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Information on EC 2.4.99.20 - 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase and Organism(s) Rattus norvegicus and UniProt Accession Q64244

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IUBMB Comments
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 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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Rattus norvegicus
UNIPROT: Q64244
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The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
adp-ribosyl cyclase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diphosphopyridine nucleosidase
ambiguous
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NADP+ + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide
show the reaction diagram
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+ = 2'-phospho-cyclic ADP-ribose + nicotinamide
show the reaction diagram
reaction 1a
2'-phospho-cyclic ADP-ribose + nicotinate = nicotinate-adenine dinucleotide phosphate
show the reaction diagram
reaction 1 b
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
NADP+:nicotinate ADP-ribosyltransferase
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 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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-phospho-cyclic ADP-ribose + nicotinate
nicotinate-adenine dinucleotide phosphate
show the reaction diagram
-
-
-
?
NADP+ + nicotinate
nicotinate-adenine dinucleotide phosphate + nicotinamide
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NADP+ + nicotinate
nicotinate-adenine dinucleotide phosphate + nicotinamide
show the reaction diagram
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
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
very low activity in kidney cortex and skeletal muscles
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CD38_RAT
303
1
34436
Swiss-Prot
other Location (Reliability: 4)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team