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Literature summary for 7.2.2.9 extracted from

  • Catty, P.; Boutigny, S.; Miras, R.; Joyard, J.; Rolland, N.; Seigneurin-Berny, D.
    Biochemical characterization of AtHMA6/PAA1, a chloroplast envelope Cu(I)-ATPase (2011), J. Biol. Chem., 286, 36188-36197.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Lactococcus lactis Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
D598A inactive Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast envelope inner membrane of the chloroplast envelope Arabidopsis thaliana 9941
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ag+ the enzyme is activated by silver ions with an apparent affinity in the micromolar range (40% activation at 0.005 mM compared to Cu+) Arabidopsis thaliana
Cu+ the enzyme is preferentially activated by monovalent copper ions with an apparent affinity in the micromolar range (100% activation at 0.005 mM) Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9SZC9
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein PAA1 is phosphorylated from ATP in the presence of monovalent metals (only CuCl2 and AgNO3). The presence of EGTA does not affect the phosphorylation levels Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Cu+/in
-
Arabidopsis thaliana ADP + phosphate + Cu+/out
-
?

Synonyms

Synonyms Comment Organism
copper-transporting ATPase
-
Arabidopsis thaliana
Cu(I)-ATPase
-
Arabidopsis thaliana
PAA1
-
Arabidopsis thaliana

General Information

General Information Comment Organism
physiological function PAA1 is a high affinity Cu(I) transporter of the chloroplast envelope. The sensitivity to copper and silver correlates with the presence of a functional enzyme Arabidopsis thaliana