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Information on EC 5.6.1.3 - plus-end-directed kinesin ATPase

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EC Tree
IUBMB Comments
Kinesins are a family of motor proteins that move unidirectionally along microtubules as they hydrolyse ATP. The enzymes described here move towards the plus end of the microtubule, in contrast to EC 5.6.1.2, dynein ATPase and EC 5.6.1.4, minus-end-directed kinesin ATPase. They are involved in organelle movement in mitosis and meiosis, and also power vesicular trafficking toward the synapse in neurons. The motor domain, which contains the ATP- and microtubule-binding activities, is located at the N-terminus while the C-terminus links to the cargo being transported.
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UNIPROT: Q99661
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
kinesin, kinesin-1, kif3a, kinesin-5, kif1a, kif11, kif4a, kifc1, kinesin-2, kif5b, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
kinesin-13 protein
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kinesin
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
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SYSTEMATIC NAME
IUBMB Comments
kinesin ATP phosphohydrolase (plus-end-directed)
Kinesins are a family of motor proteins that move unidirectionally along microtubules as they hydrolyse ATP. The enzymes described here move towards the plus end of the microtubule, in contrast to EC 5.6.1.2, dynein ATPase and EC 5.6.1.4, minus-end-directed kinesin ATPase. They are involved in organelle movement in mitosis and meiosis, and also power vesicular trafficking toward the synapse in neurons. The motor domain, which contains the ATP- and microtubule-binding activities, is located at the N-terminus while the C-terminus links to the cargo being transported.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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 plus end)
show the reaction diagram
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-
-
?
additional information
?
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the KVD motif of kinesin Kif2C interacts directly with tubulin. ATP hydrolysis in Kif2C is not required for tubulin release
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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 plus end)
show the reaction diagram
-
-
-
?
additional information
?
-
the KVD motif of kinesin Kif2C interacts directly with tubulin. ATP hydrolysis in Kif2C is not required for tubulin release
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tubulin-vinblastine assemblies
stimulation of the ATPase activity of the enzyme
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additional information
microtubule-stimulated ATPase
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000047 - 0.00388
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.069 - 0.97
ATP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the kinesin superfamily
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KIF2C_HUMAN
725
0
81313
Swiss-Prot
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Biol. Chem.
290
18721-18731
2015
Homo sapiens (Q99661)
Manually annotated by BRENDA team