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Literature summary extracted from
- Specific cyclic ADP-ribose phosphohydrolase obtained by mutagenic engineering of Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase (2018), Sci. Rep., 8, 1036 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.6.1.13 | gene ADPRM, cloned from liver, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 | Homo sapiens |
| 3.6.1.53 | gene ADPRM, cloned from liver, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.6.1.13 | F37A/L196F/C253A | site-directed mutagenesis, specific cyclic ADP-ribose phosphohydrolase obtained by mutagenic engineering of Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase. Mutagenesis of human ADPRibase-Mn at Phe37, Leu196 and Cys253 alters its specificity, the best substrate of the mutant is cyclic ADP-ribose (cADPR), the Cys253 mutation is essential for cADPR preference. The proximity to the northern ribose of cADPR in docking models indicates Cys253 is a steric constraint for cADPR positioning | Homo sapiens |
| 3.6.1.13 | F37A/L196F/C253G | site-directed mutagenesis, the mutant with a smaller residue 253 shows increased cADPR specificity | Homo sapiens |
| 3.6.1.13 | F37A/L196F/D250A/C253G | site-directed mutagenesis, the quadruple mutant shows a detrimental effect of the D250A substitution on the efficiency with all substrates (1.3-3.4fold decrease), and more markedly so for cADPR, such that the substrate efficiency ratios are less favourable than for the triple mutant F37A/L196F/C253G | Homo sapiens |
| 3.6.1.13 | F37A/L196F/V252A/C253G | site-directed mutagenesis, the mutant with displays the desired specificity, with cADPR kcat/KM is about 20-200fold larger than for any other substrate. The quadruple mutant shows detrimental effects of the V252A substitution on the efficiency with ADP-ribose, CDP-choline and 2',3'-cAMP (1.1-2.8fold decrease) while it increases 2fold the efficiency with cADPR | Homo sapiens |
| 3.6.1.13 | F37A/L196F/V252A/C253G/T279A | site-directed mutagenesis | Homo sapiens |
| 3.6.1.13 | additional information | design of mutations at or near residue 253 of human ADPRibase-Mn, in the vicinity of the adenine N1-linked (northern) ribose of cADPR, for altering the substrate specificity of the enzyme, overview | Homo sapiens |
| 3.6.1.53 | F37A/L196F/C253A | site-directed mutagenesis, specific cyclic ADP-ribose phosphohydrolase obtained by mutagenic engineering of Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase. Mutagenesis of human ADPRibase-Mn at Phe37, Leu196 and Cys253 alters its specificity, the best substrate of the mutant is cyclic ADP-ribose (cADPR), the Cys253 mutation is essential for cADPR preference. The proximity to the northern ribose of cADPR in docking models indicates Cys253 is a steric constraint for cADPR positioning | Homo sapiens |
| 3.6.1.53 | F37A/L196F/C253G | site-directed mutagenesis, the mutant with a smaller residue 253 shows increased cADPR specificity | Homo sapiens |
| 3.6.1.53 | F37A/L196F/D250A/C253G | site-directed mutagenesis, the quadruple mutant shows a detrimental effect of the D250A substitution on the efficiency with all substrates (1.3-3.4fold decrease), and more markedly so for cADPR, such that the substrate efficiency ratios are less favourable than for the triple mutant F37A/ L196F/C253G | Homo sapiens |
| 3.6.1.53 | F37A/L196F/V252A/C253G | site-directed mutagenesis, the mutant with displays the desired specificity, with cADPR kcat/KM is about 20-200fold larger than for any other substrate | Homo sapiens |
| 3.6.1.53 | F37A/L196F/V252A/C253G | site-directed mutagenesis, the quadruple mutant shows detrimental effects of the V252A substitution on the efficiency with ADP-ribose, CDP-choline and 2',3'-cAMP (1.1-2.8fold decrease) while it increases 2fold the efficiency with cADPR. F37A/L196F/V252A/C253G-ADPRibase-Mn displays substrate efficiency ratios highly | Homo sapiens |
| 3.6.1.53 | F37A/L196F/V252A/C253G/T279A | site-directed mutagenesis | Homo sapiens |
| 3.6.1.53 | additional information | design of mutations at or near residue 253 of human ADPRibase-Mn, in the vicinity of the adenine N1-linked (northern) ribose of cADPR, for altering the substrate specificity of the enzyme, overview | Homo sapiens |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.1.13 | Mn2+ | dependent on, dinuclear metal centre | Homo sapiens |  |
| 3.6.1.53 | Mn2+ | dependent on, dinuclear metal centre | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.1.13 | ADP-D-ribose + H2O | Homo sapiens | - |
AMP + D-ribose 5-phosphate | - |
? | |
| 3.6.1.13 | CDP-choline + H2O | Homo sapiens | reaction of EC 3.6.1.53 | CMP + phosphocholine | - |
? | |
| 3.6.1.13 | cyclic ADP-ribose + H2O | Homo sapiens | - |
N1-(5-phosphoribosyl)-AMP | - |
? | |
| 3.6.1.13 | additional information | Homo sapiens | ADP-ribose/CDP-alcohol diphosphatase (ADPRibase-Mn) acts as cyclic ADP-ribose (cADPR) phosphohydrolase with much lower efficiency than on its major substrates | ? | - |
- |
|
