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Literature summary for 2.7.7.7 extracted from

  • Pisani, F.M., Rossi M.
    Evidence that an archaeal alpha-like DNA polymerase has a modular organization of its associated catalytic activities (1994), J. Biol. Chem., 269, 7887-7992.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Mg2+-dependent DNA-polymerizing activity Saccharolobus solfataricus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
-
1 * 100000, likely it is cleaved by the action of endogenous proteases during the purification procedure. As a consequence of that, two proteolytic fragments of about 50 and 40 kDa, in addition to the intact 100-kDa molecular species, can be detected upon SDS-PAGE Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn bifunctional enzyme EC 2.7.7.7/EC 3.1.11.2. The polymerization and the 3'-5' exonuclease activity of a family B DNA polymerase can be ascribed to physically distinct modules of the enzyme molecule Saccharolobus solfataricus diphosphate + DNAn+1
-
?

Subunits

Subunits Comment Organism
monomer 1 * 100000, likely it is cleaved by the action of endogenous proteases during the purification procedure. As a consequence of that, two proteolytic fragments of about 50 and 40 kDa, in addition to the intact 100-kDa molecular species, can be detected upon SDS-PAGE Saccharolobus solfataricus