Literature summary for 7.2.2.8 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.

Search for more literature for 7.2.2.8

Cloned(Commentary)

Cloned (Comment)	Organism
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

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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

Synonyms	Comment	Organism
ATP7B	-	Homo sapiens

General Information

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)