Any feedback?
Literature summary for 2.7.7.102 extracted from
- A highly divergent archaeo-eukaryotic primase from the Thermococcus nautilus plasmid, pTN2 (2014), Nucleic Acids Res., 42, 3707-3719 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermococcus nautili | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| M13mp18 ssDNA + n dNTP | - |
Thermococcus nautili | M13mp18 ssDNA/pppdN(pdN)n-1 + (n-1) diphosphate | - |
? |  |
| additional information | no substrates: NTPs | Thermococcus nautili | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PolpTN2 | - |
Thermococcus nautili |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | primase/polymerase PolpTN2 is encoded by the pTN2 plasmid and exhibits primase, polymerase and nucleotidyl transferase activities. It specifically incorporates dNTPs, to the exclusion of rNTPs. PolpTN2 can efficiently prime DNA synthesis by PolB DNA polymerase. The N-terminal PriS-like domain of PolpTN2 exhibits all activities of the full-length enzyme but is much less efficient in priming cellular DNA polymerases. The N-terminal domain possesses reverse transcriptase activity | Thermococcus nautili |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
