2.4.99.20: 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase
This is an abbreviated version!
For detailed information about 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase, go to the full flat file.
Reaction
Synonyms
2'-phospho-cyclic-ADP-ribose transferase, ADP-ribosyl cyclase 1, ADPRC 1, BST1, CD38, diphosphopyridine nucleosidase
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Substrates Products
Substrates Products on EC 2.4.99.20 - 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase
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REACTION DIAGRAM
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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2'-phospho-cyclic ADP-ribose + nicotinamide
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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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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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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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