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Literature summary for 5.6.1.3 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
Search for more literature for 5.6.1.3

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography 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)
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 ?
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

Subunits Comment Organism
dimer
-
 Drosophila melanogaster

Synonyms

Synonyms Comment Organism
kinesin
-
 Drosophila melanogaster
kinesin-1
-
 Drosophila melanogaster