The 4-carboxyaldehyde form of VITAMIN B 6 which is converted to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid.
This is the active form of VITAMIN B 6 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).
An enzyme that catalyzes reversibly the phosphorylation of pyridoxal in the presence of ATP with the formation of pyridoxal 5-phosphate and ADP. Pyridoxine, pyridoxamine and various derivatives can also act as acceptors. EC 2.7.1.35.
The 4-aminomethyl form of VITAMIN B 6. During transamination of amino acids, PYRIDOXAL PHOSPHATE is transiently converted into pyridoxamine phosphate.
The 4-methanol form of VITAMIN B 6 which is converted to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. Although pyridoxine and Vitamin B 6 are still frequently used as synonyms, especially by medical researchers, this practice is erroneous and sometimes misleading (EE Snell; Ann NY Acad Sci, vol 585 pg 1, 1990).
A class of inorganic or organic compounds that contain the borohydride (BH4-) anion.
An enzyme catalyzing the deamination of pyridoxaminephosphate to pyridoxal phosphate. It is a flavoprotein that also oxidizes pyridoxine-5-phosphate and pyridoxine. EC 1.4.3.5.
A nutritional condition produced by a deficiency of VITAMIN B 6 in the diet, characterized by dermatitis, glossitis, cheilosis, and stomatitis. Marked deficiency causes irritability, weakness, depression, dizziness, peripheral neuropathy, and seizures. In infants and children typical manifestations are diarrhea, anemia, and seizures. Deficiency can be caused by certain medications, such as isoniazid.
A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.
The protein components of enzyme complexes (HOLOENZYMES). An apoenzyme is the holoenzyme minus any cofactors (ENZYME COFACTORS) or prosthetic groups required for the enzymatic function.
VITAMIN B 6 refers to several PICOLINES (especially PYRIDOXINE; PYRIDOXAL; & PYRIDOXAMINE) that are efficiently converted by the body to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, and aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into PYRIDOXAMINE phosphate. Although pyridoxine and Vitamin B 6 are still frequently used as synonyms, especially by medical researchers, this practice is erroneous and sometimes misleading (EE Snell; Ann NY Acad Sci, vol 585 pg 1, 1990). Most of vitamin B6 is eventually degraded to PYRIDOXIC ACID and excreted in the urine.
Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.
The catabolic product of most of VITAMIN B 6; (PYRIDOXINE; PYRIDOXAL; and PYRIDOXAMINE) which is excreted in the urine.
A PYRIDOXAL-phosphate containing enzyme that catalyzes the dehydration and deamination of L-serine to form pyruvate. This enzyme was formerly listed as EC 4.2.1.13.
A group of compounds that are monomethyl derivatives of pyridines. (From Dorland, 28th ed)
A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.
Condensation products of aromatic amines and aldehydes forming azomethines substituted on the N atom, containing the general formula R-N:CHR. (From Grant & Hackh's Chemical Dictionary, 5th ed)
A pyridoxal phosphate enzyme that catalyzes the reaction of glycine and 5,10-methylene-tetrahydrofolate to form serine. It also catalyzes the reaction of glycine with acetaldehyde to form L-threonine. EC 2.1.2.1.
The rate dynamics in chemical or physical systems.
An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC 4.2.99.8.
A pyridoxal-phosphate protein that reversibly catalyzes the conversion of L-alanine to D-alanine. EC 5.1.1.1.
A class of glucosyltransferases that catalyzes the degradation of storage polysaccharides, such as glucose polymers, by phosphorolysis in animals (GLYCOGEN PHOSPHORYLASE) and in plants (STARCH PHOSPHORYLASE).
An essential amino acid. It is often added to animal feed.
An enzyme that catalyzes the cleavage of tyrosine to phenol, pyruvate, and ammonia. It is a pyridoxal phosphate protein. The enzyme also forms pyruvate from D-tyrosine, L-cysteine, S-methyl-L-cysteine, L-serine, and D-serine, although at a slower rate. EC 4.1.99.2.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the reversible transfer of an amino group between D-Alanine and alpha-ketoglutarate to form PYRUVATE and D-GLUTAMATE, respectively. It plays a role in the synthesis of the bacterial CELL WALL. This enzyme was formerly classified as EC 2.6.1.10.
An enzyme that catalyzes the conversion of L-tryptophan and water to indole, pyruvate, and ammonia. It is a pyridoxal-phosphate protein, requiring K+. It also catalyzes 2,3-elimination and beta-replacement reactions of some indole-substituted tryptophan analogs of L-cysteine, L-serine, and other 3-substituted amino acids. (From Enzyme Nomenclature, 1992) EC 4.1.99.1.
