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Information on EC 2.7.1.107 - diacylglycerol kinase (ATP) and Organism(s) Rattus norvegicus and UniProt Accession O08560

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EC Tree
IUBMB Comments
Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Activity is stimulated by certain phospholipids [4,7]. In plants and animals the product 1,2-diacyl-sn-glycerol 3-phosphate is an important second messenger. cf. EC 2.7.1.174, diacylglycerol kinase (CTP).
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This record set is specific for:
Rattus norvegicus
UNIPROT: O08560
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dgk, diacylglycerol kinase, dag kinase, dg kinase, dgkzeta, dagk, dgkalpha, dgk-zeta, diglyceride kinase, dgkepsilon, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diacylglycerol kinase zeta
-
1,2-diacylglycerol kinase
-
-
-
-
1,2-diacylglycerol kinase epsilon
-
-
adenosine 5'-triphosphate:1,2-diacylglycerol 3-phosphotransferase
-
-
-
-
arachidonoyl-specific diacylglycerol kinase
-
-
-
-
ATP:diacylglycerol phosphotransferase
-
-
-
-
DAGKalpha
-
-
-
-
DAGKepsilon
-
-
DG kinase
-
-
-
-
DGK-alpha
-
-
-
-
DGK-theta
-
-
-
-
DGKalpha
-
isoform
DGKbeta
DGKdelta
-
-
-
-
DGKepsilon
-
isoform
DGKgamma
-
-
-
-
DGKiota
DGKksi
-
-
-
-
DGKzeta
diacylglycerol kinase
-
-
-
-
diacylglycerol kinase (ATP dependent)
-
-
-
-
diacylglycerol kinase beta
diacylglycerol kinase epsilon
-
-
diacylglycerol:ATP kinase
-
-
-
-
diglyceride kinase
-
-
-
-
kinase (phosphorylating), 1,2-diacylglycerol
-
-
-
-
kinase, 1,2-diacylglycerol (phosphorylating)
-
-
-
-
sn-1,2-diacylglycerol kinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:1,2-diacyl-sn-glycerol 3-phosphotransferase
Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Activity is stimulated by certain phospholipids [4,7]. In plants and animals the product 1,2-diacyl-sn-glycerol 3-phosphate is an important second messenger. cf. EC 2.7.1.174, diacylglycerol kinase (CTP).
CAS REGISTRY NUMBER
COMMENTARY hide
60382-71-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
-
-
-
?
ATP + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
ATP + 1,2-diarachidonoyl-glycerol
ADP + 1,2-diarachidonoyl-glycerol 3-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 1,2-didecanoylglycerol
ADP + 1,2-didecanoylglycerol 3-phosphate
show the reaction diagram
-
enzyme type I: activity is 157% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 141% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1,2-didodecanoylglycerol
ADP + 1,2-didodecanoylglycerol 3-phosphate
show the reaction diagram
-
enzyme type I: activity is 107% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 227% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1,2-dihexadecanoylglycerol
ADP + 1,2-dihexadecanoylglycerol 3-phosphate
show the reaction diagram
-
enzyme type I: activity is 198% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 231% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1,2-dioctanoylglycerol
ADP + 1,2-dioctanoylglycerol 3-phosphate
show the reaction diagram
ATP + 1,2-ditetradecanoylglycerol
ADP + 1,2-ditetradecanoylglycerol 3-phosphate
show the reaction diagram
-
enzyme type I: activity is 200% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 262% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1-palmitoyl-2-arachidonoyl-sn-glycerol
ADP + 1-palmitoyl-2-arachidonoyl-sn-glycerol 3-phosphate
show the reaction diagram
-
enzyme type I: activity is 181% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 116% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1-palmitoyl-2-linoleoyl-sn-glycerol
ADP + 1-palmitoyl-2-linoleoyl-sn-glycerol 3-phosphate
show the reaction diagram
-
enzyme type I: activity is 116% of the activity with rac-1,2-dioleoylglycerol, enzyme type II: activity is 86% of the activity with rac-1,2-dioleoylglycerol
-
-
?
