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Literature summary for 2.7.11.20 extracted from

  • Hong-Brown, L.Q.; Brown, C.R.; Huber, D.S.; Lang, C.H.
    Lopinavir impairs protein synthesis and induces eEF2 phosphorylation via the activation of AMP-activated protein kinase (2008), J. Cell. Biochem., 105, 814-823.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Calmodulin required Mus musculus
additional information inhibition of eEF2 phosphorylation leads to increased activity of its upstream regulators AMP-activated protein kinase and eEF2 kinase, overview Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
compound C AMPK inhibitor compound C blocks eEF2K and eEF2 phosphorylation Mus musculus
lopinavir i.e. LPV, increases the phosphorylation of eEF2 kinase on Ser366 reducing its activity, LPV affects eEF2 activity via an AMPK-eEF2K dependent pathway, overview Mus musculus
additional information rottlerin suppresses eEF2K, but not eEF2 phosphorylation in myocytes Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Mus musculus
Mg2+ required Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [eukaryotic translation elongation factor 2] Mus musculus inhibition of eEF2 phosphorylation leads to increased activity of its upstream regulators AMP-activated protein kinase, AMPK, and eEF2 kinase, eEF2K, regulation, overview ADP + [eukaryotic translation elongation factor 2] phosphate
-
?
additional information Mus musculus rottlerin suppresses eEF2K, but not eEF2 phosphorylation in myocytes ?
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation of eEF2K can either inhibit or enhance the activity of its downstream substrate, depending on the site of phosphorylation and the type of stimul, lopinavir increases the phosphorylation of eEF2 kinase on Ser366 reducing its activity, LPV affects eEF2 activity via an AMPK-eEF2K dependent pathway, overview Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
C2C12 cell murine myoblasts Mus musculus
-
myocyte
-
Mus musculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [eukaryotic translation elongation factor 2] inhibition of eEF2 phosphorylation leads to increased activity of its upstream regulators AMP-activated protein kinase, AMPK, and eEF2 kinase, eEF2K, regulation, overview Mus musculus ADP + [eukaryotic translation elongation factor 2] phosphate
-
?
ATP + [eukaryotic translation elongation factor 2] i.e. eEF2, both AMP-activated protein kinase, AMPK, and eEF2 kinase, eEF2K, phosphorylate eEF2, thus two distinct paths lead to eEF2 phosphorylation, overview Mus musculus ADP + [eukaryotic translation elongation factor 2] phosphate
-
?
additional information rottlerin suppresses eEF2K, but not eEF2 phosphorylation in myocytes Mus musculus ?
-
?

Synonyms

Synonyms Comment Organism
eEF2 kinase
-
Mus musculus
eEF2K
-
Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Mus musculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Mus musculus