An enzyme that catalyzes the conversion of L-serine and 1-(indol-3-yl)glycerol 3-phosphate to L-tryptophan and glyceraldehyde 3-phosphate. It is a pyridoxal phosphate protein that also catalyzes the conversion of serine and indole into tryptophan and water and of indoleglycerol phosphate into indole and glyceraldehyde phosphate. (From Enzyme Nomenclature, 1992) EC 4.2.1.20.
The inactive form of GLYCOGEN PHOSPHORYLASE that is converted to the active form PHOSPHORYLASE A via phosphorylation by PHOSPHORYLASE KINASE and ATP.
Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
A multifunctional pyridoxal phosphate enzyme. In the second stage of cysteine biosynthesis it catalyzes the reaction of homocysteine with serine to form cystathionine with the elimination of water. Deficiency of this enzyme leads to HYPERHOMOCYSTEINEMIA and HOMOCYSTINURIA. EC 4.2.1.22.
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A pyridoxal-phosphate protein that catalyzes the conversion of L-tyrosine to tyramine and carbon dioxide. The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine. (From Enzyme Nomenclature, 1992) EC 4.1.1.25.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Cystathionine is an intermediate sulfur-containing amino acid in the transsulfuration pathway, formed from homocysteine and serine by the enzyme cystathionine beta-synthase, which is involved in the biosynthesis of cysteine and glutathione.
Imines are organic compounds containing a functional group with a carbon-nitrogen double bond (=NH or =NR), classified as azomethines, which can be produced from aldehydes or ketones through condensation with ammonia or amines.
Semicarbazides are organic compounds containing a functional group with the structure NH2-NH-CO-NH2, which are commonly used as reagents in chemical reactions to form semicarbazones, and can also be found in some pharmaceuticals and industrial chemicals.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
A pyridoxal phosphate enzyme that catalyzes the formation of glutamate gamma-semialdehyde and an L-amino acid from L-ornithine and a 2-keto-acid. EC 2.6.1.13.
An enzyme of the transferase class that catalyzes condensation of the succinyl group from succinyl coenzyme A with glycine to form delta-aminolevulinate. It is a pyridoxyal phosphate protein and the reaction occurs in mitochondria as the first step of the heme biosynthetic pathway. The enzyme is a key regulatory enzyme in heme biosynthesis. In liver feedback is inhibited by heme. EC 2.3.1.37.
An enzyme that converts brain gamma-aminobutyric acid (GAMMA-AMINOBUTYRIC ACID) into succinate semialdehyde, which can be converted to succinic acid and enter the citric acid cycle. It also acts on beta-alanine. EC 2.6.1.19.
Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Enzymes that catalyze the cleavage of a carbon-sulfur bond by means other than hydrolysis or oxidation. EC 4.4.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Measurement of the intensity and quality of fluorescence.
Analogs of those substrates or compounds which bind naturally at the active sites of proteins, enzymes, antibodies, steroids, or physiological receptors. These analogs form a stable covalent bond at the binding site, thereby acting as inhibitors of the proteins or steroids.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Antibacterial agent used primarily as a tuberculostatic. It remains the treatment of choice for tuberculosis.
Autosomal recessive inborn error of methionine metabolism usually caused by a deficiency of CYSTATHIONINE BETA-SYNTHASE and associated with elevations of homocysteine in plasma and urine. Clinical features include a tall slender habitus, SCOLIOSIS, arachnodactyly, MUSCLE WEAKNESS, genu varus, thin blond hair, malar flush, lens dislocations, an increased incidence of MENTAL RETARDATION, and a tendency to develop fibrosis of arteries, frequently complicated by CEREBROVASCULAR ACCIDENTS and MYOCARDIAL INFARCTION. (From Adams et al., Principles of Neurology, 6th ed, p979)
One of the AROMATIC-L-AMINO-ACID DECARBOXYLASES, this enzyme is responsible for the conversion of DOPA to DOPAMINE. It is of clinical importance in the treatment of Parkinson's disease.
A multifunctional pyridoxal phosphate enzyme. In the final step in the biosynthesis of cysteine it catalyzes the cleavage of cystathionine to yield cysteine, ammonia, and 2-ketobutyrate. EC 4.4.1.1.
Anemia characterized by the presence of erythroblasts containing excessive deposits of iron in the marrow.
Glutarates are organic compounds, specifically carboxylic acids, that contain a five-carbon chain with two terminal carboxyl groups and a central methyl group, playing a role in various metabolic processes, including the breakdown of certain amino acids. They can also refer to their salts or esters. Please note that this definition is concise and may not cover all aspects of glutarates in depth.
A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).
Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Organic compounds containing a carbonyl group in the form -CHO.
