Literature summary for 5.6.1.8 extracted from

Lynch, T.J.; Albanesi, J.P.; Korn, E.D.; Robinson, E.A.; Bowerst, B.; Fujisaki, H.
ATPase activities and actin-binding properties of subfragments of Acanthamoeba myosin IA (1986), J. Biol. Chem., 261, 17156-17162.

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Activating Compound

Activating Compound	Comment	Organism	Structure
actin	-	Acanthamoeba castellanii

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

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	Acanthamoeba castellanii	-	ADP + phosphate + myosin bound to actin filament at position n+1	-	?

Organism

Organism	UniProt	Comment	Textmining
Acanthamoeba castellanii	-	ATPase activity of myosin I is stimulated 30 - 40fold by F-actin, when a single serine residue of its heavy chain is phosphorylated	-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
17	-	ATP	myosin IA, 100-kDa fragment resulting from digestion of myosin heavy chain with alpha-chymotrypsin shows similar activity	Acanthamoeba castellanii

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Release 2023.1 (January 2023)