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Literature summary for 5.6.1.3 extracted from

  • Farrell, C.M.; Mackey, A.T.; Klumpp, L.M.; Gilbert, S.P.
    The role of ATP hydrolysis for kinesin processivity (2002), J. Biol. Chem., 277, 17079-17087.
    View publication on PubMed
Search for more literature for 5.6.1.3

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
R210A approx. 0.6% of wild-type kcat, ATP binding is comparable with wild-type Drosophila melanogaster

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.12
-
 ATP 22-25°C, pH 7.2 Drosophila melanogaster

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + a kinesin associated with a microtubule at position n Drosophila melanogaster
-
 ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
 ?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a kinesin associated with a microtubule at position n
-
 Drosophila melanogaster ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
20 25 ATP 22-25°C, pH 7.2, kinesin-microtubules complex Drosophila melanogaster