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ATP + 1,2-dioleoyl-sn-glycerol
ADP + 1,2-dioleoyl-sn-glycerol 3-phosphate
-
recombinant enzyme
-
-
?
ATP + 1,2-dipalmitoylglycerol
ADP + 1,2-dipalmitoylglycerol 3-phosphate
ATP + 1-arachidonoylglycerol
ADP + 1-arachidonoylglycerol 3-phosphate
-
-
-
-
?
ATP + 1-arachidoylglycerol
ADP + 1-arachidoylglycerol 3-phosphate
-
-
-
-
?
ATP + 1-caproylglycerol
ADP + 1-caproylglycerol 3-phosphate
-
-
-
-
?
ATP + 1-capryloylglycerol
ADP + 1-capryloylglycerol 3-phosphate
-
-
-
-
?
ATP + 1-lauroylglycerol
ADP + 1-lauroylglycerol 3-phosphate
-
-
-
-
?
ATP + 1-linolenoylglycerol
ADP + 1-linolenoylglycerol 3-phosphate
-
-
-
-
?
ATP + 1-linoleoylglycerol
ADP + 1-linoleoylglycerol 3-phosphate
-
-
-
-
?
ATP + 1-monoolein
ADP + 1-oleoylglycerol 3-phosphate
-
i.e. 1-monooleolylglyerol
-
-
?
ATP + 1-myristoylglycerol
ADP + 1-myristoylglycerol 3-phosphate
-
-
-
-
?
ATP + 1-oleoyl-sn-glycerol
ADP + 1-oleoyl-sn-glycerol 3-phosphate
-
recombinant enzyme
-
-
?
ATP + 1-palmitoleoylglycerol
ADP + 1-palmitoleoylglycerol 3-phosphate
-
-
-
-
?
ATP + 1-palmitoyl-sn-glycerol
ADP + 1-palmitoyl-sn-glycerol 3-phosphate
-
recombinant enzyme
-
-
?
ATP + 1-palmitoylglycerol
ADP + 1-palmitoylglycerol 3-phosphate
ATP + 1-stearoyl-sn-glycerol
ADP + 1-stearoyl-sn-glycerol 3-phosphate
-
recombinant enzyme
-
-
?
ATP + 1-stearoylglycerol
ADP + 1-stearoylglycerol 3-phosphate
-
-
-
-
?
ATP + 2-arachidonoyl glycerol
ADP + 2-arachidonoylglycerol 3-phosphate
-
-
-
-
?
ATP + 2-arachidonoyl-glycerol
ADP + 2-arachidonoyl-glycerol 3-phosphate
ATP + 2-arachidonoylglycerol
ADP + 2-arachidonoylglycerol 3-phosphate
-
-
-
-
?
ATP + 2-arachidoylglycerol
ADP + 2-arachidoylglycerol 3-phosphate
-
-
-
-
?
ATP + 2-caproylglycerol
ADP + 2-caproylglycerol 3-phosphate
-
-
-
-
?
ATP + 2-lauroylglycerol
ADP + 2-lauroylglycerol 3-phosphate
-
-
-
-
?
ATP + 2-linolenoylglycerol
ADP + 2-linolenoylglycerol 3-phosphate
-
-
-
-
?
ATP + 2-linoleoylglycerol
ADP + 2-linoleoylglycerol 3-phosphate
-
-
-
-
?
ATP + 2-monoolein
ADP + 2-oleoyoglycerol 3-phosphate
-
i.e. 2-monooleolylglyerol
-
-
?
ATP + 2-palmitoleoylglycerol
ADP + 2-palmitoleoylglycerol 3-phosphate
-
-
-
-
?
ATP + 2-palmitoylglycerol
ADP + 2-palmitoylglycerol 3-phosphate
-
-
-
-
?
ATP + 2-stearoylglycerol
ADP + 2-stearoylglycerol 3-phosphate
-
-
-
-
?
ATP + acylglycerol
ADP + acyl-sn-glycerol 3-phosphate
ATP + acylglycerol
ADP + lysophosphatidic acid
ATP + diacylglycerol
ADP + phosphatidic acid
ATP + monoacylglycerol
ADP + lysophosphatidic acid
ATP + PTEN protein
ADP + phosphorylated PTEN protein
-
-
-
?
additional information
?
