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Usage

Uses

Used in Pharmaceutical Industry:
Pyridoxal is used as a precursor for the synthesis of pyridoxal 5'-phosphate (PLP), which is the active form of vitamin B6. PLP acts as a coenzyme for numerous enzymes involved in the metabolism of amino acids, lipids, and carbohydrates. It is essential for the proper functioning of the nervous system and the synthesis of neurotransmitters, such as serotonin and dopamine.
Used in Nutritional Supplements:
Pyridoxal is used as a dietary supplement to provide the body with vitamin B6, which is necessary for maintaining good health. It helps in the conversion of food into energy, supports the immune system, and contributes to the production of red blood cells.
Used in Food Industry:
In the food industry, pyridoxal is used as a nutrient fortifier to enhance the vitamin B6 content of various products, such as cereals, bread, and other fortified foods. This helps in ensuring that consumers receive adequate amounts of this essential nutrient in their diet.
Used in Cosmetics Industry:
Pyridoxal is also used in the cosmetics industry as an ingredient in skincare products, particularly those targeting anti-aging and skin rejuvenation. It is believed to help improve skin elasticity, reduce the appearance of fine lines and wrinkles, and promote a more youthful complexion.
Used in Research and Development:
Pyridoxal is utilized in research and development for studying the structure and function of enzymes and other proteins that require vitamin B6 for their activity. It is also used in the synthesis of various pharmaceutical compounds and as a starting material for the production of other related compounds with potential therapeutic applications.

Enzyme inhibitor

This photosensitive aldehyde form of vitamin B6 (FW = 167.16 g/mol), systematically referred to as 3-hydroxy-5-(hydroxymethyl)-2-methyl-4- pyridinecarboxaldehyde, is the immediate precursor to the coenzyme pyridoxal 5’-phosphate (PLP) and is often a weaker competitive inhibitor of PLP binding to PLP-dependent enzymes). Pyridoxal is soluble in water (1 g/2 mL) and sensitive to heat, particularly at alkaline pH. The pKa values are 4.23 (phenol OH), 8.70 (pyridinium NH+), and 13.0. Pyridoxal has a lmax value of 252 nm at pH 7.0 (e = 8200 M–1cm–1). It is typically supplied as the hydrochloride. Target(s): O-acetylhomoserine aminocarboxypropyltransferase, or O-acetylhomoserine (thiol)-lyase; alanine racemase; aldehyde dehydrogenase; arginine decarboxylase; cystathionine b-lyase, or cystine lyase; cysteine synthase; dextransucrase; b-fructofuranosidase, or invertase; glutamate dehydrogenase; hemoglobin S polymerization; hydroxyacyl-glutathione hydrolase, or glyoxalase II; kynurenine 3- monooxygenase; lactoylglutathione lyase, or glyoxalase I; NMN nucleosidase; phosphopantothenoylcysteine decarboxylase; porphobilinogen synthase, or d-aminolevulinate dehydratase; pyridoxal kinase; pyridoxal phosphatase, weakly inhibited; starch phosphorylase; thiamin phosphatase; tyrosinase; and xanthine dehydrogenase.

InChI:InChI=1/C8H9NO3/c1-5-8(12)7(4-11)6(3-10)2-9-5/h2,4,10,12H,3H2,1H3

Upstream product

• 65-23-6 5-hydroxy-6-methyl-3,4-pyridinedimethanol 
• 85-87-0 pyridoxamine 
• 298-12-4 Glyoxilic acid 
• 13933-83-0 Pyridoxyliden-DL-alanin 
• 7664-93-9 sulfuric acid 
• 7647-01-0 hydrogenchloride 
• 328-50-7 α-ketoglutaric acid 
• 7732-18-5 water 
• 2280-44-6 D-Glucose 
• 61-90-5 L-leucine 
• 3458-28-4 D-Mannose 
• 65-22-5 pyridoxal hydrochloride 
• 58-56-0 pyridoxal hydrochloride 
• 54-47-7 pyridoxal 5'-phosphate 

Downstream Products

• 98497-88-2 pyridoxylidenetryptamine Schiff base 
• 4875-52-9 5-hydroxymethyl-2-methyl-4-(4,5,6,7-tetrahydro-1(3)H-imidazo[4,5-c]pyridin-4-yl)-pyridin-3-ol 
• 36120-58-8 1-(3-hydroxy-5-hydroxymethyl-2-methyl-pyridin-4-yl)-1,2,3,4-tetrahydro-isoquinoline-6,7-diol 
• 328-50-7 α-ketoglutaric acid 
• 85-87-0 pyridoxamine 
• 2392-63-4 N-pyruvoyl-alanine 
• 127-17-3 2-oxo-propionic acid 
• 82845-28-1 N-pyridoxyl-phenylalanine 
• 781-66-8 Pyridoxal-semicarbazon 
• 14942-15-5 N-pyridoxyl-L-tyrosine 
• 6956-94-1 4-[(2-hydroxyethyl)iminomethyl]-5-hydroxymethyl-2-methylpyridin-3-ol 
• 3814-80-0 3-hydroxy-5-hydroxymethyl-2-methylpyridine-4-carbaldehyde thiosemicarbazone 
• 15273-06-0 pyridoxal-phenethylimine 
• 4943-88-8 pyridoxal-phenylimine 

