EC Number   |
General Information |
Reference |
|---|
   2.7.1.94 | 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 |
737779 |
| 2.7.1.94 | 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 |
737779 |
| 2.7.1.94 | 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 |
739084 |
| 2.7.1.94 | 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 |
739046 |
| 2.7.1.94 | malfunction |
presence or absence of 1-MGK and 2-MGK activities may be essential to the pathophysiological functions of each DGK isozyme |
737779 |
| 2.7.1.94 | malfunction |
silencing the expression of the enzyme dramatically suppresses cell proliferation, migration and invasion of glioma cells in vitro |
761230 |
| 2.7.1.94 | malfunction |
the mutated enzyme is associated with Sengers syndrome |
762499 |
| 2.7.1.94 | metabolism |
the enzyme has a dual function in protein translocation and lipid biosynthesis |
762499 |
| 2.7.1.94 | 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 |
738754 |
| 2.7.1.94 | 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 |
739742 |
