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Literature summary extracted from

  • Bocquier, A.; Liu, L.; Cann, I.; Komori, K.; Kohda, D.; Ishino, Y.
    Archaeal primase Bridging the gap between RNA and DNA polymerases (2001), Curr. Biol., 11, 452-456 .
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.102 Mg2+ little activity in presence of Mg2+ Pyrococcus furiosus
2.7.7.102 Mn2+ 5 mM, required Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.102 Pyrococcus furiosus Q9P9H1 small subunit PriS
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.102 M13mp18 ssDNA + n dNTP
-
 Pyrococcus furiosus M13mp18 ss DNA/pppdN(pdN)n-1 + (n-1) diphosphate
-
 ?
2.7.7.102 additional information enzyme is specific for dNTPs Pyrococcus furiosus ?
-
 ?
2.7.7.102 poly(dT)220 + n ATP
-
 Pyrococcus furiosus poly(dT)220/pppdA(pdA)n-1 + (n-1) diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.102 ? x * 40772, calculated from sequecne Pyrococcus furiosus

Synonyms

EC Number Synonyms Comment Organism
2.7.7.102 PriS
-
 Pyrococcus furiosus

General Information

EC Number General Information Comment Organism
2.7.7.102 physiological function does not catalyze by itself the synthesis of short RNA primers but preferentially utilizes deoxynucleotides to synthesize DNA fragments up to several kilobases in length. PriS does not require primers for the synthesis of long DNA strands. PriS interacts with replication protein A Pyrococcus furiosus