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Information on EC 3.6.1.53 - Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase and Organism(s) Rattus norvegicus and UniProt Accession Q5M886
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3.6.1.53 Mn2+-dependent ADP-ribose/CDP-alcohol diphosphataseIUBMB Comments
Requires Mn2+. Unlike EC 3.6.1.13, ADP-ribose diphosphatase, it cannot utilize Mg2+. ADP-D-ribose, CDP-choline, CDP-ethanolamine and ADP are substrates for this enzyme but ADP-D-glucose, UDP-D-glucose, CDP-D-glucose, CDP, CMP and AMP are not hydrolysed . The mammalian enzyme hydrolyses cyclic ADP-ribose to 1-(5-phospho-beta-D-ribosyl)-AMP with ~100-fold lower efficiency than ADP-D-ribose . In rat, the enzyme is found predominantly in thymus and spleen.
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Word Map
- 3.6.1.53
- dithiothreitol
-
adp-ribosylation
-
nonenzymatic
-
phosphohydrolysis
-
cadpr
-
napqi
- pyrophosphatases
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cdp-alcohols
- n-acetyl-p-benzoquinoneimine
- nitroprusside
-
hepatotoxicity
- acetaminophen
- rodent
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
adpribase-i, adpribase-ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADPRibase-Mn
Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase
ADPRibase-Mn
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-
-
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Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase
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-
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SYSTEMATIC NAME
IUBMB Comments
CDP-choline phosphohydrolase
Requires Mn2+. Unlike EC 3.6.1.13, ADP-ribose diphosphatase, it cannot utilize Mg2+. ADP-D-ribose, CDP-choline, CDP-ethanolamine and ADP are substrates for this enzyme but ADP-D-glucose, UDP-D-glucose, CDP-D-glucose, CDP, CMP and AMP are not hydrolysed [2]. The mammalian enzyme hydrolyses cyclic ADP-ribose to 1-(5-phospho-beta-D-ribosyl)-AMP with ~100-fold lower efficiency than ADP-D-ribose [3]. In rat, the enzyme is found predominantly in thymus and spleen.
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
ADP + H2O
?
27% activity at 0.5 mM substrate compared to ADP-ribose
-
-
?
CDP-ethanolamine + H2O
?
89% activity at 0.5 mM substrate compared to ADP-ribose
-
-
?
CDP-ethanolamine + H2O
CMP + phosphoethanolamine
84% of the activity with ADP-ribose
-
-
?
CDP-glycerol + H2O
?
89% activity at 0.5 mM substrate compared to ADP-ribose
-
-
?
CDP-glycerol + H2O
CMP + phosphoglycerol
103% of the activity with ADP-ribose
-
-
?
adenosine 5'-diphospho-5'-adenosine + H2O
AMP
-
-
45% of the activity with ADP-ribose
-
?
CDP-choline + H2O
CMP + phosphocholine
-
140% of the activity with ADP-ribose
-
-
?
CDP-ethanolamine + H2O
CMP + phosphoethanolamine
-
89% of the activity with ADP-ribose
-
-
?
CDP-glycerol + H2O
CMP + phosphoglycerol
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89% of the activity with ADP-ribose
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-
?
IDP-ribose + H2O
IMP + D-ribose 5-phosphate
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-
105% of the activity with ADP-ribose
-
?
ADP-ribose + H2O
AMP + D-ribose 5-phosphate
100% activity at 0.5 mM substrate
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-
?
CDP-choline + H2O
CMP + phosphocholine
156% of the activity with ADP-ribose
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-
?
CDP-choline + H2O
CMP + phosphocholine
140% activity at 0.5 mM substrate compared to ADP-ribose
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-
?
cyclic ADP-ribose + H2O
N1-(5-phosphoribosyl)-AMP
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cADPR is an ADPRibase-Mn ligand and substrate
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-
?
cyclic ADP-ribose + H2O
N1-(5-phosphoribosyl)-AMP
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ADPRibase-Mn activity on cyclic ADP-ribose is 65fold less efficient than on ADP-ribose
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-
?
cyclic ADP-ribose + H2O
N1-(5-phosphoribosyl)-AMP
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product determination and analysis, cADPR is an ADPRibase-Mn ligand and substrate. ADPRibase-Mn activity on cADPR is 65fold less efficient than on ADP-ribose, the best substrate. Phosphohydrolytic pattern of the reaction, overview
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-
?
additional information
?
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ADP-glucose, UDP-glucose, CDP-glucose, CDP, CMP, and AMP are not hydrolysed
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-
?
additional information
?
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ADPRibase-Mn hydrolyzes the phosphoanhydride linkages of ADP-ribose, CDP-choline, CDP-glycerol, CDP-ethanolamine, and ADP with decreasing efficiencies, requiring low micromolar Mn2+ concentrations not substituted by Mg2+. ADPRibase-Mn hydrolyzes ADP-ribose, CDP-choline, CDP-glycerol and CDP-ethanolamine with decreasing catalytic efficiencies
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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
cyclic ADP-ribose + H2O
N1-(5-phosphoribosyl)-AMP
-
cADPR is an ADPRibase-Mn ligand and substrate
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-
?
additional information
?
