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

BRENDA support

Literature summary for 2.7.7.7 extracted from

  • Zheng, R.; Matsui, E.; Shen, Y.; Musti, K.V.; Feng, Y.; Darnis, S.; Kawarabayasi, Y.; Kikuchi, H.; Harata, K.; Matsui, I.
    The novel function of a short region K253xRxxxD259 conserved in the exonuclease domain of hyperthermostable DNA polymerase I from Pyrococcus horikoshii (2001), Extremophiles, 5, 111-117.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D259E moderate decrease of the polymerizing activity Pyrococcus horikoshii
D259G moderate decrease of the polymerizing activity Pyrococcus horikoshii
D259K the exonuclease activity of the mutant enzyme decreases drastically to 0.58% compared with that of the wild-type DNA polymerase Pyrococcus horikoshii
D259N moderate decrease of the polymerizing activity Pyrococcus horikoshii
K253E exonuclease activity of mutant increases 2.7fold compared to wild-type activity Pyrococcus horikoshii
K253E/R255E exonuclease activity of mutant increases 1.8fold compared to wild-type activity Pyrococcus horikoshii
R255D exonuclease activity of mutant increases 2.9fold compared to wild-type activity Pyrococcus horikoshii

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the negative charge and the side-chain length of D259 might play a supporting role in coordinating the conserved Mg2+ to the correct position at the active center in the exonuclease domain Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O59610
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn the functional motif, K253xRxxxD259 (outside known motifs Exo I, II, and III), that is important not only for exonuclease activity but also for polymerizing activity, confirms functional interdependence between the polymerase and exonuclease domains. The short loop region, K253G254R255, probably contributes to binding to DNA substrates Pyrococcus horikoshii diphosphate + DNAn+1
-
?

Synonyms

Synonyms Comment Organism
DNA polymerase I
-
Pyrococcus horikoshii