Any feedback?
Literature summary for 5.6.1.4 extracted from
- The ATPase pathway that drives the kinesin-14 Kar3Vik1 powerstroke (2012), J. Biol. Chem., 287, 36673-36682.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of truncated KAR3, coexpression of Kar3 and Vik1 in Escherichia coli strain BL21-CodonPlus(DE)-RIL yielding a Kar3Vik1 heterodimer that forms through the GCN4 leucine zipper | Saccharomyces cerevisiae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | pulse-chase kinetics of ATP binding of the nucleotide-free microtubule-Kar3Vik1 complex and acid quench kinetics of ATP hydrolysis, ATP-promoted dissociation kinetics of the microtubule-Kar3Vik1 complex, detailed overview | Saccharomyces cerevisiae |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| microtubule | tight binding of Kar3 to the microtubule | Saccharomyces cerevisiae | 5874 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Saccharomyces cerevisiae |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 46150 | - |
recombinant truncated KAR3, sequence calculation | Saccharomyces cerevisiae |
| 88880 | - |
recombinant Kar3Vik1 heterodimer, sequence calculation | Saccharomyces cerevisiae |
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 | Saccharomyces cerevisiae | - |
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end) | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | P17119 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + a kinesin associated with a microtubule at position n | - |
Saccharomyces cerevisiae | ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end) | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Kar3 | - |
Saccharomyces cerevisiae |
| Kar3Vik1 | - |
Saccharomyces cerevisiae |
| kinesin-14 | - |
Saccharomyces cerevisiae |
| microtubule minus-end-directed kinesin-14 | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | kinesin-14 represents a subfamily of kinesins that are nonprocessive, promote microtubule (MT)2 minus-end-directed force generation, and contain C-terminal motor domains that are dimerized through an N-terminal coiled coil. Kinesin-14s use an microtubule minus-end-directed rotation or bending of the coiled-coil stalk to generate force | Saccharomyces cerevisiae |
| metabolism | key differences in the ATPase cycles of Kar3Vik1 and Kar3Cik1, these two motors have distinctive biological functions | Saccharomyces cerevisiae |
| additional information | Kar3, a microtubule minus-end-directed kinesin-14, dimerizes with either Vik1 or Cik1. The C-terminal globular domain of Vik1 exhibits the structure of a kinesin motor domain and binds microtubules independently of Kar3 but lacks a nucleotide binding site. The tight binding of Kar3 to the microtubule destabilizes the Vik1 interaction with the microtubule, positioning Kar3Vik1 for the start of the powerstroke. Rapid ATP binding to Kar3 is associated with rotation of the coiled-coil stalk, and the post-powerstroke ATP hydrolysis at 26/s is independent of Vik1, providing further evidence that Vik1 rotates with the coiled coil during the powerstroke. Detachment of Kar3Vik1 from the microtubule completes the cycle and allows the motor to return to its initial conformation | Saccharomyces cerevisiae |
| physiological function | the only known function of Kar3Vik1 is to cross-link parallel microtubules at the spindle poles during mitosis. Kinesin Kar3Vik1 binds across adjacent microtubule protofilaments and uses a minus-end-directed powerstroke to drive ATP-dependent motility | Saccharomyces cerevisiae |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
