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

BRENDA support

Literature summary for 7.2.2.8 extracted from

  • Drees, S.L.; Beyer, D.F.; Lenders-Lomscher, C.; Luebben, M.
    Distinct functions of serial metal-binding domains in the Escherichia coli P1B-ATPase CopA (2015), Mol. Microbiol., 97, 423-438.
    View publication on PubMed
Search for more literature for 7.2.2.8

Activating Compound

Activating Compound Comment Organism Structure
additional information metal-binding domain copper-loaded MBD1 serves CopA in a chaperone-like fashion, copper-loaded metal-binding domain MBD2 shows negligible stimulation Escherichia coli

Protein Variants

Protein Variants Comment Organism
C14S/C17S site-directed mutagenesis, a dysfunctional non-copper-binding mutant Escherichia coli
additional information construction of several truncation mutants of the metal-binding domains of CopA enzyme. Complementation of copA-deficient Escherichia coli strain DC194 by homologous expression of the wild-type and mutant enzymes to different extents and growth monitoring in copper-supplemented media, overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli A0A061K6S9 gene copA
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 ATPase hydrolysis rates of purified and reconstituted wild-type CopA and enzyme truncation mutants Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Cu+[side 1]
-
 Escherichia coli ADP + phosphate + Cu+[side 2]
-
 ?
additional information intramolecular copper transfer within CopA metal-binding domains, quantitative analysis via analytical gel filtration, overview Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
CopA
-
 Escherichia coli
copper export ATPase
-
 Escherichia coli
P1B-ATPase
-
 Escherichia coli

General Information

General Information Comment Organism
evolution the enzme belongs to the superfamily of P-type ATPases, which are capable of exporting transition metal ions at the expense of ATP hydrolysis. P1BATPases share a conserved structure of three cytoplasmic domains linked by a transmembrane domain. In addition, they possess a unique class of domains located at the N-terminus. P1B-ATPases show general functional divergence of tandem metal-binding domains, which is governed by the length of the inter-domain linker Escherichia coli
additional information roles of the two adjacent metal-binding domains of CopA: the distal N-terminal metal-binding domain possesses a function analogous to the metallochaperones of related prokaryotic copper resistance systems, that is its involvement in the copper transfer to the membrane integral ion-binding sites of CopA. In contrast, the proximal domain metal-binding domain has a regulatory role by suppressing the catalytic activity of CopA in absence of copper Escherichia coli
physiological function P1B-ATPases are among the most common resistance factors to metal-induced stress, they are capable of exporting transition metal ions at the expense of ATP hydrolysis. Copper binding to metal-binding domains appears non-essential, because no loss of function is observed when the ligand CxxC motifs are omitted Escherichia coli