EC Number   |
General Information |
Reference |
|---|
    2.7.1.30 | evolution |
although there are two African human pathogenic Trypanosoma subspecies: Trypanosoma brucei gambiense (Tbg) and Trypanosoma brucei rhodesiense (Tbr), it is reported in that the amino acid sequences of their GKs are exactly identical. Hence, TbgGK represents the glycerol kinase of both subspecies |
760620 |
| 2.7.1.30 | evolution |
Bacteria and Eukarya have cell membranes with sn-glycerol-3-phosphate (G3P), whereas archaeal membranes contain sn-glycerol-1-phosphate (G1P). Determining the time at which cells with either G3P-lipid membranes or G1P-lipid membranes appeared is important for understanding the early evolution of terrestrial life. Reconstructed molecular phylogenetic trees of G1PDH (G1P dehydrogenase, EgsA/AraM), which is responsible for G1P synthesis and G3PDHs (G3P dehydrogenase, GpsA and GlpA/GlpD), and glycerol kinase (GlpK), which is responsible for G3P synthesis. Together with the distribution of these protein-encoding genes among archaeal and bacterial groups, phylogenetic analyses suggest that GlpA/GlpD in the Commonote (the last universal common ancestor of all extant life with a cellular form, Commonote commonote) acquired EgsA (G1PDH) from the archaeal common ancestor (Commonote archaea) and acquired GpsA and GlpK from a bacterial common ancestor (Commonote bacteria). The Commonote probably possessed a G3P-lipid membrane synthesized enzymatically, after which the archaeal lineage acquires G1PDH followed by the replacement of a G3P-lipid membrane with a G1P-lipid membrane. Detailed overview |
760456 |
| 2.7.1.30 | evolution |
both Gykl1 and Gk2 are thought to have arisen by the transposition of Gk located on the X chromosome, and have high homology with Gk. But both Gykl1 and Gk2 show testis-specific expression, and the proteins have no glycerol kinase activity in vitro, unlike GK and GK5 |
761751 |
| 2.7.1.30 | evolution |
glycerol kinase is a member of the ATPase superfamily, which includes hexokinase, actin, and heat shock protein. These share a common betabetabetaalphabetaalphabetaalpha folding motif and markedly change conformation upon substrate binding because of interdomain motion |
-, 761561 |
| 2.7.1.30 | malfunction |
a glycerol kinase knockout strain is incapable to grow on glycerol and shows higher NADPH-dependent xylitol production compared to the wild type strain |
-, 721849 |
| 2.7.1.30 | malfunction |
frequently observed variation in the glpK coding sequence produces a drug-tolerant phenotype that can reduce antibiotic efficacy and may contribute to the evolution of resistance. Common variation in a homopolymeric region in the glpK gene is associated with drug resistance in clinical isolates. Glycerol catabolic defects are associated with extensive drug resistance in Korea. A panel of Korean Mycobacterium tuberculosis isolates that vary in drug sensitivity profiles, from fully sensitive strains to extensively evolved clones that are phenotypically resistant to more than ten different antibiotics. GlpK frameshift mutations are common in Mycobacterium tuberculosis isolates and associated with drug resistance in Peru |
-, 761788 |
| 2.7.1.30 | malfunction |
Gk2-deficient mice show male infertility with disordered mitochondrial sheath formation. Gk2 disrupted mice are male infertile because their spermatozoa cannot pass through the uterotubal junction (UTJ) due to reduced motility. Disorganization of the mitochondrial sheath occurs in glycerol kinase 2 (Gk2) disrupted mice |
761751 |
| 2.7.1.30 | malfunction |
overexpression of glycerol kinase GlcA bypasses the requirement of glycerol-3-phosphate dehydrogenase (EC 1.1.1.8), encoded by gene gfdA, in glucose media for colony growth. The DELTAgfdADELTAglcA double mutant shows an exacerbation of colony defects in both glucose and glycerol media |
-, 761192 |
| 2.7.1.30 | malfunction |
overexpression of glycerol kinase under oxidative stress with glycerol supplementation leads to enhancement of lipid production in Synechocystis sp. PCC 6803 |
760718 |
| 2.7.1.30 | malfunction |
silencing GK5 in PC9R cells induces mitochondrial damage, caspase activation, cell cycle arrest, and apoptosis via SREBP1/SCD1 signaling pathway. The exosomal mRNA of GK5 in the plasma of patients with gefitinib-resistant adenocarcinoma is significantly higher compared with that of gefitinib-sensitive patients. GK5 knockdown induces PC9R cell apoptosis and cell cycle arrest in the presence of gefitinib, as well as PC9R cell mitochondrial dysfunction and caspase activation. GK5 knockdown suppresses tumor proliferation in vivo |
761627 |
