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Literature summary for 3.1.99.B2 extracted from

  • Roberts, J.A.; Bell, S.D.;, White, M.F.
    An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA (2003), Mol. Microbiol., 48, 361-371.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
proliferating-cell-nuclear-antigen Sulfolobus XPF is only active in the presence of the sliding clamp PCNA (Proliferating-Cell-Nuclear-Antigen), which is a heterotrimer in this organism. Interactions with two of the three subunits of PCNA are mediated via a C-terminal interaction motif. The PCNA-XPF complex acts as a structure-specificnuclease on a range of DNA flap, bubble and junction substrates Saccharolobus solfataricus

Cloned(Commentary)

Cloned (Comment) Organism
-
Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q7LXL5
-
-
Saccharolobus solfataricus P2 Q7LXL5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Sulfolobus XPF is only active in the presence of the sliding clamp PCNA (Proliferating-Cell-Nuclear-Antigen), which is a heterotrimer in this organism. Interactions with two of the three subunits of PCNA are mediated via a C-terminal interaction motif. The PCNA-XPF complex acts as a structure-specific nuclease on a range of DNA flap, bubble and junction substrates. The best substrate is a 3' flap structure, which is cut too quickly to allow accurate determination of the reaction rate using manual sampling methods. This rate is estimated as 6.8 per. The splayed duplex is cleaved at a rate of 0.60 per min, at least 10fold more slowly than the 3' flap substrate, and the fixed four-way junction is cut with a rate of 0.057 per min, 10-fold more slowly than the splayed duplex and 100fold more slowly than the flap substrate. As the four-way junction is cut in all four arms, the true rate of cleavage of this substrate is probably fourfold faster Saccharolobus solfataricus ?
-
?
additional information Sulfolobus XPF is only active in the presence of the sliding clamp PCNA (Proliferating-Cell-Nuclear-Antigen), which is a heterotrimer in this organism. Interactions with two of the three subunits of PCNA are mediated via a C-terminal interaction motif. The PCNA-XPF complex acts as a structure-specific nuclease on a range of DNA flap, bubble and junction substrates. The best substrate is a 3' flap structure, which is cut too quickly to allow accurate determination of the reaction rate using manual sampling methods. This rate is estimated as 6.8 per. The splayed duplex is cleaved at a rate of 0.60 per min, at least 10fold more slowly than the 3' flap substrate, and the fixed four-way junction is cut with a rate of 0.057 per min, 10-fold more slowly than the splayed duplex and 100fold more slowly than the flap substrate. As the four-way junction is cut in all four arms, the true rate of cleavage of this substrate is probably fourfold faster Saccharolobus solfataricus P2 ?
-
?

Synonyms

Synonyms Comment Organism
XPF repair endonuclease
-
Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
assay at Saccharolobus solfataricus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information the best substrate is a 3' flap structure, which is cut too quickly to allow accurate determination of the reaction rate using manual sampling methods. This rate is estimated as 6.8 per min. The splayed duplex is cleaved at a rate of 0.60 per min, at least 10-fold more slowly than the 3' flap substrate, and the fixed four-way junction is cut with a rate of 0.057 per min, 10fold more slowly than the splayed duplex and 100fold more slowly than the flap substrate. As the four-way junction is cut in all four arms, the true rate of cleavage of this substrate is probably fourfold faster Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
assay at Saccharolobus solfataricus