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Literature summary for 5.6.2.4 extracted from

  • Moreau, M.J.; McGeoch, A.T.; Lowe, A.R.; Itzhaki, L.S.; Bell, S.D.
    ATPase site architecture and helicase mechanism of an archaeal MCM (2007), Mol. Cell., 28, 304-314.
    View publication on PubMed
Search for more literature for 5.6.2.4

Protein Variants

Protein Variants Comment Organism
D488A mutant has an apparent increase in helicase activity but a reduction in ATPase activity to approximately one third of wild-type levels. This mutant has a gel filtration profile compatible with a dimer or trimer. All other proteins appear hexameric Saccharolobus solfataricus
K366E severely compromised helicase activity but only a modest reduction in ATPase activity Saccharolobus solfataricus
additional information the enzyme can tolerate catalytically inactive subunits and still function as a helicase. A mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity Saccharolobus solfataricus
R359A severely compromised helicase activity but only a modest reduction in ATPase activity Saccharolobus solfataricus
T374A reduced but detectable helicase activity with an increase in ATPase activity Saccharolobus solfataricus

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q9UXG1
-
-
Saccharolobus solfataricus P2 Q9UXG1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O the enzyme can tolerate catalytically inactive subunits and still function as a helicase. The mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity Saccharolobus solfataricus ADP + phosphate
-
 ?
ATP + H2O the enzyme can tolerate catalytically inactive subunits and still function as a helicase. The mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity Saccharolobus solfataricus P2 ADP + phosphate
-
 ?

Subunits

Subunits Comment Organism
homohexamer the enzyme can tolerate catalytically inactive subunits and still function as a helicase. A mode of intersubunit communication within mini-chromosome maintenance complex supports a semisequential model for harnessing the energy of ATP binding, hydrolysis, and release in the generation of helicase activity Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
mini-chromosome maintenance complex
-
 Saccharolobus solfataricus
SsoMCM
-
 Saccharolobus solfataricus