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Literature summary extracted from

  • Brzeska, H.; Martin, B.M.; Korn, E.D.
    The catalytic domain of Acanthamoeba myosin I heavy chain kinase. I. Identification and characterization following tryptic cleavage of the native enzyme (1996), J. Biol. Chem., 271, 27049-27055.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.7 acidic phospholipids enhance the activation of the enzyme by autophosphorylation Acanthamoeba castellanii
2.7.11.7 additional information enzyme is stimulated by its autophosphorylation Acanthamoeba castellanii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.7 Mg2+
-
 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
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.7 ATP + GRGRSSVYS
-
 Acanthamoeba castellanii ADP + GRGRSS(-phosphate)VYS
-
 ?
2.7.11.7 ATP + myosin heavy chain kinase 35 kDa trypsin fragment of the C-terminus of the maximally activated, phosphorylated enzyme is fully catalytically active and contains 2 thirds of the autophosphorylation sites of the native enzyme Acanthamoeba castellanii ADP + myosin heavy chain kinase phosphate
-
 ?
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 35 kDa trypsin fragment of the C-terminus of the maximally activated, phosphorylated enzyme is fully catalytically active and contains 2 thirds of the autophosphorylation sites of the native enzyme Acanthamoeba castellanii ADP + myosin I heavy chain phosphate
-
 ?
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 ?
-
 ?
2.7.11.7 additional information localization of autophosphorylation sites Acanthamoeba castellanii ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.7 MIHC kinase
-
 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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.7 7.5
-
 assay at Acanthamoeba castellanii

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.7 ATP
-
 Acanthamoeba castellanii