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Literature summary extracted from

  • Thoresen, T.; Gelles, J.
    Processive movement by a kinesin heterodimer with an inactivating mutation in one head (2008), Biochemistry, 47, 9514-9521.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.6.1.3 wild type and R210K mutant enzymes are expressed in Escherichia coli BL21(DE3) pLysS cells Drosophila melanogaster

Protein Variants

EC Number Protein Variants Comment Organism
5.6.1.3 R210K essentially inactive, the point mutation in kinesin heavy chain disrups the ability of the enzyme active site to catalyze ATP P-O bond cleavage, pairing the inactive R210K subunit with a wild type subunit produces a dimer with essentially the full mechanochemical function of homodimeric wild type kinesin-1 Drosophila melanogaster

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.6.1.3 66000
-
 SDS-PAGE Drosophila melanogaster

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)
-
 ?

Subunits

EC Number Subunits Comment Organism
5.6.1.3 homodimer
-
 Drosophila melanogaster

Synonyms

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