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Literature summary extracted from

  • Kocik, E.; Skowronek, K.J.; Kasprzak, A.A.
    Interactions between subunits in heterodimeric Ncd molecules (2009), J. Biol. Chem., 284, 35735-35745.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.6.1.4 expressed in Escherichia coli BL21(DE3) pLys strain Drosophila melanogaster

Protein Variants

EC Number Protein Variants Comment Organism
5.6.1.4 E585A the mutated amino acids are key residues that are involved in the mediation of structural changes in the head that follow the hydrolysis of the nucelotide. The mutant retains the basal, very low ATPase activity but shows negligible microtubule-stimulated ATPase Drosophila melanogaster
5.6.1.4 E585D the mutated amino acids are key residues that are involved in the mediation of structural changes in the head that follow the hydrolysis of the nucelotide. The mutant retains the basal, very low ATPase activity but shows negligible microtubule-stimulated ATPase Drosophila melanogaster
5.6.1.4 additional information a deletion in the motor domain in one of the subunits resulting in a single-headed molecule, NcN, resulting in a low affinity for microtubules. Mutated homodimers have no microtubule-activated ATPase and no motility, whereas NcN have motility comparable with that of the wild-type Ncd Drosophila melanogaster
5.6.1.4 N600K a decoupling mutant, Asn600 is essential for integrity of the Ncd dimeric structure and transmission of conformational changes from the switch region to the microtubule-binding site. The mutant retains the basal, very low ATPase activity but shows negligible microtubule-stimulated ATPase Drosophila melanogaster
5.6.1.4 R552A the mutated amino acids are key residues that are involved in the mediation of structural changes in the head that follow the hydrolysis of the nucelotide. The mutant retains the basal, very low ATPase activity but shows negligible microtubule-stimulated ATPase Drosophila melanogaster

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
5.6.1.4 mutated protein molecules carrying point mutations in one of the heads, thus producing heterodimeric motors Drosophila melanogaster

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 the heterodimer E585A/wild-type Ncd construct exhibits 16% of the wild-type activity Drosophila melanogaster ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
 ?

Subunits

EC Number Subunits Comment Organism
5.6.1.4 heterodimer although the heterodimers have one fully active and one inactive head, the ATPase and motility of Ncd heterodimers vary dramatically, clearly demonstrating that interactions between motor domains exist in Ncd Drosophila melanogaster
5.6.1.4 homodimer mutated homodimers have no microtubule-activated ATPase and no motility, whereas NcN have motility comparable with that of the wild-type Ncd Drosophila melanogaster

Synonyms

EC Number Synonyms Comment Organism
5.6.1.4 kinesin-14 Ncd Ncd, non-claret disjunctional is an often studied minus-end-directed motor in Drosophila melanogaster Drosophila melanogaster

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.6.1.4 25
-
 assay at Drosophila melanogaster

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.6.1.4 0.1
-
 ATP mutant NcN-E585D, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster
5.6.1.4 0.19
-
 ATP E585D/E585E, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster
5.6.1.4 0.2
-
 ATP mutant E585A/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster
5.6.1.4 0.6
-
 ATP mutant E552A plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster
5.6.1.4 0.6
-
 ATP mutant E552A/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster
5.6.1.4 0.6
-
 ATP mutant N600K plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster
5.6.1.4 0.6
-
 ATP mutant NcN-E585D plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster
5.6.1.4 0.7
-
 ATP mutant E585A plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster
5.6.1.4 0.7
-
 ATP mutant E585D plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster
5.6.1.4 0.9
-
 ATP E585D/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster
5.6.1.4 1.3
-
 ATP wild-type/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster
5.6.1.4 1.4
-
 ATP mutant N600K/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster
5.6.1.4 1.9
-
 ATP mutant NcN, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.6.1.4 7.2
-
 assay at Drosophila melanogaster

General Information

EC Number General Information Comment Organism
5.6.1.4 physiological function the non-processive minus-end-directed kinesin-14 Ncd is involved in the organization of the microtubule network during mitosis. Only one of the two domains is involved in the interaction with the microtubules Drosophila melanogaster