ATP + 1-palmitoyl-2-oleoyl-sn-glycerol
ADP + 1-palmitoyl-2-oleoyl-sn-glycerol 3-phosphate
show the reaction diagram
ATP + 1-stearoyl-2-arachidonoyl-sn-glycerol
ADP + 1-stearoyl-2-arachidonoyl-sn-glycerol 3-phosphate
show the reaction diagram
-
-
-
-
?
ATP + ceramide
ADP + ceramide 3-phosphate
show the reaction diagram
ATP + rac-1,2-dioleoylglycerol
ADP + rac-1,2-dioleoylglycerol 3-phosphate
show the reaction diagram
-
-
-
-
?
ATP + sn-1,2-dioleoylglycerol
ADP + sn-1,2-dioleoylglycerol 3-phosphate
show the reaction diagram
GTP + 1,2-diacyl-sn-glycerol
GDP + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
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 + 1,2-diacyl-sn-glycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
ATP + 1,2-diacylglycerol
ADP + 1,2-diacyl-sn-glycerol 3-phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
when Mg2+ is excluded from the assay, Cd2+ supports activity to lesser extent
Co2+
-
when Mg2+ is excluded from the assay, Co2+ supports activity to lesser extent
Zn2+
-
when Mg2+ is excluded from the assay, Zn2+ supports activity to lesser extent
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine
-
0.5 mM, 5% inhibition of DGK I and 28% inhibition of DGK IV
ADP
-
0.5 mM, 77% inhibition of DGK I and 66% inhibition of DGK IV
AMP
-
0.5 mM, 18% inhibition of DGK I and 14% inhibition of DGK IV
ATPgammaS
-
0.5 mM, 93% inhibition of DGK I and 71% inhibition of DGK IV
cAMP
-
0.5 mM, 20% inhibition of DGK I and 15% inhibition of DGK IV
CDP
-
0.5 mM, 43% inhibition of DGK I and 28% inhibition of DGK IV
ceramide
-
-
CTP
-
0.5 mM, 42% inhibition of DGK I and 9% inhibition of DGK IV
dioctanoylglycerol
-
above 3.4 mol%
dioleoylglycerol
-
above 3.4 mol%
GDP
-
0.5 mM, 74% inhibition of DGK I and 72% inhibition of DGK IV
GTPgammaS
-
0.5 mM, 37% inhibition of DGK I and 32% inhibition of DGK IV
H2O2
-
endogenous nuclear diacylglycerol kinase zeta rapidly translocates to the cytoplasm following H2O2 treatment
quercetin
-
0.1 mM, 41% inhibition of DGK I and 15% inhibition of DGK IV
R59022
R59949
additional information
-
no inhibition by R59022, a type I DAGK inhibitor
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cardiolipin
-
half-maximal activation by 1 mol%
D-glucose
-
exposure of L6 cell myotubes overexpressing human insulin receptors to 25 mM glucose for 5 min decreases the intracellular levels of diacylglycerol, paralleled by transient activation of diacylglycerol kinase and of insulin receptor signaling. Following 30-min exposure, both diacylglycerol levels and diacylglycerol kinase activity return close to basal levels. Glucose exposure redistributes diacylglycerol kinase isoforms alpha and delta, from the prevalent cytosolic localization to the plasma membrane fraction
detergent
-
no activity in absence of detergent
-
endothelin-1
-
activates diacylglycerol kinase in caveolae/rafts and noncaveolae/rafts of mesenteric arteries. Activation does not depend on phosphatidylinositol 3-kinase. In response to norepinephrin, but not to epithelin-1, protein kinase PKB translocates to caveolae/rafts
H2O2
-
endogenous nuclear diacylglycerol kinase zeta rapidly translocates to the cytoplasm following H2O2 treatment
norepinephrine
-
stimulates an increase in diacylglycerol kinase activity in caveolae/rafts of mesenteric arteries. Activation depends on phosphatidylinositol 3-kinase. In response to norepinephrin, but not to epithelin-1, protein kinase PKB translocates to caveolae/rafts
phosphatidic acid
-
good activator of DGK IV, no effect on DGK I activity
phosphatidylcholine
phosphatidylinositol
phosphatidylserine
Phospholipid
-
activation by phospholipid is not stereospecific and is mimicked partially by fatty acids
sodium cholate
-
enhances activity of DGK I and DGK IV
sodium deoxycholate
-
enhances activity of DGK I and DGK IV
