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Literature summary extracted from

  • Hackney, D.D.; Baek, N.; Snyder, A.C.
    Half-site inhibition of dimeric kinesin head domains by monomeric tail domains (2009), Biochemistry, 48, 3448-3456.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.6.1.3 additional information Drosophila melanogaster the binding of tail peptides to head dimers is fast and readily reversible, the second tail peptide in a folded kinesin-1 may be available to bind other molecules while kinesin-1 remains folded ?
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
5.6.1.3 Ni-NTA column chromatography 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)
-
 ?
5.6.1.3 additional information the binding of tail peptides to head dimers is fast and readily reversible, the second tail peptide in a folded kinesin-1 may be available to bind other molecules while kinesin-1 remains folded Drosophila melanogaster ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.6.1.3 dimer
-
 Drosophila melanogaster

Synonyms

EC Number Synonyms Comment Organism
5.6.1.3 kinesin
-
 Drosophila melanogaster
5.6.1.3 kinesin-1
-
 Drosophila melanogaster