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Literature summary for 3.6.1.23 extracted from

  • Szabo, J.E.; Nemeth, V.; Papp-Kadar, V.; Nyiri, K.; Leveles, I.; Bendes, A.A.; Zagyva, I.; Rona, G.; Palinkas, H.L.; Besztercei, B.; Ozohanics, O.; Vekey, K.; Liliom, K.; Toth, J.; Vertessy, B.G.
    Highly potent dUTPase inhibition by a bacterial repressor protein reveals a novel mechanism for gene expression control (2014), Nucleic Acids Res., 42, 11912-11920.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Staphylococcus phage phi11 Q8SDV3
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General Information

General Information Comment Organism
physiological function the expression of phage-related pathogenicity islands transfer initiating proteins is repressed by proteins called Stl. Phage phi11 helper phage dUTPase eliminates Stl binding to its cognate DNA by binding tightly to Stl protein. dUTPase enzymatic activity is strongly inhibited in the dUTPase:Stl complex and the dUTPase:dUTP complex is inaccessible to the Stl repressor Staphylococcus phage phi11