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

BRENDA support

Literature summary for 7.2.2.8 extracted from

  • Mandal, A.K.; Cheung, W.D.; Arguello, J.M.
    Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus (2002), J. Biol. Chem., 277, 7201-7208.
    View publication on PubMed
Search for more literature for 7.2.2.8

Activating Compound

Activating Compound Comment Organism Structure
additional information dithiothreitol is necessary in the medium to maintain the metal in its Cu(I) redox state Archaeoglobus fulgidus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Archaeoglobus fulgidus

Inhibitors

Inhibitors Comment Organism Structure
N-methylglucamine
-
 Archaeoglobus fulgidus
oligomycin
-
 Archaeoglobus fulgidus
vanadate
-
 Archaeoglobus fulgidus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.25
-
 ATP pH 6.1, 75°C, ATPase activity Archaeoglobus fulgidus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information high salt concentration stimulate the ATPase, reaching a plateau at 400–500 mM. This effect appears independent of the cation, since NaCl or KCl yields similar Ag-ATPase stimulation. Experiments using N-methylglucamine to increase ionic strength in the medium could not confirm this point. Although the amine at low concentration (under 10 mM) stimulats the ATPase as NaCl or KCl, it leads to a sharp inactivation at higher concentrations Archaeoglobus fulgidus

Organism

Organism UniProt Comment Textmining
Archaeoglobus fulgidus O29777
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Archaeoglobus fulgidus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Ag+[side 1] the enzyme is activated by Ag+ and to a lesser extent by Cu+. Maximum Cu+-ATPase activity is 25% of that measured in the presence of Ag+. However, Cu+interacts with the enzyme with higher apparent affinity. The activation by Ag+ or Cu+is dependent on the presence of millimolar amounts of cysteine. In the presence of ATP, these metals drive the formation of an acid-stable phosphoenzyme with apparent affinities similar to those observed in the ATPase activity determinations. Comparable levels of phosphoenzyme are reached in the presence of both cations. The stimulation of phosphorylation by the cations suggests that CopA drives the outward movement of the metal Archaeoglobus fulgidus ADP + phosphate + Ag+[side 2]
-
 ?
ATP + H2O + Cu+[side 1] the enzyme is activated by Ag+ and to a lesser extent by Cu+. Maximum Cu+-ATPase activity is 25% of that measured in the presence of Ag+.However, Cu+interacts with the enzyme with higher apparent affinity. The activation by Ag+ or Cu+is dependent on the presence of millimolar amounts of cysteine. In the presence of ATP, these metals drive the formation of an acid-stable phosphoenzyme with apparent affinities similar to those observed in the ATPase activity determinations. Comparable levels of phosphoenzyme are reached in the presence of both cations. The stimulation of phosphorylation by the cations suggests that CopA drives the outward movement of the metal Archaeoglobus fulgidus ADP + phosphate + Cu+[side 2]
-
 ?

Synonyms

Synonyms Comment Organism
Ag+/Cu+-ATPase
-
 Archaeoglobus fulgidus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
75
-
-
 Archaeoglobus fulgidus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
60 80 60°C: about 55% of maximal activity, 80°C: about 75% of maximal activity Archaeoglobus fulgidus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1 6.5
-
 Archaeoglobus fulgidus

pH Range

pH Minimum pH Maximum Comment Organism
6 7 pH 6.0: about 30% of maximal activity, pH 7.0: about 30% of maximal activity Archaeoglobus fulgidus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0047
-
 oligomycin pH 6.1, 75°C Archaeoglobus fulgidus

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.024
-
 pH 6.1, 75°C Archaeoglobus fulgidus vanadate
25
-
 pH 6.1, 75°C Archaeoglobus fulgidus N-methylglucamine