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Literature summary for 5.6.1.4 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.
    View publication on PubMed

Crystallization (Commentary)

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
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-
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Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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)
-
?