-
ATP + 1,2-dipalmitoylglycerol
ADP + 1,2-dipalmitoylglycerol 3-phosphate
-
-
product identified as alpha-phosphatidic acid
?
ATP + 1,2-dipalmitoylglycerol
ADP + 1,2-dipalmitoylglycerol 3-phosphate
-
-
product identified as alpha-phosphatidic acid
?
ATP + 1-palmitoylglycerol
ADP + 1-palmitoylglycerol 3-phosphate
-
-
-
-
?
ATP + 1-palmitoylglycerol
ADP + 1-palmitoylglycerol 3-phosphate
-
-
-
?
ATP + 1-palmitoylglycerol
ADP + 1-palmitoylglycerol 3-phosphate
-
-
-
?
ATP + 2-arachidonoyl-glycerol
ADP + 2-arachidonoyl-glycerol 3-phosphate
-
-
-
-
?
ATP + 2-arachidonoyl-glycerol
ADP + 2-arachidonoyl-glycerol 3-phosphate
-
recombinant enzyme
-
-
?
ATP + acylglycerol
ADP + acyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + acylglycerol
ADP + acyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + acylglycerol
ADP + acyl-sn-glycerol 3-phosphate
-
the enzyme acts on both 1- and 2-acylglycerols, substrate specificity, overview
-
-
?
ATP + acylglycerol
ADP + acyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + acylglycerol
ADP + acyl-sn-glycerol 3-phosphate
-
the enzyme acts on both 1- and 2-acylglycerols, substrate specificity, overview
-
-
?
ATP + acylglycerol
ADP + acyl-sn-glycerol 3-phosphate
-
the enzyme acts on both 1- and 2-acylglycerols, substrate specificity, overview
-
-
?
ATP + acylglycerol
ADP + lysophosphatidic acid
-
-
-
?
ATP + acylglycerol
ADP + lysophosphatidic acid
-
-
-
-
?
ATP + acylglycerol
ADP + lysophosphatidic acid
-
-
-
?
ATP + diacylglycerol
ADP + phosphatidic acid
-
-
-
-
?
ATP + diacylglycerol
ADP + phosphatidic acid
-
-
i.e. diacyl-glycerol 3-phosphate, regulation mechanism, overview
-
?
ATP + diacylglycerol
ADP + phosphatidic acid
-
-
i.e. diacyl-glycerol 3-phosphate
-
?
ATP + diacylglycerol
ADP + phosphatidic acid
-
-
i.e. diacyl-glycerol 3-phosphate
-
?
ATP + monoacylglycerol
ADP + lysophosphatidic acid
-
-
-
-
?
ATP + monoacylglycerol
ADP + lysophosphatidic acid
-
-
i.e. acyl-sn-glycerol 3-phosphate, regulation mechanism, overview
-
?
ATP + monoacylglycerol
ADP + lysophosphatidic acid
-
-
i.e. acyl-sn-glycerol 3-phosphate
-
?
ATP + monoacylglycerol
ADP + lysophosphatidic acid
-
-
-
?
ATP + monoacylglycerol
ADP + lysophosphatidic acid
-
-
i.e. acyl-sn-glycerol 3-phosphate
-
?
additional information
?
-
-
1-monostearin amongst the 1-acylglycerols and 2-monoarachidonin amongst the 2-acylglycerols give the highest activity
-
-
?
additional information
?
-
-
preference for substrates with unsaturated fatty acids except for 1- and 2-monostearins
-
-
?
additional information
?
-
-
lysophosphatidic acid induces the cytokine interleukin-8 correlated with angiogenesis, tumorigenicity, and cancer cell proliferation, the enzyme modulates cross talk with EGFR in prostate cancer cells, enzyme regulates the synthesis of the bioactive phospholipids lysophosphatidic acid and phosphatidic acid, activation of extracellular signal related kinase 1 and 2, thus being involved in pathenogenesis of cancer via enhanced cell proliferation
-
-
?
additional information
?
