium-mobilizing metabolite from NADP+
J. Biol. Chem.
270
30327-30333
1995
Homo sapiens (P28907), Aplysia californica (P29241)
brenda
Graeff, R.; Liu, Q.; Kriksunov, I.A.; Hao, Q.; Lee, H.C.
Acidic residues at the active sites of CD38 and ADP-ribosyl cyclase determine nicotinic acid adenine dinucleotide phosphate (NAADP) synthesis and hydrolysis activities
J. Biol. Chem.
281
28951-28957
2006
Homo sapiens (P28907)
brenda
Rah, S.Y.; Mushtaq, M.; Nam, T.S.; Kim, S.H.; Kim, U.H.
Generation of cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate by CD38 for Ca2+ signaling in interleukin-8-treated lymphokine-activated killer cells
J. Biol. Chem.
285
21877-21887
2010
Mus musculus (P56528)
brenda
El-Hamoly, T.; El-Sharawy, D.; El Refaye, M.; Abd El-Rahman, S.
L-Thyroxine modifies nephrotoxicity by regulating the apoptotic pathway The possible role of CD38/ADP-ribosyl cyclase-mediated calcium mobilization
PLoS ONE
12
e0184157
2017
Mus musculus
brenda