ExplorEnz: EC 5.6.1.4

Your query returned 1 entry. Printable version

5.6.1.4

Accepted name:

minus-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 minus end)

Other name(s):

non-claret disjunctional; ncd (gene name)

Systematic name:

kinesin ATP phosphohydrolase (minus-end-directed)

Comments:

Kinesins are a family of motor proteins that move unidirectionally along microtubules as they hydrolyse ATP and are involved in organelle movement. This enzyme is similar to EC 5.6.1.3, plus-end-directed kinesin ATPase, but the organization of the different domains differs, resulting in movement in the opposite direction along the microtubules.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	McDonald, H.B., Stewart, R.J. and Goldstein, L.S. The kinesin-like ncd protein of Drosophila is a minus end-directed microtubule motor. Cell 63 (1990) 1159–1165. [PMID: 2261638]
2.	Chandra, R., Salmon, E.D., Erickson, H.P., Lockhart, A. and Endow, S.A. Structural and functional domains of the Drosophila ncd microtubule motor protein. J. Biol. Chem. 268 (1993) 9005–9013. [PMID: 8473343]
3.	Lockhart, A. and Cross, R.A. Origins of reversed directionality in the ncd molecular motor. EMBO J. 13 (1994) 751–757. [PMID: 8112290]
4.	Henningsen, U. and Schliwa, M. Reversal in the direction of movement of a molecular motor. Nature 389 (1997) 93–96. [DOI] [PMID: 9288974]
5.	Sablin, E.P., CASe, R.B., Dai, S.C., Hart, C.L., Ruby, A., Vale, R.D. and Fletterick, R.J. Direction determination in the minus-end-directed kinesin motor ncd. Nature 395 (1998) 813–816. [DOI] [PMID: 9796817]

[EC 5.6.1.4 created 2000 as 3.6.4.5, transferred 2018 to EC 5.6.1.4]