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Literature summary extracted from

  • Lao-Sirieix, S.H.; Bell, S.D.
    The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase and 3-terminal nucleotidyl transferase activities (2004), J. Mol. Biol., 344, 1251-1263.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.B16 expression in Escherichia coli Saccharolobus solfataricus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.B16 D101A/D103A the catalyric site mutant enzyme does not exhibit any detectable catalytic activity, even when higher concentrations of enzyme are utilised. The result demonstrate that the terminal transferase-like activity of PriSL is dependent on the catalytic activity of the primase. D101 and D103 are necessary for PriSL catalytic activity Saccharolobus solfataricus
2.7.7.B16 N175A/R176 the affinity of DNA-binding site mutant for NTPs is approximately tenfold lower than that of the wild-type primase and that its enzymatic capability is diminished. Therefore, the mutation of N175 and R176 does not alter the DNA binding properties of the primase but modifies its affinity for free NTPs Saccharolobus solfataricus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.B16 0.025
-
 NTP pH 8.0, 60°C, in presence of M13 ssDNA as template Saccharolobus solfataricus
2.7.7.B16 0.028
-
 dNTP pH 8.0, 60°C, in presence of M13 ssDNA as template Saccharolobus solfataricus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.B16 Mn2+ the enzyme requires manganese ions for catalytic activity Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.B16 NTP + n NTP Saccharolobus solfataricus
-
 N(pN)n + n diphosphate
-
 ?
2.7.7.B16 NTP + n NTP Saccharolobus solfataricus P2
-
 N(pN)n + n diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.B16 Saccharolobus solfataricus Q9UWW1 and Q97Z83 Q9UWW1: large subunit, Q97Z83: small subunit
-
2.7.7.B16 Saccharolobus solfataricus P2 Q9UWW1 and Q97Z83 Q9UWW1: large subunit, Q97Z83: small subunit
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.B16
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.B16 dNTP + n dNTP the oligonucleotides 20-mer oligo(dA), -(dC), -(dG) and -(dT) are used with varying efficiencies, with oligo(d)A being the poorest substrate and oligo(dC) the most preferred one. The enzyme is capable of utilising both ribonucleotides and deoxyribonucleotides for primer synthesis in the presence of natural, or synthetic, single-stranded DNA. It has a significantly higher affinity for ribonucleotides than for deoxyribonucleotides. In addition to the primase and polymerase activities, the enzyme possesses a template-independent 3'-terminal nucleotidyl transferase activity Saccharolobus solfataricus dN(pdN)n + n diphosphate
-
 ?
2.7.7.B16 dNTP + n dNTP the oligonucleotides 20-mer oligo(dA), -(dC), -(dG) and -(dT) are used with varying efficiencies, with oligo(d)A being the poorest substrate and oligo(dC) the most preferred one. The enzyme is capable of utilising both ribonucleotides and deoxyribonucleotides for primer synthesis in the presence of natural, or synthetic, single-stranded DNA. It has a significantly higher affinity for ribonucleotides than for deoxyribonucleotides. In addition to the primase and polymerase activities, the enzyme possesses a template-independent 3'-terminal nucleotidyl transferase activity Saccharolobus solfataricus P2 dN(pdN)n + n diphosphate
-
 ?
2.7.7.B16 NTP + n NTP
-
 Saccharolobus solfataricus N(pN)n + n diphosphate
-
 ?
2.7.7.B16 NTP + n NTP the oligonucleotides 20-mer oligo(dA), -(dC), -(dG) and -(dT) are used as template with varying efficiencies, with oligo(d)A being the poorest substrate and oligo(dC) the most preferred one. The enzyme is capable of utilising both ribonucleotides and deoxyribonucleotides for primer synthesis in the presence of natural, or synthetic, single-stranded DNA. It has a significantly higher affinity for ribonucleotides than for deoxyribonucleotides. Products with an apparent length of 14 nt and 7 nt are mainly synthesised. In addition to the primase and polymerase activities, the enzyme possesses a template-independent 3'-terminal nucleotidyl transferase activity Saccharolobus solfataricus N(pN)n + n diphosphate
-
 ?
2.7.7.B16 NTP + n NTP
-
 Saccharolobus solfataricus P2 N(pN)n + n diphosphate
-
 ?
2.7.7.B16 NTP + n NTP the oligonucleotides 20-mer oligo(dA), -(dC), -(dG) and -(dT) are used as template with varying efficiencies, with oligo(d)A being the poorest substrate and oligo(dC) the most preferred one. The enzyme is capable of utilising both ribonucleotides and deoxyribonucleotides for primer synthesis in the presence of natural, or synthetic, single-stranded DNA. It has a significantly higher affinity for ribonucleotides than for deoxyribonucleotides. Products with an apparent length of 14 nt and 7 nt are mainly synthesised. In addition to the primase and polymerase activities, the enzyme possesses a template-independent 3'-terminal nucleotidyl transferase activity Saccharolobus solfataricus P2 N(pN)n + n diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.B16 heterodimer
-
 Saccharolobus solfataricus

Synonyms

EC Number Synonyms Comment Organism
2.7.7.B16 PriSL
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.B16 60
-
 assay at Saccharolobus solfataricus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.B16 8
-
 the optimal glycine–NaOH buffer is at pH 9 (pH 8 at 60°C) Saccharolobus solfataricus