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Literature summary for 5.6.1.3 extracted from

  • Wang, W.; Shen, T.; Guerois, R.; Zhang, F.; Kuerban, H.; Lv, Y.; Gigant, B.; Knossow, M.; Wang, C.
    New insights into the coupling between microtubule depolymerization and ATP hydrolysis by kinesin-13 protein Kif2C (2015), J. Biol. Chem., 290, 18721-18731.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information microtubule-stimulated ATPase Homo sapiens
tubulin-vinblastine assemblies stimulation of the ATPase activity of the enzyme Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of the wild-type and mutant minimal functional domain of Kif2C, a fragment comprising the proximal part of the neck region and the motor domain Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant minimal functional domain Kif2C-(sN+M)-sL2 in complex with ADP, by vapor diffusion using a crystallization buffer consisting of 0.1 M Tris-HCl, pH 8.0, 1.5 M ammonium sulfate, and 10% ethylene glycol, at 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using HsKif2C motor domain-ADP, PDB ID 2HEH, as a starting model Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information construction of L2, DVK, and DSK loop2 mutants of the functional domain of Kif2C, the microtubule depolymerization activity of the DVK mutant is remarkably decreased compared to the wild-type, while the DSK mutant does not show microtubule depolymerization activity even at high concentrations Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000047
-
ATP pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DSK Homo sapiens
0.000058
-
ATP pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DVK Homo sapiens
0.00008
-
ATP pH 6.8, 25°C, tubulin-stimulated recombinant Kif2C functional domain wild-type Homo sapiens
0.00018
-
ATP pH 6.8, 25°C, tubulin-stimulated recombinant Kif2C functional domain mutant L2 Homo sapiens
0.0006
-
ATP pH 6.8, 25°C, microtubule-stimulated recombinant Kif2C functional domain mutant DSK Homo sapiens
0.00062
-
ATP pH 6.8, 25°C, tubulin-vinblastine-stimulated recombinant Kif2C functional domain mutant L2 Homo sapiens
0.00105
-
ATP pH 6.8, 25°C, microtubule-stimulated recombinant Kif2C functional domain mutant DVK Homo sapiens
0.0013
-
ATP pH 6.8, 25°C, microtubule-stimulated recombinant Kif2C functional domain mutant L2 Homo sapiens
0.00388
-
ATP pH 6.8, 25°C, tubulin-vinblastine-stimulated recombinant Kif2C functional domain wild-type Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

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 Homo sapiens
-
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
?
additional information Homo sapiens the KVD motif of kinesin Kif2C interacts directly with tubulin. ATP hydrolysis in Kif2C is not required for tubulin release ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q99661
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a kinesin associated with a microtubule at position n
-
Homo sapiens ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
?
additional information the KVD motif of kinesin Kif2C interacts directly with tubulin. ATP hydrolysis in Kif2C is not required for tubulin release Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
Kif2C
-
Homo sapiens
kinesin-13 protein
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.069
-
ATP pH 6.8, 25°C, tubulin-vinblastine-stimulated recombinant Kif2C functional domain mutant L2 Homo sapiens
0.079
-
ATP pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DSK Homo sapiens
0.1
-
ATP pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DVK Homo sapiens
0.117
-
ATP pH 6.8, 25°C, tubulin-stimulated recombinant Kif2C functional domain mutant L2 Homo sapiens
0.152
-
ATP pH 6.8, 25°C, tubulin-stimulated recombinant Kif2C functional domain wild-type Homo sapiens
0.18
-
ATP pH 6.8, 25°C, microtubule-stimulated recombinant Kif2C functional domain mutant DSK Homo sapiens
0.21
-
ATP pH 6.8, 25°C, microtubule-stimulated recombinant Kif2C functional domain mutant L2 Homo sapiens
0.62
-
ATP pH 6.8, 25°C, tubulin-vinblastine-stimulated recombinant Kif2C functional domain wild-type Homo sapiens
0.97
-
ATP pH 6.8, 25°C, microtubule-stimulated recombinant Kif2C functional domain mutant DVK Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
assay at Homo sapiens

General Information

General Information Comment Organism
evolution the enzyme belongs to the kinesin superfamily Homo sapiens
additional information kinesin-13s have a clearly longer loop 2 that folds as a beta-hairpin with a conserved KVD motif at its tip. This KVD motif is necessary for microtubule depolymerization by kinesin-13s. Structural modeling of the Kif2C motor domain in its ATP state in complex with tubulin, overview. The beta-hairpin structure of loop 2 is conserved but shortened. In the mutant, as in the wild type protein, the hairpin that displays the KVD motif interacts similarly with the neck helix, but the KVD motif contacts neither the rest of the motor domain nor the neck helix Homo sapiens
physiological function the interaction of the kinesin-13 Kif2C KVD motif with tubulin is essential. The interaction of the KVD motif quantitatively determines the activities of Kif2C Homo sapiens