-
-
the enzyme plays a critical role in epidermal growth factor-induced mitogenesis of prostate cancer cells via EGF and IFG-II, and lysophosphatidic acid, the first way can be inhibited by enzyme suppression, the second cannot, enzyme function and regulation in initiation and progression of prostate cancer, lysophosphatidic acid enhances surival and suppresses apoptosis by reducing levels of the apoptosis-promoting protein Bax, and is involved in signal transduction pathways, overview
-
-
?
additional information
?
-
-
no activity by the recombinant enzyme with C6-ceramide and sphingosine
-
-
?
additional information
?
-
-
in addition to its main activity, phosphorylation of 1,2-diacyl-sn-glycerol to 1,2-diacyl-sn-glycerol 3-phosphate, EC 2.7.1.107, the enzyme also shows acylglycerol kinase activity, EC 2.7.1.94. Both monoacylglycerol kinase activities are low
-
-
?
additional information
?
-
-
in addition to its main activity, phosphorylation of 1,2-diacyl-sn-glycerol to 1,2-diacyl-sn-glycerol 3-phosphate, EC 2.7.1.107, the enzyme also shows acylglycerol kinase activity, EC 2.7.1.94. Both monoacylglycerol kinase activities are very low
-
-
?
additional information
?
-
-
in addition to its main activity, phosphorylation of 1,2-diacyl-sn-glycerol to 1,2-diacyl-sn-glycerol 3-phosphate, EC 2.7.1.107, the enzyme also shows acylglycerol kinase activity, EC 2.7.1.94. The 2-MGK activity is very low
-
-
?
additional information
?
-
-
the enzyme modulates cross talk with EGFR in prostate cancer cells, enzyme regulates the synthesis of the bioactive phospholipids lysophosphatidic acid and phosphatidic acid, activation of extracellular signal related kinase 1 and 2, thus being involved in pathenogenesis of cancer via enhanced cell proliferation
-
-
?
additional information
?
-
-
increasing activity in the order: 1-monoacylglycerol, 2-monoacylglycerol, 1,2-diacylglycerol
-
-
?
additional information
?
-
-
when saturated fatty acids are present the order of decreasing activity varies directly with increasing chain length for C10 to C20
-
-
?
additional information
?
-
-
a single enzyme may function as diacylglycerol and monoacylglycerol kinase
-
-
?
additional information
?
-
-
in addition to its main activity, phosphorylation of 1,2-diacyl-sn-glycerol to 1,2-diacyl-sn-glycerol 3-phosphate, EC 2.7.1.107, the enzyme also shows acylglycerol kinase activity, EC 2.7.1.94. The 2-MGK activity is very low
-
-
?
additional information
?
-
-
in addition to its main activity, phosphorylation of 1,2-diacyl-sn-glycerol to 1,2-diacyl-sn-glycerol 3-phosphate, EC 2.7.1.107, the enzyme also shows acylglycerol kinase activity, EC 2.7.1.94. The 2-MGK activity is very low
-
-
?
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ATP + acylglycerol
ADP + acyl-sn-glycerol 3-phosphate
ATP + acylglycerol
ADP + lysophosphatidic acid
ATP + diacylglycerol
ADP + phosphatidic acid
-
-
i.e. diacyl-glycerol 3-phosphate, regulation mechanism, overview
-
?
ATP + monoacylglycerol
ADP + lysophosphatidic acid
additional information
?
-
ATP + acylglycerol
ADP + acyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + acylglycerol
ADP + acyl-sn-glycerol 3-phosphate
-
-
-
-
?
ATP + acylglycerol
ADP + acyl-sn-glycerol 3-phosphate
-
-
-
?
ATP + acylglycerol
ADP + lysophosphatidic acid
-
-
-
?
ATP + acylglycerol
ADP + lysophosphatidic acid
-
-
-
-
?
ATP + acylglycerol
ADP + lysophosphatidic acid
-
-
-
?
ATP + monoacylglycerol
ADP + lysophosphatidic acid
-
-
i.e. acyl-sn-glycerol 3-phosphate, regulation mechanism, overview
-
?
ATP + monoacylglycerol
ADP + lysophosphatidic acid
-
-
-
?
additional information
?
