Glycerokinase from Escherichia coli

Research Area: Cell Signaling
Glycerol kinase (GK) is a member of the FGGY carbohydrate kinase family (ATP: glycerol 3-phosphotransferase), which is responsible for transferring a phosphate group from ATP to glycerol.

Glycerol kinase (glpK) was used to study the effects of pain controlling neuropeptides on human fat cell lipolysis.

Glycerol kinase has been used along with adenosine triphosphate (ATP) for the conversion of glycerol to glycerol-3 phosphate (glycerol-3P) in white adipose tissue (WAT) adipocyte samples by label distribution method. It has also been used along with adenosine triphosphate (ATP) in the derivatization of glycerol to sn-glycerol-3 phosphate (glycerol-3P).

Glycerol kinase (GK), the primary enzyme involved in regulating glycerol uptake and its metabolism, was initially identified in E. coli. This enzyme acts as a catalyst in the Mg²⁺-ATP-dependent phosphorylation of glycerol to produce G3P, a crucial intermediate in various metabolic pathways, including the synthesis of glycerolipids and triglycerides, as well as glycogenesis, glycolysis, and gluconeogenesis.
GK participates in the glycerol 3-phosphate shuttle and, in conjunction with glycerol 3-phosphate dehydrogenase, converts glycerol into dihydroxyacetone phosphate. It plays a pivotal role in plasma glycerol withdrawal, glycerol utilization by different tissues, and in maintaining carbohydrate homeostasis. GK is positioned at the nexus of lipid and carbohydrate metabolism and may play a potential role in type 2 diabetes mellitus (T2DM).

Glycerol kinase catalyzes tge MgATP-dependent phosphorylation of glycerol to produce sn-glycerol-3-phosphate and is the rate limiting enzyme in the utilization of glycerol. It is also subject to feedback regulation by fructose-1,6-bisphosphate.

Suspension in 3.1 M (NH₄)₂SO₄ pH 7.3, with 1% BSA and 2% trehalose

One unit will convert 1.0 μmole of glycerol and ATP to L-α-glycerophosphate and ADP per min at pH 9.8 at 25 °C in a coupled system with PK/LDH.