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

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The enzyme appears in viruses and cellular organisms

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
ORF56; REN1H1, plasmid pRN1, orf 904
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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PolpTN2 is indeed formed by the association of an N-terminal DNA polymerase/primase domain and a C-terminal domain whose sequences bear a distant similarity to the catalytic and regulatory subunits, respectively, of heterodimeric (PriS-PriL) archaeal and eukaryotic primases. The N-terminal domain possesses reverse transcriptase activity this activity can reflect an ancestral function of archaeal and eukaryotic primases proteins in the transition from the RNA to the DNA world
malfunction
physiological function
additional information
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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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
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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
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
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
8
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primase assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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primase assay at
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the enzyme protein corresponds to a fusion between an N-terminal domain homologous to the small catalytic subunit PriS of heterodimeric archaeal and eukaryotic primases and a C-terminal domain related to their large regulatory subunit PriL. This unique domain configuration is not found in other virus- and plasmid-encoded primases in which PriS-like domains are typically fused to different types of helicases, domain organization of the PolpTN2 primase–polymerase, three-dimensional structure comparisons, overview
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
cloning of plasmid pRN1, DNA and amino acid sequence determination and analysis, genetic structure and stem-loop structures within the 232-bp pRN1 putative origin of replication, overview. Quantitative RT-PCR expression analysis, mapping the putative origin of replication of pRN1
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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sequence analysis and comparisons of the N-terminal PriS-like domain of PolpTN2
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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
additional information