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Information on EC 2.7.7.B16 - DNA primase
for references in articles please use BRENDA:EC2.7.7.B16preliminary BRENDA-supplied EC number
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EC Tree
2.7.7.B16 DNA primaseSpecify your search results
Word Map
- 2.7.7.B16
-
single-stranded
- helicase
- polymerases
- bacteriophage
- primases
- fork
-
priming
- oligoribonucleotides
- dnab
-
polydt
-
alpha-primase
-
okazaki
-
dna-dependent
- aphidicolin
- ssdna
-
lagging-strand
-
replisome
- alpha-amanitin
-
primer-template
- rntp
-
helicase-primase
-
polymerase-primase
-
rna-primed
-
polymerase-alpha
-
alpha-dna
-
primosome
- primpol
-
template-primer
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
n
=
dN(pdN)n
+
n
+
n
=
N(pN)n
+
n
Synonyms
dna primase, dnag primase, polptn2, ssoprisl, prisl, pabp41, pabp46, mjpri, pit3 replication protein, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Mjpri
pIT3 replication protein
PriSL
Sso core primase
SsoPriSL
pIT3 replication protein
the Rep245 protein is the N-terminal domain of the pIT3 replication protein encompassing residues 31245
pIT3 replication protein
the Rep245 protein is the N-terminal domain of the pIT3 replication protein encompassing residues 31245
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dNTP + n dNTP = dN(pdN)n + n diphosphate
-
-
-
-
NTP + n NTP = N(pN)n + n diphosphate
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + ATP
A(pA)n + n diphosphate
Q5JJ72; Q5JJ73
oligo(dT)30 supports extensive DNA and RNA synthesis. Oligo(dT)30 supports the synthesis of shorter RNA chains than those formed in the presence of oligo(dC)30 as well as the production of higher levels of RNA than DNA
-
-
?
dATP + dATP
dA(pdA)n + n diphosphate
Q5JJ72; Q5JJ73
oligo(dT)30 supports extensive DNA and RNA synthesis
-
-
?
dATP + glycerol
dAMP-glycerol + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dATP + Tris
dAMP-Tris + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dCTP + glycerol
dAMP-glycerol + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dCTP + Tris
dAMP-Tris + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dGTP + glycerol
dGMP-glycerol + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dGTP + Tris
dGMP-Tris + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dNTP + n NTP
(dNTP)n+1 + n diphosphate
Q9V292; Q9V291
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
-
-
?
dTTP + glycerol
dTMP-glycerol + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
dTTP + Tris
dTMP-Tris + diphosphate
Q5JJ72; Q5JJ73
the products are formed by the p41 catalytic subunit alone and the p41-p46 complex in the absence of a DNA template. They are not formed with preparations containing the catalytically inactive p41 subunit
-
-
?
ATP + n ATP
A(pA)n + n diphosphate
the enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
ATP + n ATP
A(pA)n + n diphosphate
the enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
dGTP + n dGTP
dG(pdG)n + n diphosphate
the catalytic efficiency of the primase heterodimer for dGMP incorporation is 3.6fold higher than that for GMP incorporation
-
-
?
dGTP + n dGTP
dG(pdG)n + n diphosphate
Q5JJ72; Q5JJ73
oligo(dC)30 supports extensive DNA and RNA synthesis. Of the four homo-oligodeoxynucleotides, 30 nt in length oligo(dC)30 is the most effective template supporting extensive DNA synthesis with dGTP. dGTP incorporation exceeds the level of oligo(dC)30 template added, and the lengths of DNA chains are 100 nt
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
Q9P9H1; Q8U4H7
the p41-p46 primase preferentially uses dNTPs compared to NTPs. DNA strand synthesis is stimulated by the addition of NTPs or by addition of ATP to the same level. ATP is the preferable initiating nucleotide for the p41-p46 complex
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
de novo DNA synthesis is 10 times more effective than RNA synthesis
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
-
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
-
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
the enzyme is capable of template-dependent nucleotide polymerization across discontinuous dsDNA templates. The products are shorter than those obtained on ssDNA templates. It prefers NTP over dNTP in template-dependent nucleotide polymerization. The enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
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
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
utilizes poly-pyrimidine single-stranded DNA templates with low efficiency for de novo synthesis of RNA primers. Its synthetic function is specifically activated by thymine-containing synthetic bubble structures that mimic early replication intermediates. The enzyme is able to incorporate dATP on oligo(A)15/poly(dT) but with lower efficiency with respect to ATP. In addition, the Sso DNA primase is not able to elongate oligo(rA)15 when it is not annealed to poly(dT) or to initiate de novo synthesis on poly(dT) with dATP
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
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
