Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Hu, J.; Guo, L.; Wu, K.; Liu, B.; Lang, S.; Huang, L.
    Template-dependent polymerization across discontinuous templates by the heterodimeric primase from the hyperthermophilic archaeon Sulfolobus solfataricus (2012), Nucleic Acids Res., 40, 3470-3483 .
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.102 Saccharolobus solfataricus Q97Z83 and Q9UWW1 Q97Z83 i.e. small subunit PriS, Q9UWW1 i.e. large subunit PriL
-
2.7.7.102 Saccharolobus solfataricus DSM 16170 Q97Z83 and Q9UWW1 Q97Z83 i.e. small subunit PriS, Q9UWW1 i.e. large subunit PriL
-

Synonyms

EC Number Synonyms Comment Organism
2.7.7.102 SSO0557 large subunit Saccharolobus solfataricus
2.7.7.102 SSO1048 small subunit Saccharolobus solfataricus

General Information

EC Number General Information Comment Organism
2.7.7.102 physiological function the enzyme is able to synthesize products far longer than templates in vitro. The long products result from template-dependent polymerization across discontinuous templates, which is initiated through either primer synthesis or terminal transfer, and occurs efficiently on templates containing contiguous dCs. The enzyme is able to promote strand annealing. PriSL catalyzes template-dependent polymerization across discontinuous templates with either dNTPs or rNTPs as the substrates but prefers the latter Saccharolobus solfataricus