Benfotiamine raises the blood level of thiamine pyrophosphate (TPP), the biologically active co-enzyme of thiamine. Thiamine and its co-enzyme, TPP thiamine (vitamin B1) plays an essential part in the metabolism of glucose, through actions of it co-enzyme TPP (thiamine pyrophosphate). TPP is formed by the enzymatically catalyzed addition of two phosphate groups donated by ATP to thiamine. TPP also goes by the name thiamine diphosphate. In the cytoplasm of the cell, glucose, a 6-carbon sugar, is metabolized to pyruvic acid, which is converted into acetyl-CoA, otherwise known as active acetate. Acetyl CoA enters the mitochondrion, where it serves as the starting substrate in the Kreb’s cycle citric acid cycle. The Krebs cycle is the primary source of cellular metabolic energy. TPP, along with other co-enzymes, is essential for the removal of CO2 from pyruvic acid, which in turn is a key step in the conversion of pyruvic acid to acetyl CoA. CO2 removal from pyruvic acid is called oxidative decarboxylation and for this reason, TPP was originally referred to as cocarboxylase. TPP is thus vital to the cell’s energy supply. Benfotiamine helps maintain healthy cells in the presence of blood glucose. Acting as a biochemical super-thiamin, it does this through several different cellular mechanisms, as discussed below. Benfotiamine and glucose metabolism benfotiamine normalizes cellular processes fueled by glucose metabolites. As long as glucose remains at normal levels, excess glucose metabolites do not accumulate within the cell. The bulk of the cell’s glucose supply is converted to pyruvic acid, which serves as substrate for production of acetyl CoA, the primary fuel for the krebs cycle. Of the total amount of metabolic energy (in the form of ATP) released from food, the Krebs cycle generates about 90 percent.
- Belonging to the family of compounds knows as allithiamines
- Benfotiamine is fat-soluble and more bioavailable and physiologically active than thiamin
- Helps maintain healthy cells in the presence of blood glucose
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