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Information on EC 2.7.7.B16 - DNA primase and Organism(s) Thermococcus kodakarensis and UniProt Accession Q5JJ72

for references in articles please use BRENDA:EC2.7.7.B16
preliminary BRENDA-supplied EC number
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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.B16 DNA primase
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This record set is specific for:
Thermococcus kodakarensis
UNIPROT: Q5JJ72 not found.
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The taxonomic range for the selected organisms is: Thermococcus kodakarensis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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dNTP
+
n
dNTP
=
dN(pdN)n
+
n
diphosphate
+
n
=
dN(pdN)n
+
n
NTP
+
n
NTP
=
N(pN)n
+
n
diphosphate
+
n
=
N(pN)n
+
n
Synonyms
dna primase, dnag primase, polptn2, ssoprisl, prisl, pabp41, pabp46, mjpri, pit3 replication protein, more
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + ATP
A(pA)n + n diphosphate
show the reaction diagram
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
show the reaction diagram
Q5JJ72; Q5JJ73
oligo(dT)30 supports extensive DNA and RNA synthesis
-
-
?
dATP + glycerol
dAMP-glycerol + diphosphate
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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 + n dGTP
dG(pdG)n + n diphosphate
show the reaction diagram
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
-
-
?
dGTP + Tris
dGMP-Tris + diphosphate
show the reaction diagram
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 dNTP
dN(pdN)n + n diphosphate
show the reaction diagram
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
-
-
?
dTTP + glycerol
dTMP-glycerol + diphosphate
show the reaction diagram
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
show the reaction diagram
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
-
-
?
GTP + n GTP
G(pG)n + n diphosphate
show the reaction diagram
Q5JJ72; Q5JJ73
oligo(dC)30 supports extensive DNA and RNA synthesis
-
-
?
NTP + n NTP
N(pN)n + n diphosphate
show the reaction diagram
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 0.09
ATP
0.03 - 0.04
dATP
0.05
dGTP
Q5JJ72; Q5JJ73
pH 8.0, 60°C, in presence of oligo(dC)
0.25
GTP
Q5JJ72; Q5JJ73
pH 8.0, 60°C, in presence of oligo(dC)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
Q5JJ72; Q5JJ73
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
Q5JJ72; Q5JJ73
assay at
70
Q5JJ72; Q5JJ73
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q5JJ72: small subunit and Q5JJ73: large subunit
Q5JJ72; Q5JJ73
SwissProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
Q5JJ72; Q5JJ73
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to repeated freezing and thawing
Q5JJ72; Q5JJ73
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Q5JJ72; Q5JJ73
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chemnitz Galal, W.; Pan, M.; Kelman, Z.; Hurwitz, J.
Characterization of DNA primase complex isolated from the archaeon, Thermococcus kodakaraensis
J. Biol. Chem.
287
16209-16219
2012
Thermococcus kodakarensis (Q5JJ72 and Q5JJ73), Thermococcus kodakarensis
Manually annotated by BRENDA team
Chemnitz Galal, W.; Pan, M.; Giulian, G.; Yuan, W.; Li, S.; Edwards, J.L.; Marino, J.P.; Kelman, Z.; Hurwitz, J.
Formation of dAMP-glycerol and dAMP-Tris derivatives by Thermococcus kodakaraensis DNA primase
J. Biol. Chem.
287
16220-16229
2012
Thermococcus kodakarensis (Q5JJ72 and Q5JJ73), Thermococcus kodakarensis
Manually annotated by BRENDA team