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Information on EC 2.7.7.B16 - DNA primase and Organism(s) Pyrococcus horikoshii and UniProt Accession O57934

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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Pyrococcus horikoshii
UNIPROT: O57934 not found.
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The enzyme appears in selected 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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dNTP + n dNTP
dN(pdN)n + n diphosphate
show the reaction diagram
de novo DNA synthesis is 10 times more effective than RNA synthesis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dNTP + n dNTP
dN(pdN)n + n diphosphate
show the reaction diagram
de novo DNA synthesis is 10 times more effective than RNA synthesis
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
O57934: small subunit, O57935: large subunit
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
at the initiation of chromosomal DNA replication, DNA primases synthesize short RNA primers, which are subsequently elongated by DNA polymerases
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cocrystalization with uridine 5'-triphosphate allowing confirmation of the location of the active site. Construction of a model between the DNA primase and a primer/template DNA based on the complex structure for the primer synthesis
crystallographic studies of of the N-terminal domain (NTD) of PriL (PriLNTD; residues 1–222) that bind to PriS, 2.9 A resolution
hanging-drop vapor diffusion method at 20°C, with polyethylene glycol 8000 as the precipitant. The crystals belong to the P3(2)21 with unit-cell parameters a = b = 77.8, c = 129.6 A, and alpha = beta = 90°, gamma = 120°. Crystals of the selenomethionine derivative are obtained by means of a cross-seeding method using native crystals. The data for the native and selenomethionine-substituted crystals are collected to 1.8 and 2.2 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y155A/Y156A/I157A
mutation reduces PriS binding 1000fold
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
hexa-histidine tagged enzyme is expressed in Escherichia coli
overexpression in Escherichia coli as a fusion protein with a hexa-histidine tag
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Matsui, E.; Nishio, M.; Yokoyama, H.; Harata, K.; Darnis, S.; Matsui, I.
Distinct domain functions regulating de novo DNA synthesis of thermostable DNA primase from hyperthermophile Pyrococcus horikoshii
Biochemistry
42
14968-14976
2003
Pyrococcus horikoshii (O57934 and O57935), Pyrococcus horikoshii
Manually annotated by BRENDA team
Ito, N.; Matsui, I.; Matsui, E.
Molecular basis for the subunit assembly of the primase from an archaeon Pyrococcus horikoshii
FEBS J.
274
1340-1351
2007
Pyrococcus horikoshii (O57934 and O57935)
Manually annotated by BRENDA team
Ito, N.; Nureki, O.; Shirouzu, M.; Yokoyama, S.; Hanaoka, F.
Crystal structure of the Pyrococcus horikoshii DNA primase-UTP complex: implications for the mechanism of primer synthesis
Genes Cells
8
913-923
2003
Pyrococcus horikoshii (O57934 and O57935), Pyrococcus horikoshii
Manually annotated by BRENDA team
Ito, N.; Nureki, O.; Shirouzu, M.; Yokoyama, S.; Hanaoka, F.
Crystallization and preliminary X-ray analysis of a DNA primase from hyperthermophilic archaeon Pyrococcus horikoshii
J. Biochem.
130
727-730
2001
Pyrococcus horikoshii (O57934 and O57935), Pyrococcus horikoshii
Manually annotated by BRENDA team