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Literature summary extracted from

  • Cattoni, D.I.; Gonzalez Flecha, F.L.; Argueello, J.M.
    Thermal stability of CopA, a polytopic membrane protein from the hyperthermophile Archaeoglobus fulgidus (2008), Arch. Biochem. Biophys., 471, 198-206.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.2.8 expression in Escherichia coli Archaeoglobus fulgidus

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.8 Archaeoglobus fulgidus O29777
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.2.2.8
-
 Archaeoglobus fulgidus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.8 ATP + H2O + Ag+[side 1] Ag+-ATPase activity is measured as the difference between the activity in the medium with Ag+ and that measured in the same medium without Ag+ Archaeoglobus fulgidus ADP + phosphate + Ag+[side 2]
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
7.2.2.8 66 85 incubation of CopA in the absence of substrates at temperatures in the 66–85°C range leads to an irreversible exponential decrease in enzyme activity suggesting a two-state process involving fully-active and inactive molecules. Although CopA inactivated much slower than mesophilic proteins, the activation energy is similar to that observed for mesophilic P-type ATPases. The inactivation process is found to be associated with the irreversible partial unfolding of the polypeptide chain. However, the inactive thermally denatured protein still conserves large hydrophobic regions and considerable secondary structure Archaeoglobus fulgidus
7.2.2.8 75
-
 complete and irreversible inactivation after 70 min Archaeoglobus fulgidus