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Literature summary for 7.2.2.8 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
Search for more literature for 7.2.2.8

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Archaeoglobus fulgidus

Protein Variants

Protein Variants Comment Organism
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
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
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
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]

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

Natural Substrates/ Products (Substrates)

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

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] 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]
-
 ?
ATP + H2O + Cu+[side 1]
-
 Archaeoglobus fulgidus ADP + phosphate + Cu+[side 2]
-
 ?
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

Synonyms Comment Organism
CopA
-
 Archaeoglobus fulgidus

Temperature Optimum [°C]

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

pH Optimum

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