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 0.14
1,2-diarachidonoyl-glycerol
0.07 - 0.09
1-stearoyl-2-arachidonoyl-sn-glycerol
0.105 - 0.506
ATP
0.42 - 0.63
GTP
0.1 - 0.125
sn-1,2-dioleoylglycerol
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.5
-
enzyne form DGK I
5.187
-
enzyme form DGK IV
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
pH 6.5: about 45% of maximal activity, pH 8.5: about 45% of maximal activity
6.8 - 9
-
pH 6.5: about 85% of maximal activity pH 9.0: about 50% of maximal activity, enzyme form DGK I
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
it remains unclear whether the multiple species, observed by isoelectric focusing represent distinct isoforms of the enzyme, or are modified versions of the type I and type II enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
DGKzeta-immunoreactivity is clearly detected in Iba1-immunoreactive cells of an oval or ameboid shape in the scar region, which represent activated microglia and/or macrophages. DGKzeta-immunoreactivity is not detected in Iba1-immunoreactive, resting microglia of ramified and dendritic configuration in the intact cortex
Manually annotated by BRENDA team
dendritic spines on neuronal dendrites
Manually annotated by BRENDA team
DGKzeta is detected heterogeneously in the nucleus and cytoplasm of small neurons of the dorsal root ganglion with variable levels of distribution, whereas it is detected exclusively in the cytoplasm of large neurons
Manually annotated by BRENDA team
-
isozymes DGKalpha and DGKzeta
Manually annotated by BRENDA team
-
neuron, DGK-II
Manually annotated by BRENDA team
-
ras-transformed
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
alveolar, isozymes DGKalpha and DGKzeta
Manually annotated by BRENDA team
-
isozyme DGKgamma, day 3-14 after birth
Manually annotated by BRENDA team
DGKbeta is expressed in medium spiny neurons constituting the striatonigral and striatopallidal pathways, whereas striatal interneurons are below the detection threshold
Manually annotated by BRENDA team
weak labeling in the neocortex
Manually annotated by BRENDA team
weak labeling in the olfactory bulb
Manually annotated by BRENDA team
-
the selective distribution of isozyme DAGKepsilon in photoreceptor cells is a light-dependent mechanism that promotes increased 1-stearoyl, 2-arachidonoylglycerol removal and synthesis of 1-stearoyl, 2-arachidonoyl phosphatidic acid in the sensorial portion of this cell
Manually annotated by BRENDA team
-
DGKbeta is the major isozyme in the pituitary gland, the signals are also detected intensely for isoform DGKzeta, moderately for DGKepsilon and faintly for DGKalpha, the signals for isoforms DGKgamma and DGKiota are below the detection level
Manually annotated by BRENDA team
-
delay of isozyme DGKgamma
Manually annotated by BRENDA team
-
from albino rats, isozyme DAGKepsilon appears to be higher in rod outer segments from rat retinas exposed to light than in those under dark conditions. DAGKepsilon in rat retina naturally exposed to room light is present in all retinal layers and is distributed along the photoreceptor cell
Manually annotated by BRENDA team
DGKiota immunoreactivity is distributed solely in the cytoplasm of most of the dorsal root ganglion
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
isoform DGKzeta translocates from the nucleus to the cytoplasm inbeta-cells in response to a beta-cell-selective toxin streptozotocin
Manually annotated by BRENDA team
-
DGKepsilon is detected in a filamentous pattern, parallel to the long axis of cell, and on actin stress fibers
Manually annotated by BRENDA team
diacylglacerol kinase isoform gamma
Manually annotated by BRENDA team
-
activity of DGK-I is recovered dominantly in the soluble fraction, that for DGK-II in the particulate fraction and that for DGK-III in soluble and particulate fraction
