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Literature summary for 5.6.1.8 extracted from

  • Heissler, S.M.; Liu, X.; Korn, E.D.; Sellers, J.R.
    Kinetic characterization of the ATPase and actin-activated ATPase activities of Acanthamoeba castellanii myosin-2 (2013), J. Biol. Chem., 288, 26709-26720.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.8

Activating Compound

Activating Compound Comment Organism Structure
F-actin efficiently activates the steady-state ATPase activity of wild-type enzyme about 94fold from a basal value Acanthamoeba castellanii

Protein Variants

Protein Variants Comment Organism
S639D site-directed mutagenesis, a phosphomimetic mutation that affects the processive behavior of myosin-2 filaments Acanthamoeba castellanii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics measurement by stopped-flow assays, steady-state ATPase activity, and kinetc analysis using wild-type and mutant enzymes, overview Acanthamoeba castellanii
0.428
-
 ATP wild-type S1 fragment, pH 7.0, 30°C, in presence of F-actin Acanthamoeba castellanii

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Acanthamoeba castellanii

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 P05659
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation of Ser-639 in loop-2 of myosin-2 affects the processive behavior of myosin-2 filaments Acanthamoeba castellanii

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + myosin bound to actin filament at position n = ADP + phosphate + myosin bound to actin filament at position n+1 the actin-activated release of inorganic phosphate from the acto myosin-ADP-phosphate complex is the rate-limiting step in the steady-state actomyosin ATPase cycle Acanthamoeba castellanii
a

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
-
 ?

Synonyms

Synonyms Comment Organism
myosin-2
-
 Acanthamoeba castellanii

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.77
-
 ATP mutant S639D, pH 7.0, 30°C, in presence of F-actin Acanthamoeba castellanii
1.85
-
 ATP wild-type S1 fragment, pH 7.0, 30°C, in presence of F-actin Acanthamoeba castellanii
4.68
-
 ATP wild-type S1 fragment, pH 7.0, 30°C, hyperbolic fit Acanthamoeba castellanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Acanthamoeba castellanii

Expression

Organism Comment Expression
Acanthamoeba castellanii phosphorylation of Ser639 in loop-2 of the catalytic motor domain of the heavy chain of Acanthamoeba castellanii myosin-2 and the phosphomimetic mutation S639D downregulate the actin-activated ATPase activity of both the full-length myosin and single-headed subfragment-1 down

General Information

General Information Comment Organism
additional information loop-2 of the catalytic motor domain of the heavy chain of Acanthamoeba castellanii myosin-2 Acanthamoeba castellanii