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

BRENDA support

Literature summary for 7.2.2.12 extracted from

  • Okkeri, J.; Haltia, T.
    The metal-binding sites of the zinc-transporting P-type ATPase of Escherichia coli. Lys693 and Asp714 in the seventh and eighth transmembrane segments of ZntA contribute to the coupling of metal binding and ATPase activity (2006), Biochim. Biophys. Acta, 1757, 1485-1495.
    View publication on PubMed
Search for more literature for 7.2.2.12

Cloned(Commentary)

Cloned (Comment) Organism
into the pTRCHisA vector for expression in the Escherichia coli TOP 10 strain Escherichia coli

Protein Variants

Protein Variants Comment Organism
D714M significant metal-independent ATPase activity, poor phosphorylation by ATP and Pi Escherichia coli
K693N very low activity, no Cu2+-dependent phosphorylation with ATP, hyperphosphorylation by Pi, altered metal sensitivity of phosphorylation by Pi Escherichia coli
K693N/D714M very low activity and phosphorylation with ATP, almost normal phosphorylation with Pi, altered metal senstivity of Pi phosphorylation Escherichia coli
SAAS mutation of two the two cysteines to serines in the CAAC motif near the N-terminus, ATPase activity 50%, diminished phosphorylation, faster dephosphorylation Escherichia coli
SPS mutation of two the two cysteines to serines in the CPC motif in transmembrane helix 6, inactive, very low phosphorylation Escherichia coli

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 on PAA gels the protein is present in three forms, as a monomer with an apparent mass of 92 kDa, as a dimer of 190 kDa and as a proteolytic fragment of 67 kDa Escherichia coli
80000
-
 monomer, determined by SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
the membrane fractions of the cells are isolated Escherichia coli

Storage Stability

Storage Stability Organism
-70°C, 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 20% glycerol, 2 mM beta-mercaptoethanol, 0.5 mM PMSF Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 on PAA gels the protein is present in three forms, as a monomer with an apparent mass of 92 kDa, as a dimer of 190 kDa and as a proteolytic fragment of 67 kDa Escherichia coli
monomer on PAA gels the protein is present in three forms, as a monomer with an apparent mass of 92 kDa, as a dimer of 190 kDa and as a proteolytic fragment of 67 kDa Escherichia coli

Synonyms

Synonyms Comment Organism
zinc-transporting P-type ATPase
-
 Escherichia coli
Zn2+ -exporting ATPase
-
 Escherichia coli
ZntA
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
-
 phosphorylation assays are carried out on ice and room temperature Escherichia coli
37
-
 ATPase activity assay Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 ATPase activity assay Escherichia coli