Information on EC 2.7.7.B17 - primase (sequence-specific)

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The expected taxonomic range for this enzyme is: Sulfolobus islandicus

EC NUMBER
COMMENTARY hide
2.7.7.B17
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
primase (sequence-specific)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NTP + 7 dNTP = N(pdN)7 + 7 diphosphate
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
plasmid pRN1
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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primases are specialized DNA-dependent RNA polymerases that synthesize a short oligoribonucleotide complementary to single-stranded template DNA. In the context of cellular DNA replication, primases are indispensable since DNA polymerases are not able to start DNA polymerization de novo
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 7 dNTP
A(pdN)7 + 7 diphosphate
show the reaction diagram
NTP + 7 dNTP
N(pdN)7 + 7 diphosphate
show the reaction diagram
additional information
?
-
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multifunctional replication protein with primase, DNA polymerase and helicase activity. The minimal region required for primase activity encompasses amino-acid residues 40–370
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NTP + 7 dNTP
N(pdN)7 + 7 diphosphate
show the reaction diagram
-
primases are specialized DNA-dependent RNA polymerases that synthesize a short oligoribonucleotide complementary to single-stranded template DNA. In the context of cellular DNA replication, primases are indispensable since DNA polymerases are not able to start DNA polymerization de novo
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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His141 is involved in the coordination of the zinc ion
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine 5'-(beta,gamma-imido)triphosphate
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adenosine 5'-(beta,gamma-methylenetriphosphate)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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pH 7.5, 50°C, kinetic properties of the primase activity
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Sulfolobus islandicus
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pH 7.5, 50°C, kinetic properties of the primase activity
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Sulfolobus islandicus
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pH 7.5, 50°C, kinetic properties of the primase activity
2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
primase domain, hanging drop vapour diffusion technique
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in Escherichia coli as a His-tagged protein
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expression in Escherichia coli, wild-type and mutant enzymes
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D111A
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the mutant protein is deficient and DNA polymerase activity and primase activity, ATPase activity is unaffected
delC370
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deletion mutant retains the strict ATP dependence for primer synthesis
delC526
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deletion mutant retains the strict ATP dependence for primer synthesis
F260A
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primase activity is similar to wild-type enzyme
H141A
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mutant enzyme without primase and polymerase activity
W314A
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primer formation is severely impaired, very small amount of wild-type like products are formed
W347A
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primase activity is similar to wild-type enzyme
W361A
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primase activity is similar to wild-type enzyme
Y352A
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primase activity is completely abolished
Y367A
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primase activity is similar to wild-type enzyme