-
-
lysophosphatidic acid induces the cytokine interleukin-8 correlated with angiogenesis, tumorigenicity, and cancer cell proliferation, the enzyme modulates cross talk with EGFR in prostate cancer cells, enzyme regulates the synthesis of the bioactive phospholipids lysophosphatidic acid and phosphatidic acid, activation of extracellular signal related kinase 1 and 2, thus being involved in pathenogenesis of cancer via enhanced cell proliferation
-
-
?
additional information
?
-
-
the enzyme plays a critical role in epidermal growth factor-induced mitogenesis of prostate cancer cells via EGF and IFG-II, and lysophosphatidic acid, the first way can be inhibited by enzyme suppression, the second cannot, enzyme function and regulation in initiation and progression of prostate cancer, lysophosphatidic acid enhances surival and suppresses apoptosis by reducing levels of the apoptosis-promoting protein Bax, and is involved in signal transduction pathways, overview
-
-
?
additional information
?
-
-
the enzyme modulates cross talk with EGFR in prostate cancer cells, enzyme regulates the synthesis of the bioactive phospholipids lysophosphatidic acid and phosphatidic acid, activation of extracellular signal related kinase 1 and 2, thus being involved in pathenogenesis of cancer via enhanced cell proliferation
-
-
?
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Acidosis, Lactic
Lack of the mitochondrial protein acylglycerol kinase causes Sengers syndrome.
acylglycerol kinase deficiency
Disorders of phospholipids, sphingolipids and fatty acids biosynthesis: toward a new category of inherited metabolic diseases.
Barth Syndrome
Disorders of phospholipids, sphingolipids and fatty acids biosynthesis: toward a new category of inherited metabolic diseases.
Breast Neoplasms
Acylglycerol kinase promotes cell proliferation and tumorigenicity in breast cancer via suppression of the FOXO1 transcription factor.
Carcinogenesis
Acylglycerol kinase functions as an oncogene and an unfavorable prognostic marker of human gliomas.
Carcinoma
Acylglycerol kinase promotes the proliferation and cell cycle progression of oral squamous cell carcinoma.
Carcinoma
Acylglycerol kinase promotes tumour growth and metastasis via activating the PI3K/AKT/GSK3? signalling pathway in renal cell carcinoma.
Carcinoma, Renal Cell
Acylglycerol kinase promotes tumour growth and metastasis via activating the PI3K/AKT/GSK3? signalling pathway in renal cell carcinoma.
Cardiomyopathies
Disorders of phospholipids, sphingolipids and fatty acids biosynthesis: toward a new category of inherited metabolic diseases.
Cardiomyopathy, Hypertrophic
Acylglycerol Kinase Mutated in Sengers Syndrome Is a Subunit of the TIM22 Protein Translocase in Mitochondria.
Cardiomyopathy, Hypertrophic
Lack of the mitochondrial protein acylglycerol kinase causes Sengers syndrome.
Cataract
Acylglycerol Kinase Mutated in Sengers Syndrome Is a Subunit of the TIM22 Protein Translocase in Mitochondria.
Cataract
Identification of a truncation mutation of the acylglycerol kinase (AGK) gene in a novel autosomal recessive cataract locus.
Cataract
Lack of the mitochondrial protein acylglycerol kinase causes Sengers syndrome.
choline kinase deficiency
Disorders of phospholipids, sphingolipids and fatty acids biosynthesis: toward a new category of inherited metabolic diseases.
Diabetic Retinopathy
Expression of autotaxin and acylglycerol kinase in proliferative vitreoretinal epiretinal membranes.
Diabetic Retinopathy
Expression of lysophosphatidic acid, autotaxin and acylglycerol kinase as biomarkers in diabetic retinopathy.
Epiretinal Membrane
Expression of autotaxin and acylglycerol kinase in proliferative vitreoretinal epiretinal membranes.
Glioma
Acylglycerol kinase functions as an oncogene and an unfavorable prognostic marker of human gliomas.
Lymphatic Metastasis
Overexpression of acylglycerol kinase is associated with poorer prognosis and lymph node metastasis in nasopharyngeal carcinoma.
Metabolism, Inborn Errors
Protein moonlighting in inborn errors of metabolism: the case of the mitochondrial acylglycerol kinase.
