Literature summary for 2.7.11.20 extracted from

Tavares, C.D.; OBrien, J.P.; Abramczyk, O.; Devkota, A.K.; Shores, K.S.; Ferguson, S.B.; Kaoud, T.S.; Warthaka, M.; Marshall, K.D.; Keller, K.M.; Zhang, Y.; Brodbelt, J.S.; Ozpolat, B.; Dalby, K.N.
Calcium/calmodulin stimulates the autophosphorylation of elongation factor 2 kinase on Thr-348 and Ser-500 to regulate its activity and calcium dependence (2012), Biochemistry, 51, 2232-2245.

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Activating Compound

Activating Compound	Comment	Organism	Structure
Calmodulin	Ca2+/calmodulin stimulates the autophosphorylation of elongation factor 2 kinase on Thr348 and Ser500 to regulate its activity and calcium dependence. At a calmodulin concentration of 0.002 mM, the enzyme exhibits significant activity	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
S445A	no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate	Homo sapiens
S445D	no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate	Homo sapiens
S474A	no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate	Homo sapiens
S474D	no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate	Homo sapiens
S500A	no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate	Homo sapiens
S500D	no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate. The mutation renders the enzyme Ca2+-independent	Homo sapiens
T348A	about 95% loss of the kinase activity	Homo sapiens
T348D	about 93% loss of the kinase activity	Homo sapiens
T353A	no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate	Homo sapiens
T353D	no difference in activity compared to wild-type enzyme with respect to the ability to phosphorylate a peptide substrate	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	Ca2+/calmodulin stimulates the autophosphorylation of elongation factor 2 kinase on Thr348 and Ser500 to regulate its activity and calcium dependence. Half-maximal activity at 140 nM Ca2+. Maximal activity 0.003 mM Ca2+	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O00418	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	upon incubation with Ca2+ and calmodulin, the enzyme undergoes rapid autophosphorylation. Identification of five major autophosphorylation sites: Thr348, Thr353, Ser445, Ser474, and Ser500. Phosphorylation of Thr348 is required for substrate phosphorylation, but not selfphosphorylation	Homo sapiens

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + acetyl-RKKYKFNEDTERRRFL-amide	-	Homo sapiens	ADP + acetyl-RKKYKFNED(phospho)TERRRFL-amide	-	?
ATP + [elongation factor 2]	-	Homo sapiens	ADP + [elongation factor 2] phosphate	-	?

Synonyms

Synonyms	Comment	Organism
EEF-2K	-	Homo sapiens

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
7.5	-	assay at	Homo sapiens

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Release 2023.1 (January 2023)