-
Manually annotated by BRENDA team
-
from albino rats, isozyme DAGKepsilon appears to be higher in rod outer segments from rat retinas exposed to light than in those under dark conditions. DAGKepsilon in rat retina naturally exposed to room light is present in all retinal layers and is distributed along the photoreceptor cell
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
knockdown of DGKfzeta in cultured neurons decreases spine density
physiological function
isoform DGKf appears to form a multi-protein complex with functionally related proteins to organize efficient 1,2-diacylglycerol and 1,2-diacyl-sn-glycerol 3-phosphate signaling pathways at excitatory synapses, the DGKzeta isoform at excitatory postsynaptic sites is critically involved in spine maintenance, DGKzeta promotes neurite outgrowth
evolution
comprehensive analysis on the 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities, EC 2.7.1.94, of ten diacylglyceol kinase (DGK) isozymes, EC 2.7.1.107, from different organisms. Type I (alpha, beta, and gamma), type II (delta, eta, and kappa) and type III (epsilon) DGKs have 7.9-19.2% 2-MGK activity compared to their DGK activities, whereas their 1-MGK activities are below 3.0%. Both the 1-MGK and 2-MGK activities of the type IV DGKs (zeta and iota) are below 1% relative to their DGK activities. Type V DGKtheta has approximately 6% 1-MGK activity and below 2% 2-MGK activity compared to its DGK activity. Purified DGKtheta exhibits the same results, indicating that its 1-MGK activity is intrinsic. DGK isozymes are categorized into three types with respect to their 1-MGK and 2-MGK activities: those having (1) 2-MGK activity relatively stronger than their 1-MGK activity (types I-III), (2) only negligible 1-MGK and 2-MGK activities (type IV), and (3) 1-MGK activity stronger than its 2-MGK activity (type V). The 1-MGK activity of DGKtheta and the 2-MGK activity of DGKalpha are stronger than those of the acylglycerol kinase reported as 1-MGK and 2-MGK to date
malfunction
presence or absence of 1-MGK and 2-MGK activities may be essential to the pathophysiological functions of each DGK isozyme
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DGKZ_RAT
929
0
104009
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
104000
-
x * 104000, DGK-IVksi, calculation from amino acid sequence
110000
-
1 * 110000, enzyme from cell line PC12, SDS-PAGE
82200
-
x * 82200, DGK-Ialpha, calculation from amino acid sequence
88500
-
x * 88500, DGK-Igamma, calculation from amino acid sequence
90000
isoform DGKbeta, SDS-PAGE
90300
-
x * 90300, DGK-Ibeta, calculation from amino acid sequence
95000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G356D
inactive mutant of diacylglycerol kinase zeta due to replacement of ATP-binding domain GxGxxG with GxDxxG. Similar subcellular localization as wild type
G279D
inactive mutant of diacylglycerol kinase epsilon due to replacement of ATP-binding domain GxGxxG with GxDxxG. Similar subcellular localization as wild type
G428D
inactive mutant of diacylglycerol kinase alpha due to replacement of ATP-binding domain GxGxxG with GxDxxG. Similar subcellular localization as wild type
G491D
inactive mutant of diacylglycerol kinase gamma due to replacement of ATP-binding domain GxGxxG with GxDxxG. Similar subcellular localization as wild type
G495D
inactive mutant of diacylglycerol kinase beta due to replacement of ATP-binding domain GxGxxG with GxDxxG. In contrast to the filamentous image of the wild type, mutant is diffusely distributed throughout the cytoplasm
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
microsomal activity is more unstable on storage at 0°C than the soluble enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in presence of 1 mM dithiothreitol, microsomal and soluble enzyme stable for about 1 week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DGK I and DGK IV
