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Literature summary for 2.7.11.24 extracted from

  • Gelmedin, V.; Caballero-Gamiz, R.; Brehm, K.
    Characterization and inhibition of a p38-like mitogen-activated protein kinase (MAPK) from Echinococcus multilocularis: antiparasitic activities of p38 MAPK inhibitors (2008), Biochem. Pharmacol., 76, 1068-1081.
    View publication on PubMed

Application

Application Comment Organism
drug development Echinococcus multilocularis MPK2 is a promising target for the development of drugs against alveolar echinococcosis Echinococcus multilocularis

Cloned(Commentary)

Cloned (Comment) Organism
gene mpk2, DNA and amino acid sequence determination and analysis, sequence comparison, expression of the His-tagged enzyme in Escherichia coli Echinococcus multilocularis
isozyme p38 MAPKalpha, sequence comparison, expression of the His-tagged enzyme in Escherichia coli Echinococcus multilocularis

Inhibitors

Inhibitors Comment Organism Structure
ML3403 an ATP-competitive pyridinyl imidazole inhibitor of p38 MAPK; an ATP-competitive pyridinyl imidazole inhibitor of p38 MAPK, leads to strong dephosphorylation of MPK2 in the parasite and effective killing of parasite vesicles at concentrations that do not affect cultivated mammalian cells; an ATP-competitive pyridinyl imidazole inhibitor of p38 MAPK, leads to strong dephosphorylation of MPK2 in the parasite and effective killing of parasite vesicles at concentrations that do not affect cultivated mammalian cells Echinococcus multilocularis
SB202190 an ATP-competitive pyridinyl imidazole inhibitor of p38 MAPK; an ATP-competitive pyridinyl imidazole inhibitor of p38 MAPK, leads to dephosphorylation of MPK2 in the parasite and effective killing of parasite vesicles at concentrations that do not affect cultivated mammalian cells; an ATP-competitive pyridinyl imidazole inhibitor of p38 MAPK, leads to dephosphorylation of MPK2 in the parasite and effective killing of parasite vesicles at concentrations that do not affect cultivated mammalian cells Echinococcus multilocularis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Echinococcus multilocularis

Organism

Organism UniProt Comment Textmining
Echinococcus multilocularis
-
fox-tapeworm
-
Echinococcus multilocularis B1VK39 MPK2, cDNA; fox-tapeworm, gene mpk2
-
Echinococcus multilocularis B1VK40 MPK2, chromosomal DNA; fox-tapeworm, gene mpk2
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein MPK2 is highly autophosphorylated Echinococcus multilocularis
phosphoprotein p38 MAP kinase is activated by autophosphorylation Echinococcus multilocularis

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by affinity chromatography Echinococcus multilocularis

Source Tissue

Source Tissue Comment Organism Textmining
cell culture primary cell culture established from metacestode vesicle Echinococcus multilocularis
-
larva metacestode larval stage, expression analysis of mpk2 Echinococcus multilocularis
-
metacestode
-
Echinococcus multilocularis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + myelin basic protein
-
Echinococcus multilocularis ADP + phosphorylated myelin basic protein
-
?

Synonyms

Synonyms Comment Organism
MAPK
-
Echinococcus multilocularis
More MPK2 is a member of the mitogen-activated protein kinase, MAPK, family Echinococcus multilocularis
More p39 MAPK is a member of the mitogen-activated protein kinase, MAPK, family Echinococcus multilocularis
MPK2
-
Echinococcus multilocularis
p38 MAP kinase
-
Echinococcus multilocularis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Echinococcus multilocularis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Echinococcus multilocularis

Cofactor

Cofactor Comment Organism Structure
ATP
-
Echinococcus multilocularis