Relevant academic research and scientific papers

Kinetics of Oxidation of Pyridoxine by Chloramine-T in Acid Medium

The kinetics of oxidation of pyridoxine (PRX) by chloramine-T (CAT) in the presence of hydrochloric acid (0.04-1.14 M) have been studied over teh temperature range of 303-323 K.The rate of the reaction shows first-order dependence on each of CAT, PRX, and chloride ion concentrations.The reaction rate is independent of hydrogen ion concentration.Variations of ionic strength and dielectric constant of the medium have negligible effect on the rate.Addition of the reaction product, p-toluenesulfonamide, decreases the rate showing a negative first order dependence.The solvent isotope effect has been studied by using heavy water.The activation parameters, Ea, ΔH, and ΔS are computed from the reaction rates at various temperatures.The mechanism of PRX oxidation proposed and the rate law derived are consistent with the observed kinetics.

Kinetics and Mechanism of Oxidation of Pyridoxine by Sodium N-Chlorobenzenesulfonamidate

Oxidation of pyridoxine (PRX) by chloramine-B (CAB) in HCl medium at 313 K shows first order dependence each on oxidant, substrate and Cl- ion concentrations, but is independent of +>.A first-order retardation of rate is observed by the addition of reaction product, benzenesulfonamide.Suitable mechanism is proposed.

Engineering Mesorhizobium loti pyridoxamine-pyruvate aminotransferase for production of pyridoxamine with l-glutamate as an amino donor

Pyridoxamine-pyruvate aminotransferase (PPAT), a novel pyridoxal 5′-phosphate-independent aminotransferase, reversibly catalyzes the transfer of an amino group between pyridoxamine and pyruvate to generate pyridoxal and l-alanine. The enzyme can be used for synthesis of pyridoxamine, a promising candidate for prophylaxis and treatment of diabetic complications. A disadvantage of PPAT for industrial application to the synthesis is that it requires an expensive amino acid l-alanine as an amino donor. Here, mutated PPATs with a high activity toward 2-oxoglutarate (and hence toward l-glutamate) were prepared by a rational design plus random mutagenesis of the wild-type PPAT because l-glutamate is readily and economically available. The PPAT(Y35H/V70R/F247C) showed 9.1-fold lower Km and 4.3-fold higher kcat values than those of the wild-type PPAT. The model of the complex of mutated PPAT and pyridoxyl-l-glutamate showed that γ-carboxyl group of l-glutamate was hydrogen-bound with an imidazole group of His35. The production of pyridoxamine from pyridoxal with transformed Escherichia coli cells expressing the mutated PPAT did not correlate with the kcat value or catalytic efficiency of the mutated PPAT but with Km value at a low level. E. coli cells expressing the PPAT(M2T/Y35H/V70K/E212G) could be used for in vitro conversion of pyridoxal into pyridoxamine at 30 °C with l-glutamate as an amino donor.

Purification, molecular cloning, and characterization of pyridoxine 4-oxidase from Microbacterium luteolum.

Pyridoxine 4-oxidase (EC 1.1.3.12, PN 4-oxidase), which catalyzes the oxidation of PN by oxygen or other hydrogen acceptors to form pyridoxal and hydrogen peroxide or reduced forms of the acceptors, respectively, was purified for the first time to homogeneity from Microbacterium luteolum YK-1 (=Aureobacterium luteolum YK-1). The purified enzyme required FAD for its catalytic activity and stability. The enzyme was a monomeric protein with the subunit molecular mass of 53,000 +/- 1,000 Da. PN was the only substrate as the hydrogen donor. Oxygen, 2,6-dichloroindophenol, and vitamin K3 were good substrates as the hydrogen acceptor. The gene (pno) encoding PN 4-oxidase was cloned. The gene encodes a protein of 507 amino acid residues corresponding to the molecular mass of the subunit. PN 4-oxidase was expressed in Escherichia coli and found to have the same properties as the native enzyme from M. luteolum YK-1. Comparisons of primary and secondary structures with other proteins showed that the enzyme belongs to the GMC oxidoreductase family. M. luteolum YK-1 has four plasmids. The pno gene was found on a chromosomal DNA. Search for genes similar in sequence in other organisms suggested that a nitrogen-fixing symbiotic bacterium, Mesorhizobium loti, which harbors two plasmids, has a PN degradation pathway I in chromosomal DNA.

