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Literature summary for 2.7.7.7 extracted from

  • Kumar, S.; Bakhtina, M.; Tsai, M.D.
    Altered order of substrate binding by DNA polymerase X from African swine fever virus (2008), Biochemistry, 47, 7875-7887.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli African swine fever virus

Inhibitors

Inhibitors Comment Organism Structure
35dd(G) DNA competitive inhibition African swine fever virus
dATP using dATP as an inhibitor and dCTP as a varied substrate, the pattern of inhibition is competitive African swine fever virus
additional information Pol X is not inhibited noticeably by up to 1 mM diphosphate, at higher concentrations there is modest inhibition African swine fever virus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ binding of Mg2+-dNTP to Pol X facilitates subsequent formation of the catalytically competent Pol X-DNA-dNTP ternary complex, Pol X prefers an ordered sequential mechanism with Mg2+-dNTP as the first substrate African swine fever virus

Organism

Organism UniProt Comment Textmining
African swine fever virus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
African swine fever virus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn
-
African swine fever virus diphosphate + DNAn+1
-
?

Synonyms

Synonyms Comment Organism
DNA polymerase X
-
African swine fever virus
Pol X
-
African swine fever virus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00046
-
35dd(G) DNA
-
African swine fever virus
0.048
-
dATP
-
African swine fever virus