EC Number   |
Protein Variants |
Reference |
|---|
   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 |
712404 |
| 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 |
712404 |
| 5.6.1.4 | G347A |
binds poorly to microtubules in gliding assays, reduced microtubule gliding velocity |
655338 |
| 5.6.1.4 | G347T |
binds poorly to microtubules in gliding assays, reduced microtubule gliding velocity |
655338 |
| 5.6.1.4 | M672N |
site-directed mutagenesis, the mutation has a negligible effect on microtubule binding in the absence of nucleotides although substantially changed the Kd(MT) in the presence of AMPPNP |
719508 |
| 5.6.1.4 | more |
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 |
712404 |
| 5.6.1.4 | more |
construction of a single-headed Ncd heterodimer in which one polypeptide consists of an intact Ncd catalytic core and neck (residues 280700) and the second polypeptide consists of the neck region alone (residues 281347). This motor elicits microtubule gliding at a velocity comparable to that of the normal twoheaded Ncd homodimer with a similar ATPase kcat-value |
689146 |
| 5.6.1.4 | more |
enzyme knockdown using KifC3-mRNA targeting siRNA causing reduced KifC3 function in peroxisomal motility, the peroxisomal KifC3 knockdown phenotype depends on microtubules, is independent of the cell phase and also affects the morphology of mitochondria and endoplasmic reticulum |
733397 |
| 5.6.1.4 | more |
overexpression of full-length enzyme, accumulation in the apical sub-plasma membrane region. COOH-terminal deletion mutant lacking amino acids 1-515, distribution of enzyme homogenously throughout the cytoplasm |
656339 |
| 5.6.1.4 | more |
production of four Ncd mutants in which the C-terminus is altered or deleted, analysis of mutant affinity to the microtubule, steady-state ATPase and gliding velocity in multiple motor assays: the mutations have a dramatic effect on all three parameters measured, suggesting that the C-terminal residues of Ncd play an important role in modulating the interaction of the motor with the microtubule. In the first of the mutants, Ncd670, the entire C-terminal segment is deleted. In mutant Ncd679, the basic fragment spanning aa 671679 is left intact whereas the last 21 aa are deleted. In mutant Ncd700SG the basic fragment is replaced by the sequence GGSGGSGGS, which is uncharged and flexible. In the fourth construct NcdM672N, the hydrophobic Met672 is substituted by a small and polar Asn |
719508 |