Synthesis of symmetric N,O-donor ligands derived from pyridoxal (vitamin B6): DFT studies and structural features of their binuclear chelate complexes with the oxofilic uranyl and vanadyl(V) cations

The synthesis and the structural characterization of symmetric dimers containing uranium and vanadium atoms provide an outstanding opportunity for the study of hydrogen bonding in supramolecular architectures and unusual interactions. On the search of lig

Biochemical characterization of a recombinant acid phosphatase from Acinetobacter baumannii

Genomic sequence analysis of Acinetobacter baumannii revealed the presence of a putative Acid Phosphatase (AcpA; EC 3.1.3.2). A plasmid construct was made, and recombinant protein (rAcpA) was expressed in E. coli. PAGE analysis (carried out under denaturing/ reducing conditions) of nickel-affinity purified protein revealed the presence of a nearhomogeneous band of approximately 37 kDa. The identity of the 37 kDa species was verified as rAcpA by proteomic analysis with a molecular mass of 34.6 kDa from the deduced sequence. The dependence of substrate hydrolysis on pH was broad with an optimum observed at 6.0. Kinetic analysis revealed relatively high affinity for PNPP (Km = 90 μM) with Vmax, kcat, and Kcat/Km values of 19.2 pmoles s-1, 4.80 s-1(calculated on the basis of 37 kDa), and 5.30 × 104 M-1s-1, respectively. Sensitivity to a variety of reagents, i.e., detergents, reducing, and chelating agents as well as classic acid phosphatase inhibitors was examined in addition to assessment of hydrolysis of a number of phosphorylated compounds. Removal of phosphate from different phosphorylated compounds is supportive of broad, i.e., 'nonspecific' substrate specificity; although, the enzyme appears to prefer phosphotyrosine and/or peptides containing phosphotyrosine in comparison to serine and threonine. Examination of the primary sequence indicated the absence of signature sequences characteristic of Type A, B, and C nonspecific bacterial acid phosphatases.

Biomimic oxidation of pyridoxine by peroxo complex: A kinetic and mechanistic study

Bis-(ethylene diamine),bis-(diethylene triamine)peroxo dicobalt(III) perchlorate complex is synthesized by solution route. The prepared m-peroxo complex is characterized by FT-IR and electronic spectroscopy. The biomimic kinetics oxidations of pyridoxine by peroxo complex have been studied in aqueous medium. The reaction is first order each in the concentration of peroxo complex and H+ concentration. Increase in ionic strength has no effect on the reaction rate. The reaction does not induce the polymerization of acryl amide. The main products of the reaction has been isolated and identified by the spot test. The Arrhenius and the thermodynamic parameters have been calculated from the effect of temperature on the reaction rate. A suitable mechanism has been proposed and the experimental result is derived.

SUBSTITUTED PYRIDOXINE-LACTAM CARBOXYLATE SALTS

The present invention provides salt adducts comprising at least one positively charged moiety being a pyridoxine or a derivative thereof and at least one carboxylated 5- to 7-membered lactam ring, optionally additionally substituted, methods of their preparation, and pharmaceutical compositions and medicaments comprising them. Salt adducts of the invention and compositions comprising them may be used to in the treatment of diseases or disorders associated with or inflicted by alcohol consumption.

High rates and substrate selectivities in water by polyvinylimidazoles as transaminase enzyme mimics with hydrophobically bound pyridoxamine derivatives as coenzyme mimics

(Chemical Equation Presented) Free-radical polymers of 4-vinylimidazole and copolymers with 1-dodecyl-4-vinylimidazole were used as enzyme mimics to transaminate pyruvic acid to alanine, phenylpyruvic acid to phenylalanine, and indole-3-pyruvic acid to tryptophan in water at pH 7.5 and 20 °C using pyridoxamines carrying hydrophobic side chains as coenzyme mimics. The best enzyme mimic accelerated the transamination of indole-3-pyruvic acid by a factor of 4 million relative to the rate without the polymer, a higher rate ratio than we had previously achieved with a polyaziridine-based enzyme mimic. The properties of various polyvinylimidazoles were compared, including those prepared with the RAFT modification of the polymerization process.

Brij-35 micellar catalysed chloramine-T oxidation of vitamins: A kinetic study

The kinetics of oxidation of the vitamins (B1 and B6) by sodium salt of p-toluene sulfonamide (Chloramine-T) have been studied in presence of a non-ionic surfactant, i.e., polyoxyethylene(23)laurylether (Brij-35) in perchloric acid medium. Catalytic effect of Brij-35 micelle has been observed on the rate of oxidation. The reactions show first order, fractional order and zero-order dependence of rate with respect to chloramine-T, vitamins and HClO4, respectively. The mechanism in absence as well as in presence of surfactant has been proposed. The spectrophotometric evidence supports the binding/association between chloramine-T and Brij-35 micelle. The kinetic data have also been rationalised in terms of Menger and Portnoy's kinetic model and binding parameters have been evaluated.