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Vitamin B 6 Drug class Pyridoxal 5'-phosphate, the metabolically active form of vitamin B 6 Class identifiers Use Vitamin B 6 deficiency ATC code A11H Biological target enzyme cofactor Clinical data Drugs.com International Drug Names External links MeSH D025101 Legal status In Wikidata Vitamin B 6 is one of the B vitamins, and is an essential nutrient for humans. The term essential nutrient ...
Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B 6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. [ 5 ]
Pyridoxine, pyridoxal, pyridoxamine: The active form pyridoxal 5'-phosphate (PLP) (depicted) serves as a cofactor in many enzyme reactions mainly in amino acid metabolism including biosynthesis of neurotransmitters. [17] Vitamin B 7: Biotin: Biotin plays a key role in the metabolism of lipids, proteins and carbohydrates.
Pyridoxine (PN) [4] is a form of vitamin B 6 found commonly in food and used as a dietary supplement.As a supplement it is used to treat and prevent pyridoxine deficiency, sideroblastic anaemia, pyridoxine-dependent epilepsy, certain metabolic disorders, side effects or complications of isoniazid use, and certain types of mushroom poisoning. [5]
The enzyme pyridoxal phosphatase [1] [2] [3] (EC 3.1.3.74) catalyzes the reaction pyridoxal 5′-phosphate + H 2 O pyridoxal + phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is pyridoxal-5′-phosphate phosphohydrolase.
Pyridoxine 5′-phosphate oxidase is an enzyme, encoded by the PNPO gene, [1] [2] [3] that catalyzes several reactions in the vitamin B 6 metabolism pathway. Pyridoxine 5′-phosphate oxidase catalyzes the final, rate-limiting step in vitamin B 6 metabolism, the biosynthesis of pyridoxal 5′-phosphate, the biologically active form of vitamin B 6 which acts as an essential cofactor. [4]
Aspartate transaminase (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or (serum) glutamic oxaloacetic transaminase (GOT, SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2.6.1.1) that was first described by Arthur Karmen and colleagues in 1954.
Glycogen phosphorylase has a pyridoxal phosphate (PLP, derived from Vitamin B 6) at each catalytic site. Pyridoxal phosphate links with basic residues (in this case Lys680) and covalently forms a Schiff base. Once the Schiff base linkage is formed, holding the PLP molecule in the active site, the phosphate group on the PLP readily donates a ...