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Literature summary for 2.7.11.7 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
Search for more literature for 2.7.11.7

Activating Compound

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Acanthamoeba castellanii

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + GRGRSSVYS
-
 Acanthamoeba castellanii ADP + GRGRSS(-phosphate)VYS
-
 ?
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
-
 ?
ATP + myosin I heavy chain
-
 Acanthamoeba castellanii ADP + myosin I heavy chain phosphate
-
 ?
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
-
 ?
additional information the Mg2+-ATPase activity of the substrate myosin I is increased by its phosphorylation and the binding of F-actin Acanthamoeba castellanii ?
-
 ?
additional information localization of autophosphorylation sites Acanthamoeba castellanii ?
-
 ?

Synonyms

Synonyms Comment Organism
MIHC kinase
-
 Acanthamoeba castellanii

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Acanthamoeba castellanii