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

BRENDA support

Literature summary extracted from

  • Mandal, A.K.; Argueello, J.M.
    Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu(+)-ATPase CopA (2003), Biochemistry, 42, 11040-11047.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
7.2.2.8 C27A/C30A replacement of Cys in the N-terminal metal binding domain, mutation leads to about 40% reduction in Ag+ activated ATPase activity and about 60% reduction in Cu+-activated ATPase activity. The mutant enzyme binds Cu+, Ag+, and ATP with the same high apparent affinities as the wild-type enzyme. Evidence that the N-terminal metal binding domain disruption has no effect on the E1-E2 equilibrium is provided by the normal interaction of ATP acting with low affinity and the unaffected IC50 for vanadate inhibition observed in the C27A/C30A-substituted enzyme Archaeoglobus fulgidus
7.2.2.8 C27A/C30A/C751A/C754A mutation leads to about 40% reduction in Ag+ activated ATPase activity and about 60% reduction in Cu+-activated ATPase activity Archaeoglobus fulgidus
7.2.2.8 C380A/C382A the mutant enzyme binds ATP, indicating its correct folding and suggesting that enzyme turnover is prevented by the lack of metal binding to the transmembrane site Archaeoglobus fulgidus
7.2.2.8 C751A/C754A the mutant enzyme has no significant effect on ATPase activity, enzyme phosphorylation, apparent binding affinities of ligands, or E1-E2 equilibrium Archaeoglobus fulgidus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.2.2.8 0.22
-
 ATP pH 7.5, 20°C, C27A/C30A mutant enzyme Archaeoglobus fulgidus
7.2.2.8 0.27
-
 ATP pH 7.5, 20°C, wild-type enzyme Archaeoglobus fulgidus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.2.2.8 ATP + H2O + Cu+[side 1] Archaeoglobus fulgidus
-
 ADP + phosphate + Cu+[side 2]
-
 ?

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] although the enzyme binds Cu+ with 15 times higher apparent affinity, Ag+ drives a faster turnover because the enzyme(Ag) form undergoes a faster dephosphorylation than the enzyme(Cu) form Archaeoglobus fulgidus ADP + phosphate + Ag+[side 2]
-
 ?
7.2.2.8 ATP + H2O + Cu+[side 1]
-
 Archaeoglobus fulgidus ADP + phosphate + Cu+[side 2]
-
 ?
7.2.2.8 ATP + H2O + Cu+[side 1] although the enzyme binds Cu+ with 15 times higher apparent affinity, Ag+ drives a faster turnover because theenzyme(Ag) form undergoes a faster dephosphorylation than the enzyme(Cu) form Archaeoglobus fulgidus ADP + phosphate + Cu+[side 2]
-
 ?

Synonyms

EC Number Synonyms Comment Organism
7.2.2.8 CopA
-
 Archaeoglobus fulgidus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7.2.2.8 20
-
 assay at Archaeoglobus fulgidus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2.2.8 7.5
-
 assay at Archaeoglobus fulgidus