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Literature summary for 3.6.1.53 extracted from

  • 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 (2009), FEBS Lett., 583, 1593-1598.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.17
-
cyclic ADP-ribose pH 8.5, 25°C Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required Rattus norvegicus
Mn2+ dependent on Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP-ribose + H2O Rattus norvegicus best substrate AMP + D-ribose 5-phosphate
-
?
cyclic ADP-ribose + H2O Rattus norvegicus cADPR is an ADPRibase-Mn ligand and substrate N1-(5-phosphoribosyl)-AMP
-
?
additional information Rattus norvegicus 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 ?
-
?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP-ribose + H2O best substrate Rattus norvegicus AMP + D-ribose 5-phosphate
-
?
cyclic ADP-ribose + H2O cADPR is an ADPRibase-Mn ligand and substrate Rattus norvegicus N1-(5-phosphoribosyl)-AMP
-
?
cyclic ADP-ribose + H2O ADPRibase-Mn activity on cyclic ADP-ribose is 65fold less efficient than on ADP-ribose Rattus norvegicus N1-(5-phosphoribosyl)-AMP
-
?
cyclic ADP-ribose + H2O 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 Rattus norvegicus N1-(5-phosphoribosyl)-AMP
-
?
additional information 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 Rattus norvegicus ?
-
?

Synonyms

Synonyms Comment Organism
ADPRibase-Mn
-
Rattus norvegicus
Mn(2+)-dependent ADP-ribose/CDP-alcohol pyrophosphatase
-
Rattus norvegicus
Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase
-
Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.87
-
cyclic ADP-ribose pH 8.5, 25°C Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8.5 assay at Rattus norvegicus