Literature summary for 7.2.2.9 extracted from

Voskoboinik, I.; Mar, J.; Strausak, D.; Camakaris, J.
The regulation of catalytic activity of the Menkes copper-translocating P-type ATPase. Role of high affinity copper-binding sites (2001), J. Biol. Chem., 276, 28620-28627.

Search for more literature for 7.2.2.9

Cloned(Commentary)

Cloned (Comment)	Organism
expression of the wild type and mutant proteins in Saccharomyces cerevisiae	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
vanadate	50% inactivation at 0.05 mM	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.017	-	ATP	-	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu2+	activates inducing phosphorylation of the enzyme, inhibition is observed above 0.005 mM	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
isolation of membrane vesicles from yeast expressing recombinant enzyme	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
ATP7A	-	Homo sapiens
Menkes copper-translocating P-type ATPase	-	Homo sapiens
MNK	-	Homo sapiens

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Release 2023.1 (January 2023)