Repositioning Candidate Details
| Candidate ID: | R0032 |
| Source ID: | DB00114 |
| Source Type: | approved; investigational; nutraceutical |
| Compound Type: | small molecule |
| Compound Name: | Pyridoxal phosphate |
| Synonyms: | 3-hydroxy-2-methyl-5-((phosphonooxy)methyl)-4-pyridinecarboxaldehyde; 3-hydroxy-5-(hydroxymethyl)-2-methylisonicotinaldehyde 5-phosphate; Codecarboxylase; PLP; Pyridoxal 5-monophosphoric acid ester; Pyridoxal 5-phosphate; Pyridoxal 5'-phosphate; Pyridoxal P; Pyridoxal phosphate anhydrous; Pyridoxal-5P; Pyridoxal-P |
| Molecular Formula: | C8H10NO6P |
| SMILES: | CC1=NC=C(COP(O)(O)=O)C(C=O)=C1O |
| Structure: |
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| DrugBank Description: | 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). |
| CAS Number: | 54-47-7 |
| Molecular Weight: | 247.1419 |
| DrugBank Indication: | For nutritional supplementation and for treating dietary shortage or imbalance. |
| DrugBank Pharmacology: | 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. |
| DrugBank MoA: | 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. Pyridoxal phosphate 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. |
| Targets: | Alanine--glyoxylate aminotransferase 2, mitochondrial cofactor; Glutamate decarboxylase 1 cofactor; Cystathionine beta-synthase cofactor; Kynureninase cofactor; Serine hydroxymethyltransferase, cytosolic cofactor; Cysteine desulfurase, mitochondrial cofactor; Aspartate aminotransferase, cytoplasmic activator; Ornithine aminotransferase, mitochondrial cofactor; Ornithine decarboxylase cofactor; Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial cofactor; 4-aminobutyrate aminotransferase, mitochondrial inhibitor; Pyridoxine-5'-phosphate oxidase cofactor; Sphingosine-1-phosphate lyase 1 cofactor; Tyrosine aminotransferase cofactor; Kynurenine--oxoglutarate transaminase 1 cofactor; Glycogen phosphorylase, liver form cofactor; Serine palmitoyltransferase 2 cofactor; Cysteine sulfinic acid decarboxylase cofactor; Histidine decarboxylase cofactor; Arginine decarboxylase cofactor; L-serine dehydratase/L-threonine deaminase cofactor; 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial cofactor; Glycine dehydrogenase [decarboxylating], mitochondrial cofactor; Alanine aminotransferase 1 cofactor; Phosphoserine aminotransferase cofactor; 5-aminolevulinate synthase, nonspecific, mitochondrial cofactor; Serine--pyruvate aminotransferase cofactor; Pyridoxal phosphate phosphatase cofactor; Serine palmitoyltransferase 1 cofactor; Cystathionine gamma-lyase cofactor; Branched-chain-amino-acid aminotransferase, cytosolic cofactor; Branched-chain-amino-acid aminotransferase, mitochondrial cofactor; Proline synthase co-transcribed bacterial homolog protein binder; Aspartate aminotransferase, mitochondrial cofactor; Glycogen phosphorylase, brain form cofactor; Glycogen phosphorylase, muscle form cofactor; Aromatic-L-amino-acid decarboxylase cofactor; Aspartate aminotransferase cofactor; Serine hydroxymethyltransferase cofactor; Selenocysteine lyase variant cofactor; Phosphorylase cofactor; 5-aminolevulinate synthase cofactor; Glutamate decarboxylase 2 (Pancreatic islets and brain, 65kDa) cofactor; DDC protein cofactor; Kynurenine--oxoglutarate transaminase 3 cofactor; Glutamate decarboxylase-like protein 1 cofactor; Selenocysteine lyase cofactor; Immunoglobulin superfamily member 10 cofactor; 5-phosphohydroxy-L-lysine phospho-lyase cofactor; Glutamate decarboxylase 1 (Brain, 67kDa) cofactor; Serine hydroxymethyltransferase, mitochondrial cofactor; 5-aminolevulinate synthase, erythroid-specific, mitochondrial cofactor; Alanine aminotransferase 2 cofactor; Molybdenum cofactor sulfurase cofactor; Serine dehydratase-like cofactor; Hepatic peroxysomal alanine:glyoxylate aminotransferase cofactor; Serine racemase cofactor; O-phosphoseryl-tRNA(Sec) selenium transferase cofactor; Serine palmitoyltransferase 3 cofactor; Glutamic acid decarboxylase cofactor; Alanine-glyoxylate aminotransferase homolog cofactor |
| Inclusion Criteria: | Indication associated |
| Strategy ID | Strategy | Synonyms | Related Targets | Related Drugs |
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| Diseases ID | DO ID | Disease Name | Definition | Class | |
|---|---|---|---|---|---|
| I02 | 5113 | Nutritional deficiency disease | A nutrition disease that is characterized by deficiency of a nutritional element, such as a vitamin, mineral, carbohydrate, protein, fat, or general energy content. https://medlineplus.gov/malnutrition.html | disease of metabolism/acquired metabolic disease/nutrition disease | Details |