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

BRENDA support

Literature summary for 3.6.1.23 extracted from

  • Tormo-Mas, M.A.; Donderis, J.; Garcia-Caballer, M.; Alt, A.; Mir-Sanchis, I.; Marina, A.; Penades, J.R.
    Phage dUTPases control transfer of virulence genes by a proto-oncogenic G protein-like mechanism (2013), Mol. Cell, 49, 947-958.
    View publication on PubMed
Search for more literature for 3.6.1.23

Protein Variants

Protein Variants Comment Organism
D81A mutant presents a 3fold reduced dUTP-binding capacity and an extremely low hydrolytic activity. Mutant is unable to induce transcription of the Stl-repressed SaPIbov1 genes even when expressed at a high level Dubowvirus dv80alpha
D81N mutant presents a 3fold reduced dUTP-binding capacity and an extremely low hydrolytic activity Dubowvirus dv80alpha
Y84A mutation of a strictly conserved residue. Mutant shows a reduced dUTP-binding capacity but retains some enzymatic activity Dubowvirus dv80alpha
Y84F mutation of a strictly conserved residue, mutant presents almost wild-type dUTP-binding capacity and activity Dubowvirus dv80alpha
Y84I mutation of a strictly conserved residue. Complete loss of dUTP-binding capacity Dubowvirus dv80alpha

Organism

Organism UniProt Comment Textmining
Dubowvirus dv80alpha A4ZF98
-
-

General Information

General Information Comment Organism
physiological function enzyme induces the transfer of staphylococcal pathogenicity island-encoded virulence factors by switching between active (dUTP-bound) and inactive (apo state) conformations, a conversion catalyzed by their intrinsic dUTPase activity. Binding to dUTP reorders the C-terminal motif V of the enzyme, rendering the protein into the active conformation required for staphylococcal pathogenicity island derepression. The conversion to the apo state conformation by hydrolysis of the bound dUTP generates a protein that is unable to induce the staphylococcal pathogenicity island cycle Dubowvirus dv80alpha