Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ATP | ATP binding enhances sequence-specific DNA recognition for primase anchoring | Sulfolobus islandicus |
Cloned (Comment) | Organism |
---|---|
- |
Sulfolobus islandicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ssDNA + n dNTP | Sulfolobus islandicus | primases have a fundamental role in DNA replication. They synthesize a primer that is then extended by DNA polymerases | ssDNA/pppdN(pdN)n-1 hybrid + (n-1) diphosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sulfolobus islandicus | Q54324 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Sulfolobus islandicus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ssDNA + n dNTP | primases have a fundamental role in DNA replication. They synthesize a primer that is then extended by DNA polymerases | Sulfolobus islandicus | ssDNA/pppdN(pdN)n-1 hybrid + (n-1) diphosphate | - |
? | |
ssDNA + n dNTP | a small helical bundle prepares primer synthesis by binding two nucleotides that enhance sequence-specific recognition of the DNA template. Archaeoeukaryotic primases require for synthesis a catalytic and an accessory domain. For the pRN1 archaeal primase, this domain is a 115-amino acid helix bundle domain (HBD). Only the HBD binds the DNA template. DNA binding becomes sequence-specific after a major allosteric change in the HBD, triggered by the binding of two nucleotide triphosphates | Sulfolobus islandicus | ssDNA/pppdN(pdN)n-1 hybrid + (n-1) diphosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
primase HBD | - |
Sulfolobus islandicus |
General Information | Comment | Organism |
---|---|---|
physiological function | primases have a fundamental role in DNA replication. They synthesize a primer that is then extended by DNA polymerases | Sulfolobus islandicus |