-
recombinant GST-fusion isozymes DGKalpha, DGKgamma, and DGKbeta from Escherichia coli, and Sf9 cells, respectively, and from COS-7 cells, by glutathione affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in COS-7 cell
cDNA subcloned into the EcoRI site of the simian virus 40-based expression vector pSRE
-
expression in COS-7 cell
expression in NIH 3T3 cells
-
GFP-tagged DGKh and DGKg co-expressed in human neuroblastoma cells SH-SY5Y, expression of GST-fusion isozyme DGKalpha and DGKgamma in Escherichia coli strain DH5alpha, expression of GST-fusion isozyme DGKbeta in Spodoptera frugiperda Sf9 cells via baculovirus infection system, expression of GST-fusion isozymes DGKalpha, DGKbeta, and DGKgamma in COS-7 cells
-
high kinase activity is shown in COS cells transfected with either one of the three cDNAs for DGK-I, DGK-II or DGK-III
-
recombinant expression of rat p3×FLAG-CMV-DGK isozyme beta in COS-7 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
as early as 1h after cryoinjury, DGKzeta-immunoreactivity is greatly decreased in the afflicted cerebral cortex and almost disappears in the necrotic core. On day 7 after cryoinjury, however, DGKzeta-immunoreactivity reappears in this area
DGKzeta is induced in activated microglia in brain trauma
DGKzeta mRNA levels are increased in rats on a high-fat diet, but are lower in those that become obese by a high-fat diet
protein and mRNA expression of isoform DGKepsilon in aortic smooth muscle cells is significantly increased by stimulation with serotonin
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
DGKzeta may be a therapeutic target to prevent cardiac hypertrophy and progression to heart failure
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Younes, A.; Kahn, D.W.; Besterman, J.M.; Bittman, R.; Byun, H.S.; Kolesnick, R.N.
Ceramide is a competitive inhibitor of diacylglycerol kinase in vitro and in intact human leukemia (HL-60) cells
J. Biol. Chem.
267
842-847
1992
Rattus norvegicus
Manually annotated by BRENDA team
Kato, M.; Takenawa, T.
Purification and characterization of membrane-bound and cytosolic forms of diacylglycerol kinase from rat brain
J. Biol. Chem.
265
794-800
1990
Rattus norvegicus
Manually annotated by BRENDA team
Stathopoulos, V.M.; Coco-Maroney, A.; Wei, C.W.; Goth, M.; Zaricznyj, C.; Macara, I.G.
Identification of two cytosolic diacylglycerol kinase isoforms in rat brain, and in NIH-3T3 and ras-transformed fibroblasts
Biochem. J.
272
569-575
1990
Rattus norvegicus
Manually annotated by BRENDA team
Kanoh, H.; Akesson, B.
Properties of microsomal and soluble diacylglycerol kinase in rat liver
Eur. J. Biochem.
85
225-232
1978
Rattus norvegicus
Manually annotated by BRENDA team
Walsh, J.P.; Bell, R.M.
sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis of the phospholipid cofactor requirement and divalent cation dependence
J. Biol. Chem.
261
6239-6247
1986
Rattus norvegicus
Manually annotated by BRENDA team
Hee-Cheong, M.; Fletcher, T.; Kryski, S.K.; Severson, D.L.
Diacylglycerol lipase and kinase activities in rat brain microvessels
Biochim. Biophys. Acta
883
59-68
1985
Rattus norvegicus
-
Manually annotated by BRENDA team
Goto, K.; Kondo, H.
Heterogeneity of diacylglycerol kinase in terms of molecular structure, biochemical characteristics and gene expression localization in the brain
J. Lipid Mediat. Cell Signal.
14
251-257
1996
Rattus norvegicus
Manually annotated by BRENDA team
Tabellini, G.; Bortul, R.; Santi, S.; Riccio, M.; Baldini, G.; Cappellini, A.; Billi, A.M.; Berezney, R.; Ruggeri, A.; Cocco, L.; Martelli, A.M.
Diacylglycerol kinase-theta is localized in the speckle domains of the nucleus
Exp. Cell Res.
287
143-154
2003
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Sakane, F.; Kanoh, H.