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
utilizes poly-pyrimidine single-stranded DNA templates with low efficiency for de novo synthesis of RNA primers. Its synthetic function is specifically activated by thymine-containing synthetic bubble structures that mimic early replication intermediates. The enzyme is able to incorporate dATP on oligo(A)15/poly(dT) but with lower efficiency with respect to ATP. In addition, the Sso DNA primase is not able to elongate oligo(rA)15 when it is not annealed to poly(dT) or to initiate de novo synthesis on poly(dT) with dATP
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
the enzyme is capable of template-dependent nucleotide polymerization across discontinuous dsDNA templates. The products are shorter than those obtained on ssDNA templates. It prefers NTP over dNTP in template-dependent nucleotide polymerization. The enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
Q5JJ72; Q5JJ73
the enzyme supports both DNA and RNA synthesis, whereas the p41 subunit alone marginally produces RNA and synthesizes DNA chains that are longer than those formed by the complex. The primase complex preferentially interacts with dNTP rather than ribonucleoside triphosphates and initiates RNA as well as DNA chains de novo. The archaeal primase complex, in contrast to the eukaryote homolog, can initiate DNA chain synthesis in the absence of ribonucleoside triphosphates. DNA primers formed by the archaeal complex can be elongated extensively by the Thermococcus kodakaraensis DNA polymerase (Pol) B, whereas DNA primers formed by the p41 catalytic subunit alone are not
-
-
?
GTP + n GTP
G(pG)n + n diphosphate
the enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
GTP + n GTP
G(pG)n + n diphosphate
the catalytic efficiency of the primase heterodimer for dGMP incorporation is 3.6fold higher than that for GMP incorporation
-
-
?
GTP + n GTP
G(pG)n + n diphosphate
Q5JJ72; Q5JJ73
oligo(dC)30 supports extensive DNA and RNA synthesis
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
synthesise oligoribonucleotides on various pyrimidine single-stranded DNA templates poly(dT) and poly(dC). The enzyme is almost completely inactive on a poly(dA) synthetic template
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
synthesise oligoribonucleotides on various pyrimidine single-stranded DNA templates poly(dT) and poly(dC). The enzyme is almost completely inactive on a poly(dA) synthetic template
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
Q9V292; Q9V291
the multifunctional archaeal primase is involved in priming and repair
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
Q9V292; Q9V291
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
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
Q9P9H1; Q8U4H7
the p41-p46 complex synthesizes the primers, which can be extended in the combination with other replication proteins from Pyrococcus furiosus
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
Q9P9H1; Q8U4H7
the p41-p46 primase preferentially uses dNTPs compared to NTPs. The primase complex synthesizes RNA segments only when NTPs but not dNTPs are added as the substrates. When both dNTPs and NTPs exist at equal concentrations, no RNA products are observed. ATP is the preferable initiating nucleotide for the p41-p46 complex
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the small subunit of the clamp loader replication factor C (RFC) of Sulfolobus solfataricus interacts with both the catalytic and non-catalytic subunits of the primase. The primase-clamp loader replication factor C interaction modulates the activities of both enzymes and therefore may be involved in the regulation of primer synthesis and the transfer of primers to DNA polymerase in archaea
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
de novo synthesis of larger molecular size RNA products when incubated with M13 mp18 single-stranded DNA in the presence of a ribonucleotide mixture. The Rep245 domain is capable of utilizing both ribonucleotides and deoxyribonucleotides for de novo primer synthesis and it synthesizes DNA products up to several kb in length in a template-dependent manner. The Rep245 primase-polymerase domain harbors also a terminal nucleotidyl transferase activity, being able to elongate the 3'-end of synthetic oligonucleotides in a non-templated manner. The Rep245 domain contains the catalytic residues required for both primase and polymerase activities
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the enzyme is capable of template-dependent nucleotide polymerization across discontinuous dsDNA templates. The products are shorter than those obtained on ssDNA templates. It prefers NTP over dNTP in template-dependent nucleotide polymerization. The enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
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
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
