Information on EC 3.6.4.B1 - kinesin K16

Word Map on EC 3.6.4.B1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.4.B1
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
kinesin K16
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram
-
-
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv Coker 130
-
-
Manually annotated by BRENDA team
isoform KIF5C
-
-
Manually annotated by BRENDA team
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
ADP + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
Ca2+-calmodulin inhibits the binding of kinesin-like calmodulin-binding protein to microtubules by blocking the microtubule-binding sites of kinesin-like calmodulin-binding protein
NaCl
-
basal activity is independent of NaCl, microtubule-activated enzyme shows 50% inhibition at around 40 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
kinesin-binding domain
-
activates KIF5B by 10fold in the presence of microtubules
-
microtubule
-
RAN-binding protein 2
-
allosteric activator that boosts directly the activity of a kinesin, activates the ATPase activity of KIF5B approximately 30fold in the presence of microtubules and ATP
-
RBD2-KBD-RBD3
-
induces unfolding and modest activation of KIF5B in the absence of microtubules
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.62
-
pH 7.0, 25°C
16.2
-
pH 7.0, 25°C, presence of microtubules
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
basal activity
6
-
microtubule-activated enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
associated with
Manually annotated by BRENDA team
-
in peripheral blood lymphocytes stimulated with mitogens, KIF4 expression is upregulated, and the protein is localized in the cytoplasm associated with lysosome-associated protein 1+ and perforin+ lysosomal vesicles
Manually annotated by BRENDA team
-
mesenchymal marrow cell
Manually annotated by BRENDA team
-
; marrow stromal cell line
Manually annotated by BRENDA team
-
in muscles of patients with idiopathic inflammatory myopathies, KIF4-positive inflammatory cells are found. In polymyositis and inclusion body myositis, KIF4-positive cells are mainly located around individual muscle fibers, whereas in dermamyositis, KIF4-positive cells are also near blood vessels. KIF4-positive cells are not specific to any immune lineage
Manually annotated by BRENDA team
-
sensory, with exposed ciliated endings
Manually annotated by BRENDA team
-
in manchette and the principal piece of the sperm tail, KIF17b co-localizes with Spatial-epsilon, i.e. stromal protein associated with thymus and lymph-node
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
in addition to association with segregating chromosomes through entire mitosis, it also localizes to the midzone and to midbody at ana/telophase through cytokinesis. In cells at cytokinesis, KIF4 appears as a doublet facing each other at the apical ends of two daughter cells
Manually annotated by BRENDA team
-
KLP-6 protein is targeted via its carboxy terminus to cilia. KLP-6 colocalizes with the polycystins in cilia of male-specific neurons
Manually annotated by BRENDA team
-
AtPAKRP1 is associated with the phragmoplast in the middle of interdigitating microtubules; AtPAKRP1L is present exclusively in the middle of the phragmoplast, where anti-parallel microtubules interdigitate
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
x * 60000, calculated for full-length protein, x * 38000, SDS-PAGE and calculated for motor domain
60000
-
x * 60000, calculated for full-length protein, x * 38000, SDS-PAGE and calculated for motor domain
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 60000, calculated for full-length protein, x * 38000, SDS-PAGE and calculated for motor domain
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
K16MD, the rice kinesin motor domain complexed with Mg-ADP is crystallized by the sitting drop vapor diffusion method at 19.85°C, resulting in a 2.4 A resolution. The ADP-free form of the novel rice-plant-specific kinesin K16 is very stable, whereas the ADP-free form of conventional kinesins is labile. The overall structure of K16MD is similar to that of conventional kinesin motors domains, as expected from the high amino acid sequence similarity of 43.2%. The position and length of the L5, L11m and L12 loops, which are key functional regions, are different from those observed in conventional kinesins. Moreover, the neck-lonker region of the ADP-bound K16MD shows an ordered confirmation at a position quite different from that of conventional kinesins
-
crystallized at 4°C using sitting drop vapor diffusion method and 20% polyethylene glycol 3350 in 0.2 M disodium hydrogen phosphate, 2.3 A resolution
-
four structures of the fragment encoding the potato KCBP from amino acids 884-1252, which include the motor core and the C-terminal extension containing the calmodulin-binding motif. The kinesin motor is in the ATP-like conformation, but loop 11 exhibits different conformational states, both ordered and disordered. When strucutured, loop 11 adds three additional helical turns to the N-terminal part of the following helix alpha4. Positioning of the calmodulin binding helix is not decided by crystal packing forces but is determined by the conformational state of the motor
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant kinesin motor domain
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLys strain
-
expression as fusion with green fluorescent protein in COS-7 cell
-
expression in Escherichia coli of fragment encoding the potato KCBP from amino acids 884-1252, which include the motor core and the C-terminal extension containing the calmodulin-binding motif
-
expression in Escherichia coli of full-length protein and motor domain alone; expression of the motor domain of kinesin K16 in Escherichia coli
-
expression in ganglion RGC-5 neurons and NIH3T3 fibroblast cells
-
expression in HeLa cell
-
expression in mesenchymal marrow cells and COS-7 cells, as green fluorescent protein fusion protein
-
expression in mouse cell
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q101C
-
modification in loop L5 and labeling of mutant Cys residue with 2-(4'-(2''-iodoacetamido)phenyl)aminonaphthalene-6-sulfonic acid. In the absence of nucleotides, label is incorporated at almost equimolar ratio into loop L5. In the presence of ATP and ADP, the incorporated amount is reduced to 0.62 and 0.32 mol label per mol of motor domain, respectively
T93N
-
rigor-mutant, binds to microtubules but fails to move along them
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
photoreactiveATP derivative, 2'(3')-O-(4-benzoylbenzoyl)-1,N6-etheno-ATP acts as a cross-linker to detect conformational changes in the kinesin motor domain
medicine
-
in muscles of patients with idiopathic inflammatory myopathies, KIF4-positive inflammatory cells are found. In polymyositis and inclusion body myositis, KIF4-positive cells are mainly located around individual muscle fibers, whereas in dermamyositis, KIF4-positive cells are also near blood vessels. KIF4-positive cells are not specific to any immune lineage. In peripheral blood lymphocytes stimulated with mitogens, KIF4 expression is upregulated, and the protein is localized in the cytoplasm associated with lysosome-associated protein 1+ and perforin+ lysosomal vesicles