Molecules in focus: diacylglycerol kinase
Int. J. Biochem. Cell Biol.
29
1139-1143
1997
Homo sapiens, Mesocricetus auratus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Yamada, K.; Sakane, F.; Matsushima, N.; Kanoh, H.
EF-hand motifs of alpha, beta and gamma isoforms of diacylglycerol kinase bind calcium with different affinities and conformational changes
Biochem. J.
321
59-64
1997
Homo sapiens, Rattus norvegicus, Sus scrofa, Sus scrofa DGKalpha
Manually annotated by BRENDA team
Katagiri, Y.; Ito, T.; Saino-Saito, S.; Hozumi, Y.; Suwabe, A.; Otake, K.; Sata, M.; Kondo, H.; Sakane, F.; Kanoh, H.; Kubota, I.; Goto, K.
Expression and localization of diacylglycerol kinase isozymes and enzymatic features in rat lung
Am. J. Physiol.
288
L1171-1178
2005
Rattus norvegicus
Manually annotated by BRENDA team
Adachi, N.; Oyasu, M.; Taniguchi, T.; Yamaguchi, Y.; Takenaka, R.; Shirai, Y.; Saito, N.
Immunocytochemical localization of a neuron-specific diacylglycerol kinase beta and gamma in the developing rat brain
Mol. Brain Res.
139
288-299
2005
Rattus norvegicus
Manually annotated by BRENDA team
Clarke, C.J.; Ohanian, V.; Ohanian, J.
Norepinephrine and endothelin activate diacylglycerol kinases in caveolae/rafts of rat mesenteric arteries: agonist-specific role of PI3-kinase
Am. J. Physiol. Heart Circ. Physiol.
292
H2248-H2256
2007
Rattus norvegicus
Manually annotated by BRENDA team
Sasaki, H.; Hozumi, Y.; Hasegawa, H.; Ito, T.; Takagi, M.; Ogino, T.; Watanabe, M.; Goto, K.
gene expression and localization of diacylglycerol kinase isozymes in the rat spinal cord and dorsal root ganglia
Cell Tissue Res.
326
35-42
2006
Rattus norvegicus, Rattus norvegicus (O08560)
Manually annotated by BRENDA team
Evangelisti, C.; Bortul, R.; Fala, F.; Tabellini, G.; Goto, K.; Martelli, A.M.
Nuclear diacylglycerol kinases: emerging downstream regulators in cell signalling networks
Histol. Histopathol.
22
573-579
2007
Chlorocebus aethiops, Cricetulus griseus, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Takeishi, Y.; Goto, K.; Endoh, M.
Role of siacylglycerol kinase in cellular regulatory processes: a new regulator for cardiomyocyte hypertrophy
Pharmacol. Ther.
115
352-359
2007
Rattus norvegicus
Manually annotated by BRENDA team
Song, J.; Li, J.; Mourot, J.M.; Evers, B.M.; Chung, D.H.
Diacylglycerol kinase regulation of protein kinase D during oxidative stress-induced intestinal cell injury
Biochem. Biophys. Res. Commun.
375
200-204
2008
Rattus norvegicus
Manually annotated by BRENDA team
Chibalin, A.V.; Leng, Y.; Vieira, E.; Krook, A.; Bjoernholm, M.; Long, Y.C.; Kotova, O.; Zhong, Z.; Sakane, F.; Steiler, T.; Nylen, C.; Wang, J.; Laakso, M.; Topham, M.K.; Gilbert, M.; Wallberg-Henriksson, H.; Zierath, J.R.
Downregulation of diacylglycerol kinase delta contributes to hyperglycemia-induced insulin resistance
Cell
132
375-386
2008
Mus musculus, Rattus norvegicus, Homo sapiens (Q16760), Homo sapiens
Manually annotated by BRENDA team
Kobayashi, N.; Hozumi, Y.; Ito, T.; Hosoya, T.; Kondo, H.; Goto, K.
Differential subcellular targeting and activity-dependent subcellular localization of diacylglycerol kinase isozymes in transfected cells
Eur. J. Cell Biol.