utilizes poly-pyrimidine single-stranded DNA templates with low efficiency for de novo synthesis of RNA primers. Its synthetic function is specifically activated by thymine-containing synthetic bubble structures that mimic early replication intermediates. The enzyme is able to incorporate dATP on oligo(rA)15/poly(dT) but with lower efficiency with respect to rATP. In addition, the Sso DNA primase is not able to elongate oligo(rA)15 when it is not annealed to poly(dT) or to initiate de novo synthesis on poly(dT) with dATP
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
de novo synthesis of larger molecular size RNA products when incubated with M13 mp18 single-stranded DNA in the presence of a ribonucleotide mixture. The Rep245 domain is capable of utilizing both ribonucleotides and deoxyribonucleotides for de novo primer synthesis and it synthesizes DNA products up to several kb in length in a template-dependent manner. The Rep245 primase-polymerase domain harbors also a terminal nucleotidyl transferase activity, being able to elongate the 3'-end of synthetic oligonucleotides in a non-templated manner. The Rep245 domain contains the catalytic residues required for both primase and polymerase activities
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
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
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the small subunit of the clamp loader replication factor C (RFC) of Sulfolobus solfataricus interacts with both the catalytic and non-catalytic subunits of the primase. The primase-clamp loader replication factor C interaction modulates the activities of both enzymes and therefore may be involved in the regulation of primer synthesis and the transfer of primers to DNA polymerase in archaea
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
utilizes poly-pyrimidine single-stranded DNA templates with low efficiency for de novo synthesis of RNA primers. Its synthetic function is specifically activated by thymine-containing synthetic bubble structures that mimic early replication intermediates. The enzyme is able to incorporate dATP on oligo(rA)15/poly(dT) but with lower efficiency with respect to rATP. In addition, the Sso DNA primase is not able to elongate oligo(rA)15 when it is not annealed to poly(dT) or to initiate de novo synthesis on poly(dT) with dATP
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the enzyme is capable of template-dependent nucleotide polymerization across discontinuous dsDNA templates. The products are shorter than those obtained on ssDNA templates. It prefers NTP over dNTP in template-dependent nucleotide polymerization. The enzyme synthesizes substantially more products on oligo(dC) with GTP as the substrate than on oligo(dT) with ATP as the substrate
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
Q5JJ72; Q5JJ73
the enzyme supports both DNA and RNA synthesis, whereas the p41 subunit alone marginally produces RNA and synthesizes DNA chains that are longer than those formed by the complex. The primase complex preferentially interacts with dNTP rather than ribonucleoside triphosphates and initiates RNA as well as DNA chains de novo. The archaeal primase complex, in contrast to the eukaryote homolog, can initiate DNA chain synthesis in the absence of ribonucleoside triphosphates. DNA primers formed by the archaeal complex can be elongated extensively by the Thermococcus kodakaraensis DNA polymerase (Pol) B, whereas DNA primers formed by the p41 catalytic subunit alone are not. When M13DNA is used as substrate all labeled rNTPs and dNTPs support RNA and DNA synthesis
-
-
?
additional information
?
-
the enzyme although shows 3'-terminal nucleotidyl-transferase activity
-
-
?
additional information
?
-
-
the enzyme although shows 3'-terminal nucleotidyl-transferase activity
-
-
?
additional information
?
-
-
interaction of Sulfolobus solfataricus DnaG primase (SsoDnaG) with the replicative minichromosome maintenance helicase (SsoMCM) on DNA. The site of interaction is mapped. The complex of SsoDnaG with SsoMCM stimulates the ATPase activity of SsoMCM but leaves the priming activity of SsoDnaG unchanged
-
-
?
additional information
?
-
usage of M13mp18ssDNA as a template
-
-
?
additional information
?
-
-
usage of M13mp18ssDNA as a template
-
-
?
additional information
?
-
the enzyme although shows 3'-terminal nucleotidyl-transferase activity
-
-
?
additional information
?
-
-
primase PolpTN2 is able to prime the synthesis of dsDNA by Taq DNA polymerase and by DNA polymerase PolB encoded by the chromosome of Thermococcus nautili using M13mp18ssDNA as a template, method development and evaluation, overview. Mechanism of template-free synthesis of seeds by PolB and PolpTN2 from dNTP substrates
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
interaction of Sulfolobus solfataricus DnaG primase (SsoDnaG) with the replicative minichromosome maintenance helicase (SsoMCM) on DNA. The site of interaction is mapped. The complex of SsoDnaG with SsoMCM stimulates the ATPase activity of SsoMCM but leaves the priming activity of SsoDnaG unchanged
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
de novo DNA synthesis is 10 times more effective than RNA synthesis
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
-
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
-
-
-
?
