KEGG   ENZYME: 5.6.1.3
Entry
EC 5.6.1.3                  Enzyme                                 

Name
plus-end-directed kinesin ATPase;
kinesin
Class
Isomerases;
Isomerases altering macromolecular conformation;
Enzymes altering polypeptide conformation or assembly
Sysname
kinesin ATP phosphohydrolase (plus-end-directed)
Reaction(IUBMB)
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)
Substrate
ATP [CPD:C00002];
H2O [CPD:C00001];
kinesin associated with a microtubule at position n
Product
ADP [CPD:C00008];
phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
Comment
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.
History
EC 5.6.1.3 created 2000 as 3.6.4.4, transferred 2018 to EC 5.6.1.3
Reference
1  [PMID:3926325]
  Authors
Vale RD, Reese TS, Sheetz MP.
  Title
Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility.
  Journal
Cell 42:39-50 (1985)
DOI:10.1016/S0092-8674(85)80099-4
Reference
2  [PMID:8606779]
  Authors
Kull FJ, Sablin EP, Lau R, Fletterick RJ, Vale RD
  Title
Crystal structure of the kinesin motor domain reveals a structural similarity to  myosin.
  Journal
Nature 380:550-5 (1996)
DOI:10.1038/380550a0
  Sequence
[hsa:3799]
Reference
3  [PMID:9335494]
  Authors
Howard J.
  Title
Molecular motors: structural adaptations to cellular functions.
  Journal
Nature 389:561-7 (1997)
DOI:10.1038/39247
Reference
4  [PMID:9275178]
  Authors
Nakagawa T, Tanaka Y, Matsuoka E, Kondo S, Okada Y, Noda Y, Kanai Y, Hirokawa N.
  Title
Identification and classification of 16 new kinesin superfamily (KIF) proteins in mouse genome.
  Journal
Proc Natl Acad Sci U S A 94:9654-9 (1997)
DOI:10.1073/pnas.94.18.9654
Reference
5  [PMID:17470637]
  Authors
Sindelar CV, Downing KH
  Title
The beginning of kinesin's force-generating cycle visualized at 9-A resolution.
  Journal
J Cell Biol 177:377-85 (2007)
DOI:10.1083/jcb.200612090
  Sequence
[hsa:3799]
Reference
6  [PMID:25975756]
  Authors
Wang W, Cao L, Wang C, Gigant B, Knossow M
  Title
Kinesin, 30 years later: Recent insights from structural studies.
  Journal
Protein Sci 24:1047-56 (2015)
DOI:10.1002/pro.2697
Other DBs
ExplorEnz - The Enzyme Database: 5.6.1.3
IUBMB Enzyme Nomenclature: 5.6.1.3
ExPASy - ENZYME nomenclature database: 5.6.1.3
BRENDA, the Enzyme Database: 5.6.1.3

DBGET integrated database retrieval system