Literature summary for 7.2.2.8 extracted from

Hatori, Y.; Hirata, A.; Toyoshima, C.; Lewis, D.; Pilankatta, R.; Inesi, G.
Intermediate phosphorylation reactions in the mechanism of ATP utilization by the copper ATPase (CopA) of Thermotoga maritima (2008), J. Biol. Chem., 283, 22541-22549.

Search for more literature for 7.2.2.8

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Thermotoga maritima

Protein Variants

Protein Variants	Comment	Organism
H479Q	the mutant is unable to utilize ATP, whereas phosphorylation by phosphate is retained	Thermotoga maritima

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu+	Cu+ binding to the N-metal binding domain is required to produce an active conformation of the enzyme, whereby additional Cu+ bound to an alternate (transmembrane transport) site initiates faster cycles	Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + Cu+[side 1]	Thermotoga maritima	-	ADP + phosphate + Cu+[side 2]	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	-	Thermotoga maritima

Purification (Commentary)

Purification (Comment)	Organism
-	Thermotoga maritima

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + Cu+[side 1]	-	Thermotoga maritima	ADP + phosphate + Cu+[side 2]	-	?

Synonyms

Synonyms	Comment	Organism
CopA	-	Thermotoga maritima
copper ATPase	-	Thermotoga maritima

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
60	-	-	Thermotoga maritima

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	-	-	Thermotoga maritima

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Release 2023.1 (January 2023)