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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.17 | - |
cyclic ADP-ribose | pH 8.5, 25°C | Rattus norvegicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | required | Rattus norvegicus | |
Mn2+ | dependent on | Rattus norvegicus |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Rattus norvegicus |
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 | 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 Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Rattus norvegicus |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | 8.5 | assay at | Rattus norvegicus |