Literature summary for 3.6.4.B1 extracted from

Cho, K.I.; Yi, H.; Desai, R.; Hand, A.R.; Haas, A.L.; Ferreira, P.A.
RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system (2009), EMBO Rep., 10, 480-486.

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Activating Compound

Activating Compound	Comment	Organism	Structure
kinesin-binding domain	activates KIF5B by 10fold in the presence of microtubules	Drosophila melanogaster
microtubule	the ATPase activity of the N-terminal motor of KIF5B (50 nM), but not the C-terminal coiled-coil tail domains of KIF5B (10 mM) and full-length KIF5B (50 nM), is stimulated by microtubules (300 nM)	Drosophila melanogaster
RAN-binding protein 2	allosteric activator that boosts directly the activity of a kinesin, activates the ATPase activity of KIF5B approximately 30fold in the presence of microtubules and ATP	Drosophila melanogaster
RBD2-KBD-RBD3	induces unfolding and modest activation of KIF5B in the absence of microtubules	Drosophila melanogaster

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Drosophila melanogaster	ADP + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
KIF5B	-	Drosophila melanogaster
kinesin superfamily protein 5B	-	Drosophila melanogaster
kinesin-1 motor protein	-	Drosophila melanogaster

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Release 2023.1 (January 2023)