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Literature summary for 2.7.7.B16 extracted from
- Molecular modeling and functional characterization of the monomeric primase-polymerase domain from the Sulfolobus solfataricus plasmid pIT3 (2008), FEBS J., 275, 4389-4402.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| purified following overexpression in Escherichia coli | Saccharolobus solfataricus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | the enzyme is strictly dependent on divalent cations, activating metal preferably used by Rep245 for its DNA polymerase activity is Mg2+ at concentrations between 5 and 10 mM | Saccharolobus solfataricus |  |
| Mn2+ | the enzyme is strictly dependent on divalent cations, with Mn2+ as a cofactor, the DNA polymerase activity of Rep245 is optimal at 12.5 mM and decreases noticeably at increasing amounts of Mn2+ | Saccharolobus solfataricus | |
| additional information | Rep245 polymerase activity is strictly dependent on divalent cations (Mg2+ or Mn2+), Zn2+ cations do not support the DNA polymerization activity of Rep245 | Saccharolobus solfataricus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 29000 | - |
x * 29000, Rep245 domain containing the N-terminal domain of the pIT3 replication protein encompassing residues 31245, SDS-PAGE | Saccharolobus solfataricus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| NTP + n NTP | Saccharolobus solfataricus | - |
N(pN)n + n diphosphate | - |
? | |
| NTP + n NTP | Saccharolobus solfataricus P2 | - |
N(pN)n + n diphosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | Q9UWW1 and Q97Z83 | Q9UWW1: large subunit, Q97Z83: small subunit | - |
| Saccharolobus solfataricus P2 | Q9UWW1 and Q97Z83 | Q9UWW1: large subunit, Q97Z83: small subunit | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purified following overexpression in Escherichia coli | Saccharolobus solfataricus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| NTP + n NTP | - |
Saccharolobus solfataricus | N(pN)n + n diphosphate | - |
? | |
| NTP + n NTP | de novo synthesis of larger molecular size RNA products when incubated with M13 mp18 single-stranded DNA in the presence of a ribonucleotide mixture. The Rep245 domain is capable of utilizing both ribonucleotides and deoxyribonucleotides for de novo primer synthesis and it synthesizes DNA products up to several kb in length in a template-dependent manner. The Rep245 primase-polymerase domain harbors also a terminal nucleotidyl transferase activity, being able to elongate the 3'-end of synthetic oligonucleotides in a non-templated manner. The Rep245 domain contains the catalytic residues required for both primase and polymerase activities | Saccharolobus solfataricus | N(pN)n + n diphosphate | - |
? | |
| NTP + n NTP | - |
Saccharolobus solfataricus P2 | N(pN)n + n diphosphate | - |
? | |
| NTP + n NTP | de novo synthesis of larger molecular size RNA products when incubated with M13 mp18 single-stranded DNA in the presence of a ribonucleotide mixture. The Rep245 domain is capable of utilizing both ribonucleotides and deoxyribonucleotides for de novo primer synthesis and it synthesizes DNA products up to several kb in length in a template-dependent manner. The Rep245 primase-polymerase domain harbors also a terminal nucleotidyl transferase activity, being able to elongate the 3'-end of synthetic oligonucleotides in a non-templated manner. The Rep245 domain contains the catalytic residues required for both primase and polymerase activities | Saccharolobus solfataricus P2 | N(pN)n + n diphosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 29000, Rep245 domain containing the N-terminal domain of the pIT3 replication protein encompassing residues 31245, SDS-PAGE | Saccharolobus solfataricus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| pIT3 replication protein | the Rep245 protein is the N-terminal domain of the pIT3 replication protein encompassing residues 31245 | Saccharolobus solfataricus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 65 | - |
- |
Saccharolobus solfataricus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | 75 | 45°C: about 40% of maximal activity, 75°C: about 40% of maximal activity | Saccharolobus solfataricus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
15 min, 40% loss of activity | Saccharolobus solfataricus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
maximal DNA template elongation at pH 8.0 | Saccharolobus solfataricus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 8.5 | pH 7.0: about 40% of maximal activity, pH 8.5: about 50% of maximal activity | Saccharolobus solfataricus |
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