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Literature summary extracted from

  • Brzeska, H.; Lynch, T.J.; Martin, B.; Corigliano-Murphy, A.; Korn, E.D.
    Substrate specificity of Acanthamoeba myosin I heavy chain kinase as determined with synthetic peptides (1990), J. Biol. Chem., 265, 16138-16144.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.7 phosphatidylinositol
-
Acanthamoeba castellanii
2.7.11.7 phosphatidylserine stimulation only of the autophosphorylated enzyme Acanthamoeba castellanii
2.7.11.7 Phospholipid vesicles autophosphorylation activity is increased 5-10fold in a Ca2+-independent manner Acanthamoeba castellanii
2.7.11.7 Phospholipid vesicles composed of phosphatidylserine or phosphatidylinositol, not phosphatidylcholine Acanthamoeba castellanii
2.7.11.7 Phospholipid vesicles composed of phosphatidylethanolamine Acanthamoeba castellanii

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.7 Myosin I inhibits autophosphorylation Acanthamoeba castellanii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.11.7 additional information
-
additional information Km values for derivatives of peptide GRGRSSVYS Acanthamoeba castellanii
2.7.11.7 0.05
-
GRGRSSVYS pH 7.0, 30°C Acanthamoeba castellanii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.11.7 ATP + myosin I heavy chain Acanthamoeba castellanii
-
ADP + myosin I heavy chain phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.7 Acanthamoeba castellanii
-
myosin I heavy chain kinase
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.7 cell culture
-
Acanthamoeba castellanii
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.7 ATP + GRGRSSVYS synthetic peptide with a sequence corresponding to the phosphorylation site of myosin IC Acanthamoeba castellanii ADP + GRGRSS(-phosphate)VYS
-
?
2.7.11.7 ATP + myosin I heavy chain
-
Acanthamoeba castellanii ADP + myosin I heavy chain phosphate
-
?
2.7.11.7 ATP + myosin I heavy chain substrate: myosin IB, phosphorylation site is Ser315 Acanthamoeba castellanii ADP + myosin I heavy chain phosphate
-
?
2.7.11.7 ATP + myosin I heavy chain substrate myosin IA: phosphorylation of a single threonine Acanthamoeba castellanii ADP + myosin I heavy chain phosphate
-
?
2.7.11.7 ATP + myosin I heavy chain substrate is heavy chain of myosin IC Acanthamoeba castellanii ADP + myosin I heavy chain phosphate
-
?
2.7.11.7 ATP + myosin I heavy chain myosin I from intestinal brush border Acanthamoeba castellanii ADP + myosin I heavy chain phosphate
-
?
2.7.11.7 ATP + myosin I heavy chain substrate: myosin IC, phosphorylation site is Ser311 Acanthamoeba castellanii ADP + myosin I heavy chain phosphate
-
?
2.7.11.7 ATP + myosin I heavy chain a basic amino acid is essential on amino-terminal side of phosphorylation site, two are preferable, and a Tyr-residue is essential two residues away on the COOH-terminal side Acanthamoeba castellanii ADP + myosin I heavy chain phosphate
-
?
2.7.11.7 ATP + myosin I heavy chain substrates are heavy chains of myosin IA and IB Acanthamoeba castellanii ADP + myosin I heavy chain phosphate
-
?
2.7.11.7 ATP + synthetic peptides variations in length, and number, location and kind of basic residues of the basic sequence of peptide GRGRSSVYS, overview Acanthamoeba castellanii ?
-
?
2.7.11.7 additional information substrate specificity study Acanthamoeba castellanii ?
-
?
2.7.11.7 additional information the Mg2+-ATPase activity of the substrate myosin I is increased by its phosphorylation and the binding of F-actin Acanthamoeba castellanii ?
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.7 30
-
assay at Acanthamoeba castellanii

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.7 ATP
-
Acanthamoeba castellanii