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Literature summary for 2.7.7.B16 extracted from

  • Le Breton, M.; Henneke, G.; Norais, C.; Flament, D.; Myllykallio, H.; Querellou, J.; Raffin, J.P.
    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 Pyrococcus abyssi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic parameters for the DNA primase under different metal ion conditions Pyrococcus abyssi

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ optimal concentration: 10 mM. Activity is dependent on the presence of Mg2+ and Mn2+. Increased MgCl2 concentrations only slightly enhance NTP incorporation, in contrast to MnCl2 Pyrococcus abyssi
Mn2+ optimal concentration: 5 mM. Activity is dependent on the presence of Mg2+ and Mn2+. Increased MgCl2 concentrations only slightly enhance NTP incorporation, in contrast to MnCl2 Pyrococcus abyssi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41000
-
1 * 41000 + 1 * 46000, calculated from sequence Pyrococcus abyssi
46000
-
1 * 41000 + 1 * 46000, calculated from sequence Pyrococcus abyssi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NTP + n NTP Pyrococcus abyssi the multifunctional archaeal primase is involved in priming and repair N(pN)n + n diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Pyrococcus abyssi Q9V292 and Q9V291 Q9V292: small subunit, Q9V291: large subunit
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus abyssi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dNTP + n NTP DNA primase has comparable affinities for ribonucleotides and deoxyribonucleotides. The Pabp41 subunit alone has no RNA synthesis activity but could synthesize long (up to 3 kb) DNA strands. Addition of the Pabp46 subunit increases the rate of DNA synthesis but decreases the length of the DNA fragments synthesized and confers RNA synthesis capability. DNA primase also displayed DNA polymerase, gapfilling, and strand-displacement activities Pyrococcus abyssi (dNTP)n+1 + n diphosphate
-
?
NTP + n NTP the multifunctional archaeal primase is involved in priming and repair Pyrococcus abyssi N(pN)n + n diphosphate
-
?
NTP + n NTP DNA primase has comparable affinities for ribonucleotides and deoxyribonucleotides. The Pabp41 subunit alone has no RNA synthesis activity but could synthesize long (up to 3 kb) DNA strands. Addition of the Pabp46 subunit increases the rate of DNA synthesis but decreases the length of the DNA fragments synthesized and confers RNA synthesis capability. DNA primase also displayed DNA polymerase, gapfilling, and strand-displacement activities Pyrococcus abyssi N(pN)n + n diphosphate
-
?

Subunits

Subunits Comment Organism
heterodimer 1 * 41000 + 1 * 46000, calculated from sequence Pyrococcus abyssi

Synonyms

Synonyms Comment Organism
Pabp41
-
Pyrococcus abyssi
Pabp46
-
Pyrococcus abyssi

General Information

General Information Comment Organism
physiological function the heterodimeric primase complex is necessary for archaeal survival Pyrococcus abyssi