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Literature summary extracted from

  • Tadini-Buoninsegni, F.; Bartolommei, G.; Moncelli, M.R.; Pilankatta, R.; Lewis, D.; Inesi, G.
    ATP dependent charge movement in ATP7B Cu+-ATPase is demonstrated by pre-steady state electrical measurements (2010), FEBS Lett., 584, 4619-4622.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.2.8 Recombinant adenovirus vector, rAdATP7Bmyc, containing CMV promoter driven WT human ATP7B cDNA, fused with 30 cmyc tag, expression in COS-1 cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
7.2.2.8 C575A/C578A mutation in the 6th copper site of the NMBD, catalytically inactive, no phosphoenzyme intermediate formed upon addition of ATP Homo sapiens
7.2.2.8 C983A/C985A mutation in the transmembrane copper binding site, TMBS, catalytically inactive, no phosphoenzyme intermediate formed upon addition of ATP Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.8 Homo sapiens
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-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.8 additional information detection of a positive charge displacement within a single catalytic cycle of ATP7B upon addition of ATP and formation of phosphoenzyme intermediate, C983A/C985A and C575A/C578A mutants demonstrate that ATP7B activation requires a copper binding site in the N-terminus extension Homo sapiens ?
-
?

Synonyms

EC Number Synonyms Comment Organism
7.2.2.8 ATP7B
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Homo sapiens

General Information

EC Number General Information Comment Organism
7.2.2.8 physiological function ATP7B is a copper dependent P-type ATPase, required for copper homeostasis Homo sapiens