2.7.7.B16: DNA primase
This is an abbreviated version!
For detailed information about DNA primase, go to the full flat file.
Word Map on EC 2.7.7.B16
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2.7.7.B16
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single-stranded
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helicase
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polymerases
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bacteriophage
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primases
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fork
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priming
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oligoribonucleotides
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dnab
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polydt
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alpha-primase
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okazaki
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dna-dependent
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aphidicolin
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ssdna
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lagging-strand
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replisome
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alpha-amanitin
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primer-template
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rntp
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helicase-primase
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polymerase-primase
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rna-primed
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polymerase-alpha
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alpha-dna
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primosome
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primpol
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template-primer
- 2.7.7.B16
-
single-stranded
- helicase
- polymerases
- bacteriophage
- primases
- fork
-
priming
- oligoribonucleotides
- dnab
-
polydt
-
alpha-primase
-
okazaki
-
dna-dependent
- aphidicolin
- ssdna
-
lagging-strand
-
replisome
- alpha-amanitin
-
primer-template
- rntp
-
helicase-primase
-
polymerase-primase
-
rna-primed
-
polymerase-alpha
-
alpha-dna
-
primosome
- primpol
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template-primer
Reaction
Synonyms
archaeal eukaryotic-type primase, DNA primase-polymerase, DnaG primase, Mjpri, Pabp41, Pabp46, pIT3 replication protein, PolpTN2, PriL, PriS, PriSL, PriX, Sso core primase, SsoPriSL
ECTree
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Metals Ions
Metals Ions on EC 2.7.7.B16 - DNA primase
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K+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Mg2+
Mn2+
Zn2+
additional information
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Mg2+
Q9V292; Q9V291
optimal concentration: 10 mM. Activity is dependent on the presence of Mg2+ and Mn2+. Increased MgCl2 concentrations only slightly enhance NTP incorporation, in contrast to MnCl2
Mg2+
the enzyme is strictly dependent on divalent cations, activating metal preferably used by Rep245 for its DNA polymerase activity is Mg2+ at concentrations between 5 and 10 mM
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Mn2+
Q9V292; Q9V291
optimal concentration: 5 mM. Activity is dependent on the presence of Mg2+ and Mn2+. Increased MgCl2 concentrations only slightly enhance NTP incorporation, in contrast to MnCl2
Mn2+
the enzyme is strictly dependent on divalent cations, with Mn2+ as a cofactor, the DNA polymerase activity of Rep245 is optimal at 12.5 mM and decreases noticeably at increasing amounts of Mn2+
Mn2+
the enzyme requires manganese ions for catalytic activity
Mn2+
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in a MnCl2-soaked crystal, a Mn2+ is bound to one of the oxygens of the Asp111 side chain
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+
activity requires divalent cations such Mg2+, Mn2+ or Zn2+, and is additionally stimulated by the monovalent cation K+
Zn2+
Q9P9H1; Q8U4H7
the zinc ion is located within the loop region between beta-strand 6 and the prominent helix alpha4. It is coordinated by Cys 106 and His 108 of the loop and Cys114and Cys117 at the beginning of helix alpha4
Zn2+
contain one zinc ion in the small subunits. Residues Cys116, Cys119, Cys128 and Asp131 coordinate the zinc atom
Rep245 polymerase activity is strictly dependent on divalent cations (Mg2+ or Mn2+), Zn2+ cations do not support the DNA polymerization activity of Rep245
additional information
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Rep245 polymerase activity is strictly dependent on divalent cations (Mg2+ or Mn2+), Zn2+ cations do not support the DNA polymerization activity of Rep245