dNTP + n dNTP
dN(pdN)n + n diphosphate
-
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
Q9V292; Q9V291
the multifunctional archaeal primase is involved in priming and repair
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
Q9P9H1; Q8U4H7
the p41-p46 complex synthesizes the primers, which can be extended in the combination with other replication proteins from Pyrococcus furiosus
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the small subunit of the clamp loader replication factor C (RFC) of Sulfolobus solfataricus interacts with both the catalytic and non-catalytic subunits of the primase. The primase-clamp loader replication factor C interaction modulates the activities of both enzymes and therefore may be involved in the regulation of primer synthesis and the transfer of primers to DNA polymerase in archaea
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
-
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
the small subunit of the clamp loader replication factor C (RFC) of Sulfolobus solfataricus interacts with both the catalytic and non-catalytic subunits of the primase. The primase-clamp loader replication factor C interaction modulates the activities of both enzymes and therefore may be involved in the regulation of primer synthesis and the transfer of primers to DNA polymerase in archaea
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Mg2+
Mn2+
Zn2+
additional information
Mg2+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Mg2+
Q9V292; Q9V291
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
Mg2+
the enzyme is strictly dependent on divalent cations, activating metal preferably used by Rep245 for its DNA polymerase activity is Mg2+ at concentrations between 5 and 10 mM
Mn2+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Mn2+
Q9V292; Q9V291
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
Mn2+
the enzyme is strictly dependent on divalent cations, with Mn2+ as a cofactor, the DNA polymerase activity of Rep245 is optimal at 12.5 mM and decreases noticeably at increasing amounts of Mn2+
Mn2+
the enzyme requires manganese ions for catalytic activity
Mn2+
-
in a MnCl2-soaked crystal, a Mn2+ is bound to one of the oxygens of the Asp111 side chain
Mn2+
Q5JJ72; Q5JJ73
RNA synthesis with the Thermococcus kodakaraensis primase complex is stimulated about 2fold by the presence of Mn2+, whereas the size of RNA chains is marginally affected. DNA synthesis is slightly inhibited by Mn2+
Zn2+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Zn2+
Q9P9H1; Q8U4H7
the zinc ion is located within the loop region between beta-strand 6 and the prominent helix alpha4. It is coordinated by Cys 106 and His 108 of the loop and Cys114and Cys117 at the beginning of helix alpha4
Zn2+
contain one zinc ion in the small subunits. Residues Cys116, Cys119, Cys128 and Asp131 coordinate the zinc atom
additional information
Rep245 polymerase activity is strictly dependent on divalent cations (Mg2+ or Mn2+), Zn2+ cations do not support the DNA polymerization activity of Rep245
additional information
-
Rep245 polymerase activity is strictly dependent on divalent cations (Mg2+ or Mn2+), Zn2+ cations do not support the DNA polymerization activity of Rep245
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dATP
Q5JJ72; Q5JJ73
synthesis of the short RNA chains is inhibited at all levels of dATP added, and the size of oligo(rA) chains formed and the amount of ATP incorporated are reduced
dGTP
Q5JJ72; Q5JJ73
dGTP at a molar ratio of dGTP to dATP or rATP of 10:1 inhibits both DNA and RNA synthesis. Lower molar ratios of dGTP:rATP (0.1:1) inhibit ATP incorporation by 91%, whereas dATP incorporation is reduced by 8%
GTP
Q5JJ72; Q5JJ73
dGTP at a molar ratio of dGTP to dATP or rATP of 10:1 reduces dATP incorporation by 43% and ATP incorporation by 92%
Mn2+
Q5JJ72; Q5JJ73
RNA synthesis with the Thermococcus kodakaraensis primase complex is stimulated about 2fold by the presence of Mn2+, whereas the size of RNA chains is marginally affected. DNA synthesis is slightly inhibited by Mn2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
Q5JJ72; Q5JJ73
in the presence of high levels of ATP (ATP:dATP molar ratio of 10:1), dAMP incorporation is stimulated 3-fold, although the size of dAMP-labeled products formed is reduced
additional information
synthetic function is specifically activated by thymine-containing synthetic bubble structures that mimic early replication intermediates
-
additional information
-
synthetic function is specifically activated by thymine-containing synthetic bubble structures that mimic early replication intermediates
-
additional information
PriL but not PriX enhances primer extension by PriS
-
additional information
-
PriL but not PriX enhances primer extension by PriS
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Effect of alpha-1-antichymotrypsin on activity of DNA primase isolated from human stomach adenocarcinoma cells.
Adenocarcinoma
Incorporation of alpha-1-antichymotrypsin into human stomach adenocarcinoma cell nuclei and inhibition of DNA primase activity.
