glucose-6-phosphatase

There is some research to support that compounds in the plant inhibit the enzyme glucose-6-phosphatase.

Glucose-6-phosphatase is one of the key liver enzymes involved in regulating sugar metabolism.

Glucose-6-phosphatase is an enzyme located on the inner membrane of the endoplasmic reticulum.

The G6P remains within the liver cell unless the phosphate is cleaved by glucose-6-phosphatase.

Thus glucose-6-phosphatase mediates the final, key, step in both of the two main processes of glucose production during fasting.

The principal metabolic effects of deficiency of glucose-6-phosphatase are:

Liver cells possess glucose-6-phosphatase, which removes the phosphate group from glucose-6-phosphate produced during glycogenolysis or gluconeogenesis.

Glucose-6-phosphatase is an enzyme that in humans is encoded by the G6PC gene.

The smooth endoplasmic reticulum also contains the enzyme glucose-6-phosphatase, which converts glucose-6-phosphate to glucose, a step in gluconeogenesis.

FOXO1, through increasing transcription of glucose-6-phosphatase, indirectly increases the rate of hepatic glucose production.

Next, the phosphoryl group on G6P can be cleaved by glucose-6-phosphatase so that a free glucose can be formed.

This genetic disease results from deficiency of the enzyme glucose-6-phosphatase, and has an incidence in the American population of approximately 1 in 50,000 to 100,000 births.

HNF6 is also involved in regulation of transcription of gluconeogenic enzymes such as glucose-6-phosphatase and phosphoenolpyruvate carboxykinase.

GSD Ia results from mutations of G6PC, the gene for glucose-6-phosphatase.

Because normal brain and muscle cells contain no glucose-6-phosphatase, GSD I causes no other neuromuscular effects.

Most non-autotrophic cells are unable to produce free glucose because they lack expression of glucose-6-phosphatase and, thus, are involved only in glucose uptake and catabolism.

The glucose cycle can occur in liver cells due to a liver specific enzyme glucose-6-phosphatase, which catalyse the dephosphorylation of glucose 6-phosphate back to glucose.

Hexokinase/glucokinase, phosphofructokinase, and pyruvate kinase enzymes of glycolysis are replaced with glucose-6-phosphatase, fructose-1,6-bisphosphatase, and PEP carboxykinase.

Muscle cells lack the enzyme glucose-6-phosphatase, which is required to pass glucose into the blood, so the glycogen they store is destined for internal use and is not shared with other cells.

Acute FGF21 treatment induced hepatic expression of key regulators of gluconeogenesis, lipid metabolism, and ketogenesis including glucose-6-phosphatase, phosphoenol pyruvate carboxykinase, 3-hydroxybutyrate dehydrogenase type 1, and carnitine palmitoyltransferase 1α.

The phosphate group of glucose-6-phosphate is removed by the enzyme glucose-6-phosphatase, which is not present in myocytes, and the free glucose exits the cell via GLUT2 facilitated diffusion channels in the hepatocyte cell membrane.

Very high levels of PC activity, together with high activities of other gluconeogenic enzymes including PEPCK, fructose-1,6-bisphosphatase and glucose-6-phosphatase in liver and kidney cortex, suggest that a primary role of PC is to participate in gluconeogenesis in these organs.