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Literature summary for 5.6.1.2 extracted from

  • Kon, T.; Nishiura, M.; Ohkura, R.; Toyoshima, Y.Y.; Sutoh, K.
    Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein (2004), Biochemistry, 43, 11266-11274.
    View publication on PubMed
Search for more literature for 5.6.1.2

Cloned(Commentary)

Cloned (Comment) Organism
dynein motor domains in which mutations are introduced to block nucleotide binding at each of the fourATPase associated modules Dictyostelium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information KM-values for dynein motor domains in which mutations are introduced to block nucleotide binding at each of the four ATPase associated modules Dictyostelium sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Dictyostelium sp. 5737
-

Organism

Organism UniProt Comment Textmining
Dictyostelium sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
dynein motor domains in which mutations are introduced to block nucleotide binding at each of the fourATPase associated modules Dictyostelium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a dynein associated with a microtubule at position n ATP binding and its hydrolysis only at P1 site (nucleotide-binding/hydrolysis site) are essential for the motor activities of the cytoplasmic dynein and suggests that the other nucleotide-binding/hydrolysis sites regulate the motor activities. Among them, nucleotide binding at the P3 site is not essential but is critical for microtubule-activated ATPase and motile activities of cytoplasmic dynein Dictyostelium sp. ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
 ?

Synonyms

Synonyms Comment Organism
dynein
-
 Dictyostelium sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information kcat for dynein motor domains in which mutations are introduced to block nucleotide binding at each of the four ATPase associated modules Dictyostelium sp.