Glycerol kinase Protein (His Tag), recombinant E.coli

Activity: Measured by its ability to transfer phosphate from ATP to glycerol. The specific activity is > 200U/mg protein, as measured under the described conditions. Protein Construction: A DNA sequence encoding the Escherichia coli Glycerol kinase (2T-502E) was expressed with a polyhistidine tag at the N-terminus and C-terminus. Sequence: Thr2-Glu502. Fusion tag: N-His & C-His Endotoxin: Please contact us for more information. Apparent Molecular Mass: 55-58kDa. Protein function: Glycerol kinase from E. coli (glpK) catalyzes the ATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate (G3P), the first and rate-limiting step in the utilization of glycerol. In the presence of glycerol, glpK is stimulated by interaction with the membrane-bound glycerol facilitator. In the presence of glucose, glpK activity is allosterically inhibited by fructose-1,6-bisphosphate (FBP) of the glycolytic pathway. Under physiological conditions, the enzyme is in an equilibrium between the active dimer and the inactive tetramer. FBP binds to and stabilizes the inactive form, therefore shifting the usage of glycerol metabolic pathway to glycolytic pathway. GlpK is a member of a superfamily of ATPases that includes actin, hexokinase and the heat shock protein hsc70. Although these proteins are dissimilar in amino acid sequence and function, they share similar tertiary folds and likely the same catalytic mechanism. The enzyme activity was measured using a phosphatase-coupled kinase assay. Protein function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only ATP. [The UniProt Consortium]