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-
ADPRibase-Mn hydrolyzes the phosphoanhydride linkages of ADP-ribose, CDP-choline, CDP-glycerol, CDP-ethanolamine, and ADP with decreasing efficiencies, requiring low micromolar Mn2+ concentrations not substituted by Mg2+. ADPRibase-Mn hydrolyzes ADP-ribose, CDP-choline, CDP-glycerol and CDP-ethanolamine with decreasing catalytic efficiencies
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Mn2+
additional information
Mn2+
required. Concentration of MnCl2 giving the half-maximal rate is 0.001-0.004 mM. Mn2+ cannot be replaced by Mg2+
Mn2+
dependent on, ADPRibase-Mn is inactive without added Mn2+, and it shows a high affinity for the cation, since saturation is observed at low-micromolar concentrations of Mn2+ well below the substrate concentration (0.5 mM), in no case can Mg2+ replace Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
incubation with 2.5 mM EDTA does not affect ADPRibase-Mn activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.201
ADP
recombinant enzyme, in 50 mM Tris-HCl (pH 7.5), 0.1 mM MnCl2, at 37°C
0.039
ADP-ribose
recombinant enzyme, in 50 mM Tris-HCl (pH 7.5), 0.1 mM MnCl2, at 37°C
0.3
CDP-choline
recombinant, in 50 mM Tris-HCl (pH 7.5), 0.1 mM MnCl2, at 37°C
1.422
CDP-ethanolamine
recombinant enzyme, in 50 mM Tris-HCl (pH 7.5), 0.1 mM MnCl2, at 37°C
0.304
CDP-glycerol
recombinant enzyme, in 50 mM Tris-HCl (pH 7.5), 0.1 mM MnCl2, at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.4
ADP
recombinant enzyme, in 50 mM Tris-HCl (pH 7.5), 0.1 mM MnCl2, at 37°C
12.8
ADP-ribose
recombinant enzyme, in 50 mM Tris-HCl (pH 7.5), 01 mM MnCl2, at 37°C
28.5
CDP-choline
recombinant enzyme, in 50 mM Tris-HCl (pH 7.5), 0.1 mM MnCl2, at 37°C
41.3
CDP-ethanolamine
recombinant enzyme, in 50 mM Tris-HCl (pH 7.5), 0.1 mM MnCl2, at 37°C
28.1
CDP-glycerol
recombinant enzyme, in 50 mM Tris-HCl (pH 7.5), 0.1 mM MnCl2, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
ADPRibase-Mn activity in spleen is 2.5-5fold higher than in liver and muscle
ADPRibase-Mn activity in thymus is 2.5-5fold higher than in liver and muscle
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ADPRM_RAT
337
0
38712
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
1 * 39360, calculated, 1 * 40000, SDS-PAGE, enzyme plus N-terminal extension GPLGSPNS left after proteolysis of recombinant fusion protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
1 * 39360, calculated, 1 * 40000, SDS-PAGE, enzyme plus N-terminal extension GPLGSPNS left after proteolysis of recombinant fusion protein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling based on crystal structure of the Danio rerio protein, Protein Data Base entry 2NXF, and docking of ADP-ribose
coordinates of rat ADPRibase-Mn, modelled by homology to the X-ray structure of its zebrafish orthologue, taken from the SWISS-MODEL repository, accession code q5m88. cADPR docking to a model of ADPRibase-Mn and molecular dynamics simulation, ADPRibase-Mn complexes with docked ligands show the active center in a closed conformation, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
the activities towards ADP and CDP-alcohols are highest at pH 6-8 and decrease abruptly at higher pH
690823
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Canales, J.; Pinto, R.M.; Costas, M.J.; Hernandez, M.T.; Miro, A.; Bernet, D.; Fernandez, A.; Cameselle, J.C.
Rat liver nucleoside diphosphosugar or diphosphoalcohol pyrophosphatase different from nucleotide pyrophosphatase or phosphodiesterase I: substrate specificities of Mg2+- and/or Mn2+-depeneent hydrolases acting on ADP-ribose
Biochim. Biophys. Acta
1246
167-177
1995
Rattus norvegicus
Canales, J.; Fernandez, A.; Ribeiro, J.M.; Cabezas, A.; Rodrigues, J.R.; Cameselle, J.C.; Costas, M.J.
Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: a novel metallophosphoesterase family preferentially expressed in rodent immune cells
Biochem. J.
413
103-113
2008
Mus musculus (Q99KS6), Mus musculus, Rattus norvegicus (Q5M886)
Canales, J.; Fernandez, A.; Rodrigues, J.R.; Ferreira, R.; Ribeiro, J.M.; Cabezas, A.; Costas, M.J.; Cameselle, J.C.
Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn(2+)-dependent ADP-ribose/CDP-alcohol pyrophosphatase
FEBS Lett.
583
1593-1598
2009
Rattus norvegicus
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