86
433-444
2007
Rattus norvegicus, Rattus norvegicus (O08560), Rattus norvegicus (P49621), Rattus norvegicus (P51556)
Manually annotated by BRENDA team
Miele, C.; Paturzo, F.; Teperino, R.; Sakane, F.; Fiory, F.; Oriente, F.; Ungaro, P.; Valentino, R.; Beguinot, F.; Formisano, P.
Glucose regulates diacylglycerol intracellular levels and protein kinase C activity by modulating diacylglycerol kinase subcellular localization
J. Biol. Chem.
282
31835-31843
2007
Rattus norvegicus
Manually annotated by BRENDA team
Hozumi, Y.; Watanabe, M.; Otani, K.; Goto, K.
Diacylglycerol kinase beta promotes dendritic outgrowth and spine maturation in developing hippocampal neurons
BMC Neurosci.
10
99
2009
Rattus norvegicus (P49621)
Manually annotated by BRENDA team
Nakano, T.; Hozumi, Y.; Goto, K.; Wakabayashi, I.
Localization of diacylglycerol kinase epsilon on stress fibers in vascular smooth muscle cells
Cell Tissue Res.
337
167-175
2009
Rattus norvegicus
Manually annotated by BRENDA team
Hozumi, Y.; Fukaya, M.; Adachi, N.; Saito, N.; Otani, K.; Kondo, H.; Watanabe, M.; Goto, K.
Diacylglycerol kinase beta accumulates on the perisynaptic site of medium spiny neurons in the striatum
Eur. J. Neurosci.
28
2409-2422
2008
Rattus norvegicus (P49621)
Manually annotated by BRENDA team
Hozumi, Y.; Watanabe, M.; Goto, K.
Signaling cascade of diacylglycerol kinase beta in the pituitary intermediate lobe: Dopamine D2 receptor/phospholipase Cbeta4/diacylglycerol kinase beta/protein kinase Calpha
J. Histochem. Cytochem.
58
119-129
2010
Rattus norvegicus
Manually annotated by BRENDA team
Kim, K.; Yang, J.; Kim, E.
Diacylglycerol kinases in the regulation of dendritic spines
J. Neurochem.
112
577-587
2010
Rattus norvegicus (O08560), Mus musculus (Q80UP3)
Manually annotated by BRENDA team
Nakano, T.; Iseki, K.; Hozumi, Y.; Kawamae, K.; Wakabayashi, I.; Goto, K.
Brain trauma induces expression of diacylglycerol kinase zeta in microglia
Neurosci. Lett.
461
110-115
2009
Rattus norvegicus (O08560)
Manually annotated by BRENDA team
Sato, Y.; Murakami, C.; Yamaki, A.; Mizuno, S.; Sakai, H.; Sakane, F.
Distinct 1-monoacylglycerol and 2-monoacylglycerol kinase activities of diacylglycerol kinase isozymes
Biochim. Biophys. Acta
1864
1170-1176
2016
Homo sapiens (O75912), Homo sapiens (P49619), Homo sapiens (P52429), Homo sapiens (P52824), Homo sapiens (Q13574), Homo sapiens (Q16760), Homo sapiens (Q5KSL6), Homo sapiens (Q86XP1), Sus scrofa (P20192), Rattus norvegicus (P68403)
Manually annotated by BRENDA team
Natalini, P.M.; Zulian, S.E.; Ilincheta de Boschero, M.G.; Giusto, N.M.
Diacylglycerol kinase epsilon in bovine and rat photoreceptor cells. Light-dependent distribution in photoreceptor cells
Exp. Eye Res.
112
139-150
2013
Bos taurus, Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Hozumi, Y.; Nakano, T.; Tanaka, T.; Goto, K.
Localization of diacylglycerol kinase zeta in rat pancreatic islet cells under normal and streptozotocin-induced stress conditions
Arch. Histol. Cytol.
76
23-33
2016
Rattus norvegicus (O08560)
-
Manually annotated by BRENDA team