Literature summary for 2.7.11.20 extracted from

Pigott, C.R.; Mikolajek, H.; Moore, C.E.; Finn, S.J.; Phippen, C.W.; Werner, J.M.; Proud, C.G.
Insights into the regulation of eukaryotic elongation factor 2 kinase and the interplay between its domains (2012), Biochem. J., 442, 105-118.

Search for more literature for 2.7.11.20

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C314A	complete loss of activity	Homo sapiens
C318A	complete loss of activity	Homo sapiens
D274A	loss of ability to bind ATP	Homo sapiens
H213A	complete loss of activity	Homo sapiens
H260A	complete loss of activity	Homo sapiens
K170M	complete loss of activity, loss of ability to bind ATP	Homo sapiens
K170R	complete loss of activity, loss of ability to bind ATP	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	Ca2+/calmodulin-dependent enzyme. Ca2+/calmodulin enhance the ability of the enzyme to bind to ATP	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + RKKFGESEKTKTKEFL	-	Homo sapiens	ADP + ?	-	?
ATP + [elongation factor 2]	the calmodulin-binding/alpha-kinase domain of the enzyme itself possesses autokinase activity, but is unable to phosphorylate substrates in trans. The phosphorylation of substrates in trans requires the SEL1-like domains of eEF2K	Homo sapiens	ADP + [elongation factor 2] phosphate	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Homo sapiens

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Release 2023.1 (January 2023)