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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.4.B1 kinesin-binding domain activates KIF5B by 10fold in the presence of microtubules Drosophila melanogaster
3.6.4.B1 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
3.6.4.B1 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
3.6.4.B1 RBD2-KBD-RBD3 induces unfolding and modest activation of KIF5B in the absence of microtubules Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.B1 Drosophila melanogaster
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.B1 ATP + H2O
-
 Drosophila melanogaster ADP + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.4.B1 KIF5B
-
 Drosophila melanogaster
3.6.4.B1 kinesin superfamily protein 5B
-
 Drosophila melanogaster
3.6.4.B1 kinesin-1 motor protein
-
 Drosophila melanogaster