Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.6.1.3 expression in Escherichia coli Drosophila melanogaster

Protein Variants

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.6.1.3 0.12
-
ATP 22-25°C, pH 7.2 Drosophila melanogaster

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.6.1.3 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

EC Number Organism UniProt Comment Textmining
5.6.1.3 Drosophila melanogaster
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.1.3 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]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.6.1.3 20 25 ATP 22-25°C, pH 7.2, kinesin-microtubules complex Drosophila melanogaster