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Literature summary for 5.6.1.8 extracted from

  • Yamada, A.; Yoshio, M.; Oiwa, K.
    Myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro (2013), J. Muscle Res. Cell Motil., 34, 115-123.
    View publication on PubMed
Search for more literature for 5.6.1.8

Activating Compound

Activating Compound Comment Organism Structure
F-actin myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro. At low Ca2+ concentration, Mg-ATPase is activated by F-actin only in the presence of dephosphorylated twitchin, a titin/connectinrelated giant protein, regulates interactions between actin and myosin filaments at low Ca2+ concentrations. When it is dephosphorylated, actin filaments tightly bind to myosin filaments, resulting in the catch state known as the state of high passive tension with very low energy consumption. In the absence of twitchin, F-actin does not bind to myosin filaments Mytilus galloprovincialis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state Mg-ATPase activities of purified myosin, overview Mytilus galloprovincialis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates the Mg-ATPase activity of myosin Mytilus galloprovincialis
Mg2+ required Mytilus galloprovincialis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + myosin bound to actin filament at position n Mytilus galloprovincialis
-
 ADP + phosphate + myosin bound to actin filament at position n+1
-
 ?

Organism

Organism UniProt Comment Textmining
Mytilus galloprovincialis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native myosin from smooth adductor muscle Mytilus galloprovincialis

Source Tissue

Source Tissue Comment Organism Textmining
smooth adductor muscle
-
 Mytilus galloprovincialis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + myosin bound to actin filament at position n
-
 Mytilus galloprovincialis ADP + phosphate + myosin bound to actin filament at position n+1
-
 ?

Synonyms

Synonyms Comment Organism
myosin Mg-ATPase
-
 Mytilus galloprovincialis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Mytilus galloprovincialis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Mytilus galloprovincialis

General Information

General Information Comment Organism
physiological function myosin Mg-ATPase of molluscan muscles is slightly activated by F-actin under catch state in vitro. At low Ca2+ concentration, Mg-ATPase is activated by F-actin only in the presence of dephosphorylated twitchin, a titin/connectinrelated giant protein, regulates interactions between actin and myosin filaments at low Ca2+ concentrations. When it is dephosphorylated, actin filaments tightly bind to myosin filaments, resulting in the catch state known as the state of high passive tension with very low energy consumption. When twitchin is phosphorylated actin filaments detach from the myosin filaments, resulting in relaxation of the catch. In the absence of F-actin, twitchin and its phosphorylation state do not affect Mg-ATPase activities in any of the conditions tested. Determination of a molecular mechanism for the catch, where twitchin alone does not interact with the myosin catalytic motor domain but its complex with F-actin does, forming the bridge between actin and myosin filaments and the myosin slowly hydrolyzes Mg-ATP in the catch state. Regulation mechanism, overview Mytilus galloprovincialis