Muscular Diseases
Acylglycerol Kinase Mutated in Sengers Syndrome Is a Subunit of the TIM22 Protein Translocase in Mitochondria.
Muscular Diseases
Lack of the mitochondrial protein acylglycerol kinase causes Sengers syndrome.
Muscular Dystrophies
Disorders of phospholipids, sphingolipids and fatty acids biosynthesis: toward a new category of inherited metabolic diseases.
Myoglobinuria
Disorders of phospholipids, sphingolipids and fatty acids biosynthesis: toward a new category of inherited metabolic diseases.
Nasopharyngeal Carcinoma
Acylglycerol kinase promotes paclitaxel resistance in nasopharyngeal carcinoma cells by regulating FOXM1 via the JAK2/STAT3 pathway.
Nasopharyngeal Carcinoma
Acylglycerol kinase promotes the stemness of nasopharyngeal carcinoma cells by promoting ?-catenin translocation to the nucleus through activating PI3K/Akt pathway.
Nasopharyngeal Carcinoma
Overexpression of acylglycerol kinase is associated with poorer prognosis and lymph node metastasis in nasopharyngeal carcinoma.
Neoplasm Metastasis
Acylglycerol kinase promotes tumour growth and metastasis via activating the PI3K/AKT/GSK3? signalling pathway in renal cell carcinoma.
Neoplasm Metastasis
Overexpression of acylglycerol kinase is associated with poorer prognosis and lymph node metastasis in nasopharyngeal carcinoma.
Neoplasms
Acylglycerol kinase functions as an oncogene and an unfavorable prognostic marker of human gliomas.
Neoplasms
Acylglycerol kinase is over-expressed in early-stage cervical squamous cell cancer and predicts poor prognosis.
Neoplasms
Acylglycerol kinase promotes cell proliferation and tumorigenicity in breast cancer via suppression of the FOXO1 transcription factor.
Neoplasms
Acylglycerol kinase promotes the proliferation and cell cycle progression of oral squamous cell carcinoma.
Neoplasms
Acylglycerol kinase promotes the stemness of nasopharyngeal carcinoma cells by promoting ?-catenin translocation to the nucleus through activating PI3K/Akt pathway.
Neoplasms
Acylglycerol kinase promotes tumour growth and metastasis via activating the PI3K/AKT/GSK3? signalling pathway in renal cell carcinoma.
Neoplasms
Expression of autotaxin and acylglycerol kinase in prostate cancer: association with cancer development and progression.
Neoplasms
Gene expression profiles of lysophosphatidic acid-related molecules in the prostate: relevance to prostate cancer and benign hyperplasia.
Neoplasms
Overexpression of acylglycerol kinase is associated with poorer prognosis and lymph node metastasis in nasopharyngeal carcinoma.
Neoplasms, Squamous Cell
Acylglycerol kinase is over-expressed in early-stage cervical squamous cell cancer and predicts poor prognosis.
Paraplegia
Disorders of phospholipids, sphingolipids and fatty acids biosynthesis: toward a new category of inherited metabolic diseases.
Peripheral Nervous System Diseases
Disorders of phospholipids, sphingolipids and fatty acids biosynthesis: toward a new category of inherited metabolic diseases.
Prostatic Neoplasms
A novel acylglycerol kinase that produces lysophosphatidic acid modulates cross talk with EGFR in prostate cancer cells.
Prostatic Neoplasms
Critical role of acylglycerol kinase in epidermal growth factor-induced mitogenesis of prostate cancer cells.
Prostatic Neoplasms
Expression of autotaxin and acylglycerol kinase in prostate cancer: association with cancer development and progression.
Squamous Cell Carcinoma of Head and Neck
Acylglycerol kinase promotes the proliferation and cell cycle progression of oral squamous cell carcinoma.
Stomach Neoplasms
Up-regulated acylglycerol kinase (AGK) expression associates with gastric cancer progression through the formation of a novel YAP1-AGK-positive loop.
Vitreoretinopathy, Proliferative
Expression of autotaxin and acylglycerol kinase in proliferative vitreoretinal epiretinal membranes.