| 3.6.1.13 | NADP+ + H2O | Homo sapiens | - |
nicotinic acid mononucleotide + phosphate | - |
? | |
| 3.6.1.53 | ADP-D-ribose + H2O | Homo sapiens | - |
AMP + D-ribose 5-phosphate | - |
? | |
| 3.6.1.53 | CDP-choline + H2O | Homo sapiens | - |
CMP + phosphocholine | - |
? | |
| 3.6.1.53 | cyclic ADP-ribose + H2O | Homo sapiens | - |
N1-(5-phosphoribosyl)-AMP | - |
? | |
| 3.6.1.53 | additional information | Homo sapiens | ADP-ribose/CDP-alcohol diphosphatase (ADPRibase-Mn) acts as cyclic ADP-ribose (cADPR) phosphohydrolase with much lower efficiency than on its major substrates | ? | - |
- |
|
| 3.6.1.53 | NADP+ + H2O | Homo sapiens | - |
nicotinic acid mononucleotide + phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.6.1.13 | Homo sapiens | Q3LIE5 | - |
- |
| 3.6.1.53 | Homo sapiens | Q3LIE5 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.6.1.13 | recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by glutathione affinity chromatography, proteolytic tag cleavage | Homo sapiens |
| 3.6.1.53 | recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by glutathione affinity chromatography, proteolytic tag cleavage | Homo sapiens |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.6.1.13 | liver | - |
Homo sapiens | - |
| 3.6.1.53 | liver | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.1.13 | ADP-D-ribose + H2O | - |
Homo sapiens | AMP + D-ribose 5-phosphate | - |
? | |
| 3.6.1.13 | CDP-choline + H2O | reaction of EC 3.6.1.53 | Homo sapiens | CMP + phosphocholine | - |
? | |
| 3.6.1.13 | cyclic ADP-ribose + H2O | - |
Homo sapiens | N1-(5-phosphoribosyl)-AMP | - |
? | |
| 3.6.1.13 | additional information | ADP-ribose/CDP-alcohol diphosphatase (ADPRibase-Mn) acts as cyclic ADP-ribose (cADPR) phosphohydrolase with much lower efficiency than on its major substrates | Homo sapiens | ? | - |
- |
|
| 3.6.1.13 | NADP+ + H2O | - |
Homo sapiens | nicotinic acid mononucleotide + phosphate | - |
? | |
| 3.6.1.53 | ADP-D-ribose + H2O | - |
Homo sapiens | AMP + D-ribose 5-phosphate | - |
? | |
| 3.6.1.53 | CDP-choline + H2O | - |
Homo sapiens | CMP + phosphocholine | - |
? | |
| 3.6.1.53 | cyclic ADP-ribose + H2O | - |
Homo sapiens | N1-(5-phosphoribosyl)-AMP | - |
? | |
| 3.6.1.53 | additional information | ADP-ribose/CDP-alcohol diphosphatase (ADPRibase-Mn) acts as cyclic ADP-ribose (cADPR) phosphohydrolase with much lower efficiency than on its major substrates | Homo sapiens | ? | - |
- |
|
| 3.6.1.53 | NADP+ + H2O | - |
Homo sapiens | nicotinic acid mononucleotide + phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.6.1.13 | ? | x * 40500, recombinant enzyme, SDS-PAGE | Homo sapiens |
| 3.6.1.53 | ? | x * 40500, recombinant enzyme, SDS-PAGE | Homo sapiens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.6.1.13 | ADP-ribose/CDP-alcohol diphosphatase | - |
Homo sapiens |
| 3.6.1.13 | ADPRibase-Mn | - |
Homo sapiens |
| 3.6.1.13 | cADPR phosphohydrolase | - |
Homo sapiens |
| 3.6.1.13 | cyclic ADPR phosphohydrolase | - |
Homo sapiens |
| 3.6.1.13 | More | see also for EC 3.6.1.53 | Homo sapiens |
| 3.6.1.53 | ADP-ribose/CDP-alcohol diphosphatase | - |
Homo sapiens |
| 3.6.1.53 | ADPRibase-Mn | - |
Homo sapiens |
| 3.6.1.53 | cADPR phosphohydrolase | - |
Homo sapiens |
| 3.6.1.53 | More | see also for EC 3.6.1.13 | Homo sapiens |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.13 | 37 | - |
assay at | Homo sapiens |
| 3.6.1.53 | 37 | - |
assay at | Homo sapiens |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.13 | 7.5 | - |
assay at | Homo sapiens |
| 3.6.1.53 | 7.5 | - |
assay at | Homo sapiens |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.6.1.13 | evolution | ADPRibase-Mn enzymes contain the dinuclear metal centre typical of the metallo-dependent phosphatases SCOP2 superfamily, forming within it a family of their own named as ADPRibase-Mn-like. ADPRibase-Mn proteins constitute also a functional family in the CATH classification, within cluster SC:3 of superfamily 3.60.21.10 | Homo sapiens |
| 3.6.1.13 | physiological function | cyclic ADP-ribose (cADPR) is a messenger for Ca2+ mobilization. Its turnover is believed to occur by glycohydrolysis to ADP-ribose. ADP-ribose/CDP-alcohol diphosphatase (ADPRibase-Mn) acts as cADPR phosphohydrolase with much lower efficiency than on its major substrates | Homo sapiens |
| 3.6.1.53 | evolution | ADPRibase-Mn enzymes contain the dinuclear metal centre typical of the metallo-dependent phosphatases SCOP2 superfamily, forming within it a family of their own named as ADPRibase-Mn-like. ADPRibase-Mn proteins constitute also a functional family in the CATH classification, within cluster SC:3 of superfamily 3.60.21.10 | Homo sapiens |
| 3.6.1.53 | physiological function | cyclic ADP-ribose (cADPR) is a messenger for Ca2+ mobilization. Its turnover is believed to occur by glycohydrolysis to ADP-ribose. ADP-ribose/CDP-alcohol diphosphatase (ADPRibase-Mn) acts as cADPR phosphohydrolase with much lower efficiency than on its major substrates | Homo sapiens |
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