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Literature summary for 7.2.2.12 extracted from

  • Okkeri, J.; Haltia, R.
    Expression and mutagenesis of ZntA, a zinc-transporting P-type ATPase from Escherichia coli (1999), Biochemistry, 38, 14109-14116.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E470A metal ion-stimulated activity is reduced, about 30-40%. Mutant is phosphorylated more strongly in comparison to the wild type enzyme Escherichia coli
H475Q metal ion-stimulated activity is reduced, about 30-40%. Mutant is phosphorylated more weakly in comparison to the wild type enzyme. Mutation affects the reaction with ATP and phosphate and stabilizes the enzyme in a dephosphorylated state Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ prevents Zn2+ activation when present in 2fold excess over Zn2+ Escherichia coli
vanadate
-
Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Escherichia coli 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ag+ activates ATPase activity Escherichia coli
Cu2+ enhances phosphorylation, it cannot activate the ATPase Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
92000
-
1 * 92000, also detection of a dimeric form of 190000 Da, SDS-PAGE Escherichia coli
92000
-
2 * 92000, also detection of a monomeric form of 92000 Da, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Ag+/in
-
Escherichia coli ADP + phosphate + Ag+/out
-
?
ATP + H2O + Cd2+/in
-
Escherichia coli ADP + phosphate + Cd2+/out
-
?
ATP + H2O + Pb2+/in
-
Escherichia coli ADP + phosphate + Pb2+/out
-
?
ATP + H2O + Zn2+/in
-
Escherichia coli ADP + phosphate + Zn2+/out
-
?

Subunits

Subunits Comment Organism
dimer 2 * 92000, also detection of a monomeric form of 92000 Da, SDS-PAGE Escherichia coli
monomer 1 * 92000, also detection of a dimeric form of 190000 Da, SDS-PAGE Escherichia coli
More
-
Escherichia coli