Himitan
Himitan Uses, Dosage, Side Effects, Food Interaction and all others data.
This is the active form of vitamin B6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (pyridoxamine).
The two major forms of vitamin B6 are pyridoxine and pyridoxamine. In the liver they are converted to pyridoxal phosphate (PLP) which is a cofactor in many reactions of amino acid metabolism. PLP also is necessary for the enzymatic reaction governing the release of glucose from glycogen. Pyroluria is one potential cause of vitamin B6 deficiency.
Trade Name | Himitan |
Generic | Pyridoxal phosphate |
Pyridoxal phosphate Other Names | Codecarboxylase, Pyridoxal 5-phosphate, Pyridoxal 5'-phosphate, Pyridoxal P, Pyridoxal-5P, Pyridoxal-P |
Type | |
Formula | C8H10NO6P |
Weight | Average: 247.1419 Monoisotopic: 247.024573569 |
Groups | Approved, Investigational, Nutraceutical |
Therapeutic Class | |
Manufacturer | |
Available Country | |
Last Updated: | September 19, 2023 at 7:00 am |
Uses
Himitan is a vitamin available in many formulations to correct vitamin B6 deficiency.
For nutritional supplementation and for treating dietary shortage or imbalance.
Himitan is also used to associated treatment for these conditions: Anemia, Pernicious, Vitamin B6 Deficiency, Folate supplementation therapy, Vitamin supplementation
How Himitan works
Pyridoxal Phosphate is a coenzyme of many enzymatic reactions. It is the active form of vitamin B6 which comprises three natural organic compounds, pyridoxal, pyridoxamine and pyridoxine. Himitan acts as a coenzyme in all transamination reactions, and in some oxylation and deamination reactions of amino acids. The aldehyde group of pyridoxal phosphate forms a Schiff-base linkage with the epsilon-amino group of a specific lysine group of the aminotransferase enzyme. The alpha-amino group of the amino acid substrate displaces the epsilon-amino group of the active-site lysine residue. The resulting aldimine becomes deprotonated to become a quinoid intermediate, which in turn accepts a proton at a different position to become a ketimine. Ketimine becomes hydrolyzed so that the amino group remains on the protein complex.
Food Interaction
No interactions found.Innovators Monograph
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