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Literature summary extracted from
- ADP-ribose pyrophosphatase reaction in crystalline state conducted by consecutive binding of two manganese (II) ions as cofactors (2016), Biochemistry, 55, 1801-1812 .
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.6.1.13 | crystal structures analysis of Ndx4 in the E-state obtained at 0.91 A resolution, PDB IDs are 2YVM, 1MP2, 1G0S, and 2DSB | Thermus thermophilus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.6.1.13 | cytosol | - |
Thermus thermophilus | 5829 | - |
| 3.6.1.13 | cytosol | - |
Homo sapiens | 5829 | - |
| 3.6.1.13 | cytosol | - |
Escherichia coli | 5829 | - |
| 3.6.1.13 | cytosol | - |
Mycobacterium tuberculosis | 5829 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.1.13 | Mn2+ | the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors | Thermus thermophilus |  |
| 3.6.1.13 | Mn2+ | the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors | Homo sapiens | |
| 3.6.1.13 | Mn2+ | the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors | Escherichia coli | |
| 3.6.1.13 | Mn2+ | the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors | Mycobacterium tuberculosis | |
| 3.6.1.13 | Mn2+ | the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors. Two Mn2+ ions are inserted consecutively into the catalytic center of the ES-state and ligated by Glu86 and Glu82, which are highly conserved among the Nudix family, in the ESM- and ESMM-states | Thermus thermophilus | |
| 3.6.1.13 | additional information | the ADPR-hydrolysis reaction of ADPRase from Thermus thermophilus strain HB8 (TtADPRase) requires divalent metal cations such as Mn2+, Zn2+, or Mg2+ as cofactors | Thermus thermophilus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.6.1.13 | Escherichia coli | Q93K97 | - |
- |
| 3.6.1.13 | Homo sapiens | Q9UKK9 | - |
- |
| 3.6.1.13 | Mycobacterium tuberculosis | O33199 | - |
- |
| 3.6.1.13 | Mycobacterium tuberculosis CDC 1551 | O33199 | - |
- |
| 3.6.1.13 | Mycobacterium tuberculosis Oshkosh | O33199 | - |
- |
| 3.6.1.13 | Thermus thermophilus | - |
- |
- |
| 3.6.1.13 | Thermus thermophilus | Q84CU3 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.6.1.13 | ADP-ribose pyrophosphatase | - |
Thermus thermophilus |
| 3.6.1.13 | ADP-ribose pyrophosphatase | - |
Homo sapiens |
| 3.6.1.13 | ADP-ribose pyrophosphatase | - |
Escherichia coli |
| 3.6.1.13 | ADP-ribose pyrophosphatase | - |
Mycobacterium tuberculosis |
| 3.6.1.13 | EcADPRase | - |
Escherichia coli |
| 3.6.1.13 | MT1739 | - |
Mycobacterium tuberculosis |
| 3.6.1.13 | MtADPRase | - |
Mycobacterium tuberculosis |
| 3.6.1.13 | MutT/nudix family protein | UniProt | Mycobacterium tuberculosis |
| 3.6.1.13 | Ndx2 | - |
Thermus thermophilus |
| 3.6.1.13 | Ndx4 | - |
Thermus thermophilus |
| 3.6.1.13 | NUDT5 | - |
Homo sapiens |
| 3.6.1.13 | TtADPRase | - |
Thermus thermophilus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.6.1.13 | evolution | adenosine diphosphate ribose pyrophosphatase (ADPRase) is a member of the Nudix family | Thermus thermophilus |
| 3.6.1.13 | additional information | the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors. Amino acid sequence (with Nudix motif and substrate binding site) and structure comparisons of cytosolic ADPRases from Thermus thermophilus HB8 (Ndx4 and Ndx2), Mycobacterium tuberculosis (MtADPRase), Escherichia coli (EcADPRase), and humans (NUDT5), overview | Thermus thermophilus |
| 3.6.1.13 | additional information | the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors. Amino acid sequence (with Nudix motif and substrate binding site)and structure comparisons of cytosolic ADPRases from Thermus thermophilus HB8 (Ndx4 and Ndx2), Mycobacterium tuberculosis (MtADPRase), Escherichia coli (EcADPRase), and humans (NUDT5), overview | Homo sapiens |
| 3.6.1.13 | additional information | the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors. Amino acid sequence (with Nudix motif and substrate binding site)and structure comparisons of cytosolic ADPRases from Thermus thermophilus HB8 (Ndx4 and Ndx2), Mycobacterium tuberculosis (MtADPRase), Escherichia coli (EcADPRase), and humans (NUDT5), overview | Escherichia coli |
| 3.6.1.13 | additional information | the ADP-ribose pyrophosphatase reaction in crystalline state is conducted by consecutive binding of two Mn(II) ions as cofactors. Amino acid sequence (with Nudix motif and substrate binding site)and structure comparisons of cytosolic ADPRases from Thermus thermophilus HB8 (Ndx4 and Ndx2), Mycobacterium tuberculosis (MtADPRase), Escherichia coli (EcADPRase), and humans (NUDT5), overview | Mycobacterium tuberculosis |
| 3.6.1.13 | physiological function | TtADPRase catalyzes the metal-induced and concerted general acid-base hydrolysis of ADP ribose (ADPR) into AMP and ribose-5'-phosphate (R5P) | Thermus thermophilus |
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