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Literature summary for 7.2.2.9 extracted from

  • Morgan, C.T.; Tsivkovskii, R.; Kosinsky, Y.A.; Efremov, R.G.; Lutsenko, S.
    The distinct functional properties of the nucleotide-binding domain of ATP7B, the human copper-transporting ATPase: analysis of the Wilson disease mutations E1064A, H1069Q, R1151H, and C1104F (2004), J. Biol. Chem., 279, 36363-36371.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli of the N-domain fused with a chitin-binding domain, several N-domain mutants cloned using the same procedure Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for the hydrolysis of ATP, suggesting that MgATP2+ is the substrate Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of fusion protein by chitin affinity chromatography Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + Cu2+[side 1] = ADP + phosphate + Cu2+[side 2] the N-domain can not hydrolyse ATP Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Cu2+/in
-
Homo sapiens ADP + phosphate + Cu2+/out
-
r

Synonyms

Synonyms Comment Organism
Wilson's desease protein
-
Homo sapiens
WNDP
-
Homo sapiens