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Information on EC 2.7.7.B16 - DNA primase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58249

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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Methanocaldococcus jannaschii
UNIPROT: Q58249
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Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NTP + n NTP
N(pN)n + n diphosphate
show the reaction diagram
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Mg2+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Mn2+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Zn2+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
pH 7.5: about 40% of maximal activity, pH 8.5: about 70% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41800
x * 41800, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 41800, calculated from sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
1 h, enzyme is stable
70
10 min, 20% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Desogus, G.; Onesti, S.; Brick, P.; Rossi, M.; Pisani, F.M.
Identification and characterization of a DNA primase from the hyperthermophilic archaeon Methanococcus jannaschii
Nucleic Acids Res.
27
4444-4450
1999
Methanocaldococcus jannaschii (Q58249), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii JAL-1 (Q58249)
Manually annotated by BRENDA team