Glycerol Kinase, Recombinant, E. coli, aa1-502 (GK, GK1, GKD, glpK, Glycerokinase)

Blue Ice

5255

Supplied as a liquid in Tris, NaCl, Glycerol, DTT. BSA free.

Glycerol kinase from E. coli (glpK) catalyzes the ATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate (G3P), the first and rate­limiting step in the utilization of glycerol (1). In the presence of glycerol, glpK is stimulated by interaction with the membrane-bound glycerol facilitator (2). In the presence of glucose, glpK activity is allosterically inhibited by fructose-1, 6­bisphosphate (FBP) of the glycolytic pathway (3). 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 (4). glpK is also inhibited by phosphocarrier protein IIAGlc by a regulatory mechanism distinct from that of FBP (5). 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 (6).

Source:
Recombinant protein corresponding to aa1-502 from E. coli Glycerol Kinase, fused at 6-his tag at C-terminal, expressed in E. coli.

Molecular Weight:
~52-55kD

Endotoxin:
<1.0EU/1ug (LAL method)

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.