KEGG ENZYME: 5.6.1.3

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

All links

Protein sequence (112)   
   UniProt (68)   
   RefSeq(pep) (44)   
DNA sequence (62)   
   RefSeq(nuc) (50)   
   GenBank (6)   
   EMBL (6)   
All databases (174)   

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