Literature summary extracted from

Kozielski,F.; De Bonis, S.; Burmeister, W.P.; Cohen-Addad, C.; Wade, R.H.
The crystal structure of the minis-end-directed microtubule motor protein ncd reveals variable dimer conformations (1999), Structure Fold. Des., 7, 1407-1416.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
5.6.1.4	dimeric ncd, crystals with the C222(1) space group	Drosophila melanogaster

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
5.6.1.4	ATP + H2O + a kinesin associated with a microtubule at position n	Drosophila melanogaster	-	ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
5.6.1.4	Drosophila melanogaster	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
5.6.1.4	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)	structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules	Drosophila melanogaster	a

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5.6.1.4	ATP + H2O + a kinesin associated with a microtubule at position n	-	Drosophila melanogaster	ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)	-	?

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Release 2023.1 (January 2023)