Literature summary for 5.6.1.3 extracted from

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

Search for more literature for 5.6.1.3

Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
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]

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

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)	-	?

Subunits

Subunits	Comment	Organism
homodimer	-	Drosophila melanogaster

Synonyms

Synonyms	Comment	Organism
kinesin-1	-	Drosophila melanogaster

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)