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metabolism
the enzyme has a dual function in protein translocation and lipid biosynthesis
evolution
-
comprehensive analysis on the 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities 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 (lambda 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
evolution
-
comprehensive analysis on the 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities 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
evolution
-
comprehensive analysis on the 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities 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
evolution
-
comprehensive analysis on the 1-monoacylglycerol kinase (1-MGK) and 2-monoacylglycerol kinase (2-MGK) activities 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
cell proliferation and cell cycle progression of an established voral squamous cell carcinoma cell, OSCC, cell line are decreased following enzyme AGK knockdown, and are enhanced by enzyme AGK overexpression in vitro. Aberrant AGK expression in OSCC is associated with cell proliferation and cell cycle progression. Knockdown of AGK results in reduced mRNA and protein expression levels of cyclin D1 and p-Rb, whereas the expression levels of p21 are increased
malfunction
enzyme overexpression significantly enhances, whereas silencing endogenous enzyme AGK inhibits the proliferation and tumorigenicity of breast cancer cells both in vitro and in vivo. Overexpression of AGK enhances G1-S phase transition in breast cancer cells, which is associated with activation of AKT, suppression of FOXO1 transactivity, downregulation of cyclin-dependent kinase inhibitors p21Cip1 and p27Kip1 and upregulation of the cell cycle regulator cyclin D1
malfunction
-
presence or absence of 1-MGK and 2-MGK activities may be essential to the pathophysiological functions of each DGK isozyme
malfunction
-
presence or absence of 1-MGK and 2-MGK activities may be essential to the pathophysiological functions of each DGK isozyme
malfunction
-
presence or absence of 1-MGK and 2-MGK activities may be essential to the pathophysiological functions of each DGK isozyme
malfunction
silencing the expression of the enzyme dramatically suppresses cell proliferation, migration and invasion of glioma cells in vitro
malfunction
the mutated enzyme is associated with Sengers syndrome
physiological function
acylglycerol kinase (AGK) is a multisubstrate lipid kinase, that catalyzes the production of lysophosphatidic acid and phosphatidic acid from monoacylglycerol and diacylglycerol. Acylglycerol kinase augments JAK2/STAT3 signaling in esophageal squamous cells, the enzyme AGK directly interacts with the JH2 domain to relieve inhibition of JAK2 and activate JAK2/STAT3 signaling. AGK levels significantly correlate with increased STAT3 phosphorylation, poorer disease-free survival, and shorter overall survival in primary esophageal squamous cell cancer cell, and AGK expression is significantly correlated with JAK2/STAT3 hyperactivation in esophageal squamous cell cancer cell, as well as in lung and breast cancer. Overexpression of AGK leads to activation of EGF receptor and promotes the proliferation and migration of prostate cancer cells, suggesting that AGK might act as a potent oncogene. AGK enhances JAK2 activity by blocking JH2-mediated autoinhibition of JAK2. Solid tumor cells override the autoinhibitory effect of JH2 to maintain activation of JAK2/STAT3 signaling, mechanism, overview. Enzyme AGK is a JH2 domain-interacting protein that activates the JAK2/STAT3 pathway
physiological function
acylglycerol kinase contributes to cancer progression and unfavorable clinical outcomes of patients with early-stage cervical squamous cell cancer. Early-stage cervical squamous cell cancer patients with high AGK expression level had shorter progress-free survival and overall survival time compared with patients with low AGK expression levels
physiological function
acylglycerol kinase is a multisubstrate lipid kinase, that is associated with the progression of various types of human cancer, it promotes proliferation and cell cycle progression of oral squamous cell carcinoma. Overexpression of AGK results in upregulation of the protein and mRNA expression levels of cyclin D1, and increases the expression levels of p-Rb, while p21 expression levels are downregulated. The enzyme may promote malignant cancer growth by regulating the expression of cyclin D1 and p21, during the G1-S phase transition
physiological function
acylglycerol kinase promotes cell proliferation and tumorigenicity in breast cancer via suppression of the FOXO1 transcription factor, FOXO1 is considered to be a tumor suppressor. The enzyme significantly correlates with patients' clinicopathologic characteristics, including clinical stage and tumor-nodule-metastasis (TNM) classification
