2.7.1.94: acylglycerol kinase
This is an abbreviated version!
For detailed information about acylglycerol kinase, go to the full flat file.
Word Map on EC 2.7.1.94
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2.7.1.94
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translocase
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intermembrane
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lysophosphatidic
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sengers
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phosphatidic
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monoacylglycerols
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preproteins
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tim10
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polytopic
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presequence
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lpa-induced
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medicine
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autotaxin
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diagnostics
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drug development
- 2.7.1.94
- translocase
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intermembrane
-
lysophosphatidic
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sengers
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phosphatidic
- monoacylglycerols
- preproteins
- tim10
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polytopic
- presequence
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lpa-induced
- medicine
- autotaxin
- diagnostics
- drug development
Reaction
Synonyms
1-MGK, 1-monoacylglycerol kinase, 2-MGK, 2-monoacylglycerol kinase, acylglycerol kinase, AGK, kinase, monoacylglycerol (phosphorylating), MGK, monoacylglycerol kinase, monoglyceride kinase, monoglyceride phosphokinase, More, MULK, multisubstrate lipid kinase, sn-2-monoacylglycerol kinase, TIM22 complex
ECTree
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General Information
General Information on EC 2.7.1.94 - acylglycerol kinase
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evolution
malfunction
metabolism
the enzyme has a dual function in protein translocation and lipid biosynthesis
physiological function
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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
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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
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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
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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
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
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presence or absence of 1-MGK and 2-MGK activities may be essential to the pathophysiological functions of each DGK isozyme
malfunction
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presence or absence of 1-MGK and 2-MGK activities may be essential to the pathophysiological functions of each DGK isozyme
malfunction
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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
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