Breast Neoplasms
DNA primase polypeptide 1 (PRIM1) involves in estrogen-induced breast cancer formation through activation of the G2/M cell cycle checkpoint.
Carcinoma
Effect of alpha-1-antichymotrypsin on activity of DNA primase isolated from human stomach adenocarcinoma cells.
Carcinoma
Incorporation of alpha-1-antichymotrypsin into human stomach adenocarcinoma cell nuclei and inhibition of DNA primase activity.
Carcinoma, Hepatocellular
DNA primase subunit 1 deteriorated progression of hepatocellular carcinoma by activating AKT/mTOR signaling and UBE2C-mediated P53 ubiquitination.
Carcinoma, Hepatocellular
DNA Primase Subunit 1 Expression in Hepatocellular Carcinoma and Its Clinical Implication.
Carcinoma, Hepatocellular
Inhibition of DNA primase and induction of apoptosis by 3,3'-diethyl-9-methylthia-carbocyanine iodide in hepatocellular carcinoma BEL-7402 cells.
Herpes Simplex
Herpes Simplex Virus-1 DNA Primase: A Remarkably Inaccurate yet Selective Polymerase.
Herpes Simplex
Herpes simplex virus-1 primase: a polymerase with extraordinarily low fidelity.
Herpes Simplex
Identification and characterization of a DNA primase activity present in herpes simplex virus type 1-infected HeLa cells.
Herpes Simplex
Release of RNA polymerase from vero cell mitochondria after herpes simplex virus type 1 infection.
Herpes Simplex
The herpes simplex virus type 1 origin-binding protein interacts specifically with the viral UL8 protein.
Infections
Minute virus of mice-induced modification of the murine DNA polymerase alpha-primase complex permits the salt-induced dissociation of 12S DNA primase and 10S DNA polymerase alpha components.
Infections
Release of RNA polymerase from vero cell mitochondria after herpes simplex virus type 1 infection.
Leishmaniasis
Evaluation of potential drugs against leishmaniasis targeting catalytic subunit of Leishmania donovani nuclear DNA primase using ligand based virtual screening, docking and molecular dynamics approaches.
Leukemia
Apoptosis induced by DNA primase inhibitor 3,3'-diethyl-9-methylthia-carbocyanine iodide in human leukemia HL-60 cells.
Leukemia
Differential inhibition of various deoxyribonucleic acid polymerases by Evans blue and aurintricarboxylic acid.
Leukemia
Differential inhibition of various deoxyribonucleic and ribonucleic acid polymerases by suramin.
Leukemia, Myeloid
Apoptosis induced by DNA primase inhibitor 3,3'-diethyl-9-methylthia-carbocyanine iodide in human leukemia HL-60 cells.
Neoplasms
DNA primase subunit 1 deteriorated progression of hepatocellular carcinoma by activating AKT/mTOR signaling and UBE2C-mediated P53 ubiquitination.
Neoplasms
DNA Primase Subunit 1 Expression in Hepatocellular Carcinoma and Its Clinical Implication.
Neoplasms
Mutation of DNA primase causes extensive apoptosis of retinal neurons through the activation of DNA damage checkpoint and tumor suppressor p53.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Inhibition of DNA primase by nucleoside triphosphates and their arabinofuranosyl analogs.
Starvation
Mechanisms of physiological regulation of RNA synthesis in bacteria: new discoveries breaking old schemes.
Tuberculosis
in silico screening and molecular dynamics simulations study to identify novel potent inhibitors against Mycobacterium tuberculosis DnaG primase.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.028
dNTP
pH 8.0, 60°C, in presence of M13 ssDNA as template
0.0032
NTP
recombinant PriSLX, pH 6.5, 55°C
0.025
NTP
pH 8.0, 60°C, in presence of M13 ssDNA as template
additional information
additional information
Q9V292; Q9V291
kinetic parameters for the DNA primase under different metal ion conditions
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additional information
additional information
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kinetic parameters for the DNA primase under different metal ion conditions
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000013
NTP
recombinant PriSL, pH 6.5, 55°C
0.00078
NTP
recombinant PriSX, pH 6.5, 55°C
0.0068
NTP
recombinant PriSLX, pH 6.5, 55°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
the optimal glycineNaOH buffer is at pH 9 (pH 8 at 60°C)
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
pH 7.0: about 40% of maximal activity, pH 8.5: about 50% of maximal activity
7.5 - 8.5
pH 7.5: about 40% of maximal activity, pH 8.5: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 75
45°C: about 40% of maximal activity, 75°C: about 40% of maximal activity
55 - 70