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Literature summary for 2.7.7.102 extracted from

  • Beck, K.; Vannini, A.; Cramer, P.; Lipps, G.
    The archaeo-eukaryotic primase of plasmid pRN1 requires a helix bundle domain for faithful primer synthesis (2010), Nucleic Acids Res., 38, 6707-6718 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Sulfolobus islandicus

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Sulfolobus islandicus

Protein Variants

Protein Variants Comment Organism
H141A loss of primase activity Sulfolobus islandicus
W314A poor primase activity Sulfolobus islandicus
W314F reduced primase activity Sulfolobus islandicus
W314Y reduced primase activity Sulfolobus islandicus
W347A no reduction in primase activity Sulfolobus islandicus
W361A no reduction in primase activity Sulfolobus islandicus
Y352A loss of primase activity Sulfolobus islandicus
Y352F no reduction in primase activity Sulfolobus islandicus
Y352H loss of primase activity Sulfolobus islandicus
Y352W loss of primase activity Sulfolobus islandicus
Y367A no reduction in primase activity Sulfolobus islandicus

Organism

Organism UniProt Comment Textmining
Sulfolobus islandicus Q54324 encoded on plasmid pRN1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5'-TTTTTTTTGTGCACTTT + n dNTP
-
Sulfolobus islandicus 5'-TTTTTTTTGTGCACTTT/pppdN(pdN)n-1 + (n-1) diphosphate
-
?

General Information

General Information Comment Organism
physiological function The minimal region of the protein required for primase activity encompasses amino-acid residues 40-370. The C-terminal part of the minimal region folds into a compact domain with six helices and is stabilized by a disulfide bond. The C-terminal helix of the helix bundle domain is required for primase activity Sulfolobus islandicus