physiological function
by acting as a lipid kinase, AGK catalyzes the phosphorylation of acylglycerol to generate lysophosphatidic acid , which is known to be involved in tumor progression, invasion, neovascularization, and metastasis. Overexpression of acylglycerol kinase is associated with poorer prognosis and lymph node metastasis in nasopharyngeal carcinoma. High expression of enzyme AGK is associated with significantly shorter overall and disease-free survival and is an independent prognostic factor for overall survival. High AGK expression is associated with lymph node metastasis and is an independent predicted factor for lymph node metastasis in nasopharyngeal carcinoma
physiological function
the enzyme is required for CD8+ T cell expansion, antitumor function and regulates CD8+ T cell glycolysis and activation of phosphatidylinositol-3-OH kinase-mammalian target of rapamycin. Enzyme-triggered PTEN inactivation promotes a CD8+ T cell metabolic switch
physiological function
the enzyme plays an important role in the viability and motility of glioma cells. Enzyme upregulation is involved into glioma development and progression
physiological function
the kinase activity of the enzyme is dispensable for protein import but required for the structural integrity of mitochondria and apoptotic resistance. The enzyme functions as a subunit of the carrier translocase TIM22 complex independent of its kinase activity. The enzyme mutated in Sengers syndrome is a subunit of the TIM22 complex. The enzyme is required for the import of membrane proteins ANT1 and SLC25A24 into mitochondria
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drug development
the enzyme AGK-based mechanism for constitutive activation of JAK2/STAT3 signaling in solid tumors and may represent a therapeutic target
diagnostics
early-stage cervical squamous cell cancer (CSCC) patients with high AGK expression level had shorter progress-free survival and overall survival time compared with patients with low AGK expression levels, AGK expression level can be an independent prognostic factor for survival of early-stage CSCC patients
diagnostics
overexpression of acylglycerol kinase is associated with poorer prognosis and lymph node metastasis in nasopharyngeal carcinoma and thus the enzyme has potential as a prognostic factor for overall survival in in nasopharyngeal carcinoma, and for lymph node metastasis in nasopharyngeal carcinoma
diagnostics
the enzyme AGK-based mechanism for constitutive activation of JAK2/STAT3 signaling in solid tumors and may represent a prognostic biomarker. AGK overexpression correlates with progression and poor prognosis in human esophageal squamous cell cancer cells
medicine
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homozygous mutation c.3G>A, p.M1I in the gene encoding acylglycerol kinase has been identified in two brothers who presented with vascular strokes, lactic acidosis, cardiomyopathy and cataracts, abnormal muscle cell histopathology and mitochondrial function. One proband had very abnormal mitochondria with citrate synthase crystals visible in electron micrographs, associated with markedly high citrate synthase activity. Homozygous c.979A>T, p.K327* mutation has been identified in a family with four affected members, of which two have been examined. They presented with similar clinical symptoms, but no strokes. Postmortem heart and skeletal muscle tissues showed low complex I, III and IV activities in the heart, but normal in the muscle. Skin fibroblasts showed elevated lactate/pyruvate ratios and low complex I+III activity
medicine
identification of a novel autosomal recessive cataract locus on 7q33-q36.1 in a multiplex consanguineous family with isolated congenital cataractl. Mutation is a splice-site mutation in AGK, encoding acylglycerol kinase, which leads to aberrant splicing and predicted premature truncation
medicine
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in membranes from patients with proliferative diabetic retinopathy, vascular endothelial cells express autotaxin and acylglycerol kinase in 16 and 19 out of 22 membranes, respectively. Stromal cells express autotaxin and acylglycerol kinase in 19 and 22 out of membranes, respectively. There are significant correlations between number of blood vessels expressing the panendothelial cell marker CD34 and number of blood vessels and stromal cells expressing autotaxin and acylglycerol kinase. In proliferative diabetic retinopathy membranes, spindle-shaped myofibroblasts expressing alpha-smooth muscle actin co-express autotaxin, acylglycerol kinase and LPA1 receptor
medicine
high enzyme expression is significantly associated with the grade of malignancy and poor prognosis in glioma patients. The enzyme is a therapeutic target for treatment of glioma
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