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

BRENDA support

Literature summary extracted from

  • Wijekoon, C.J.; Udagedara, S.R.; Knorr, R.L.; Dimova, R.; Wedd, A.G.; Xiao, Z.
    Copper ATPase CopA from Escherichia coli quantitative correlation between ATPase activity and vectorial copper transport (2017), J. Am. Chem. Soc., 139, 4266-4269 .
    View publication on PubMed

Cloned(Commentary)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.2.2.8 vanadate 0.2 mM, complete inhibition. Vanadate binds irreversibly to the P-domain phosphorylation site Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.2.2.8 membrane inner membrane Escherichia coli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.2.8 copper enzyme binds Cu(I) witrh subfemtomolar affinity Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.8 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.8 ATP + H2O + Cu+[side 1]
-
Escherichia coli ADP + phosphate + Cu+[side 2]
-
?
7.2.2.8 additional information in giant unilamellar vesicles, no Cu leakage or passive diffusion is found. The observed Cu uptake relies completely on active transportation Escherichia coli ?
-
?

Subunits

EC Number Subunits Comment Organism
7.2.2.8 ? x * 87900, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
7.2.2.8 CopA
-
Escherichia coli