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Literature summary for 2.7.7.102 extracted from

  • Le Breton, M.; Henneke, G.; Norais, C.; Flament, D.; Myllykallio, H.; Querellou, J.; Raffin, J.
    The heterodimeric primase from the euryarchaeon Pyrococcus abyssi a multifunctional enzyme for initiation and repair? (2007), J. Mol. Biol., 374, 1172-1185 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, independently and coexpression of subunits Pyrococcus abyssi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5
-
dNTP pH 8.0, 60°C, presence of 10 mM Mg2+ Pyrococcus abyssi
27.5
-
NTP pH 8.0, 60°C, presence of 10 mM Mg2+ Pyrococcus abyssi
60.5
-
dNTP pH 8.0, 60°C, presence of 5 mM Mg2+ Pyrococcus abyssi
198
-
dNTP pH 8.0, 60°C, presence of 5 mM Mn2+, 10 mM Mg2+ Pyrococcus abyssi

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ or Mn2+, required. Optimum concentration 5 mM Pyrococcus abyssi
Mn2+ or Mg2+, required. Optimum concentration 1 mM Pyrococcus abyssi

Organism

Organism UniProt Comment Textmining
Pyrococcus abyssi Q9V292 and Q9V291 Q9V292 i.e. small subunit PriS, Q9V291 i.e. large subunit PriL
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
M13 ssDNA + n dNTP
-
Pyrococcus abyssi M13 ssDNA/pppdN(pdN)n-1 + (n-1) diphosphate
-
?
M13 ssDNA + n NTP
-
Pyrococcus abyssi M13 ssDNA/pppN(pN)n-1 + (n-1) diphosphate
-
?

Subunits

Subunits Comment Organism
? x * 41000, subunit PrimS, plus x * 46000, subunit PrimL, claculated from sequence Pyrococcus abyssi

Synonyms

Synonyms Comment Organism
Pab2235
-
Pyrococcus abyssi
Pab2236
-
Pyrococcus abyssi

General Information

General Information Comment Organism
physiological function the small subunit PrimS alone has no RNA synthesis activity but can synthesize up to 3 kb long DNA strands. Addition of the large subunit increases the rate of DNA synthesis but decreases the length of the DNA fragments synthesized and confers RNA synthesis capability. The primase has comparable affinities for ribonucleotides and deoxyribonucleotides. DNA primase also displays DNA polymerase, gapfilling, and strand-displacement activities Pyrococcus abyssi