The Enzyme Database

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EC 5.6.1.3     
Accepted name: plus-end-directed kinesin ATPase
Reaction: ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
Other name(s): kinesin
Systematic name: kinesin ATP phosphohydrolase (plus-end-directed)
Comments: Kinesins are a family of motor proteins that move unidirectionally along microtubules as they hydrolyse ATP. The enzymes described here move towards the plus end of the microtubule, in contrast to EC 5.6.1.2, dynein ATPase and EC 5.6.1.4, minus-end-directed kinesin ATPase. They are involved in organelle movement in mitosis and meiosis, and also power vesicular trafficking toward the synapse in neurons. The motor domain, which contains the ATP- and microtubule-binding activities, is located at the N-terminus while the C-terminus links to the cargo being transported.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vale, R.D., Reese, T.S. and Sheetz, M.P. Identification of a novel force-generating protein, kinesin, in microtubule-based motility. Cell 42 (1985) 39–50. [DOI] [PMID: 3926325]
2.  Kull, F.J., Sablin, E.P., Lau, R., Fletterick, R.J. and Vale, R.D. Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature 380 (1996) 550–555. [PMID: 8606779]
3.  Howard, J. Molecular motors: structural adaptations to cellular functions. Nature 389 (1997) 561–567. [DOI] [PMID: 9335494]
4.  Nakagawa, T., Tanaka, Y., Matsuoka, E., Kondo, S., Okada, Y., Noda, F., Kanai, Y. and Hirokawa, N. Identification and classification of 16 new kinesin superfamily (KIF) proteins in mouse genome. Proc. Natl. Acad. Sci. USA 94 (1997) 9654–9659. [DOI] [PMID: 9275178]
5.  Sindelar, C.V. and Downing, K.H. The beginning of kinesin’s force-generating cycle visualized at 9-Å resolution. J. Cell Biol. 177 (2007) 377–385. [PMID: 17470637]
6.  Wang, W., Cao, L., Wang, C., Gigant, B. and Knossow, M. Kinesin, 30 years later: Recent insights from structural studies. Protein Sci. 24 (2015) 1047–1056. [PMID: 25975756]
[EC 5.6.1.3 created 2000 as 3.6.4.4, transferred 2018 to EC 5.6.1.3]
 
 


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