An enzyme that catalyzes the conversion of L-TYROSINE and 2-oxoglutarate to 4-hydroxyphenylpyruvate and L-GLUTAMATE. It is a pyridoxal-phosphate protein. L-PHENYLALANINE is hydroxylated to L-tyrosine. The mitochondrial enzyme may be identical with ASPARTATE AMINOTRANSFERASES (EC 2.6.1.1.). Deficiency of this enzyme may cause type II Tyrosinemia (see TYROSINEMIAS). EC 2.6.1.5.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Xanthurenic acid and its salts, formed as byproducts during the metabolism of tryptophan, are collectively referred to as xanthurenates, which can accumulate in conditions like hyperphenylalaninemia and may contribute to oxidative stress and cellular damage.
A group of water-soluble vitamins, some of which are COENZYMES.
Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).
A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.
Organic chemicals that form two or more coordination links with an iron ion. Once coordination has occurred, the complex formed is called a chelate. The iron-binding porphyrin group of hemoglobin is an example of a metal chelate found in biological systems.
Nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. The richest natural source is yeast. It occurs in the free form only in the retina of the eye, in whey, and in urine; its principal forms in tissues and cells are as FLAVIN MONONUCLEOTIDE and FLAVIN-ADENINE DINUCLEOTIDE.
A disease characterized by compensated hemolysis with a normal hemoglobin level or a mild to moderate anemia. There may be intermittent abdominal discomfort, splenomegaly, and slight jaundice.
A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.
An aldotriose which is an important intermediate in glycolysis and in tryptophan biosynthesis.
Enzymes that catalyze the breakage of a carbon-oxygen bond leading to unsaturated products via the removal of water. EC 4.2.1.
The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
An enzyme that catalyzes the decarboxylation of histidine to histamine and carbon dioxide. It requires pyridoxal phosphate in animal tissues, but not in microorganisms. EC 4.1.1.22.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
An enzyme of the PHOSPHORYLASES family that catalyzes the degradation of starch, a mixture of unbranched AMYLOSE and branched AMYLOPECTIN compounds. This phosphorylase from plants is the counterpart of GLYCOGEN PHOSPHORYLASE in animals that catalyzes the reaction of inorganic phosphate on the terminal alpha-1,4-glycosidic bond at the non-reducing end of glucans resulting in the release of glucose-1-phosphate.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
A thiol-containing amino acid formed by a demethylation of METHIONINE.
The sum of the weight of all the atoms in a molecule.
Enzymes of the isomerase class that catalyze the transfer of acyl-, phospho-, amino- or other groups from one position within a molecule to another. EC 5.4.
A genetic metabolic disorder resulting from serum and bone alkaline phosphatase deficiency leading to hypercalcemia, ethanolamine phosphatemia, and ethanolamine phosphaturia. Clinical manifestations include severe skeletal defects resembling vitamin D-resistant rickets, failure of the calvarium to calcify, dyspnea, cyanosis, vomiting, constipation, renal calcinosis, failure to thrive, disorders of movement, beading of the costochondral junction, and rachitic bone changes. (From Dorland, 27th ed)
A process of selective diffusion through a membrane. It is usually used to separate low-molecular-weight solutes which diffuse through the membrane from the colloidal and high-molecular-weight solutes which do not. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A water-soluble medicinal preparation applied to the skin.
A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.
Compounds that bind to and block the stimulation of PURINERGIC P2 RECEPTORS.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Enzymes that catalyze the cleavage of a carbon-oxygen bond by means other than hydrolysis or oxidation. EC 4.2.
An organism of the vegetable kingdom suitable by nature for use as a food, especially by human beings. Not all parts of any given plant are edible but all parts of edible plants have been known to figure as raw or cooked food: leaves, roots, tubers, stems, seeds, buds, fruits, and flowers. The most commonly edible parts of plants are FRUIT, usually sweet, fleshy, and succulent. Most edible plants are commonly cultivated for their nutritional value and are referred to as VEGETABLES.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A key enzyme in SPHINGOLIPIDS biosynthesis, this enzyme catalyzes the pyridoxal-5'-phosphate-dependent condensation of L-SERINE and PALMITOYL COENZYME A to 3-dehydro-D-sphinganine. The enzyme consists of two different subunits.
Glutaminase is an enzyme that catalyzes the conversion of glutamine to glutamate and ammonia, playing a crucial role in nitrogen metabolism and amino acid homeostasis within various tissues and cells, including the brain, kidney, and immune cells.
A compound that inhibits aminobutyrate aminotransferase activity in vivo, thereby raising the level of gamma-aminobutyric acid in tissues.
A rare, metallic element designated by the symbol, Ga, atomic number 31, and atomic weight 69.72.
A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the transfer of amino group of L-LYSINE onto 2-oxoglutarate to generate 2-aminoadipate 6-semialdehyde and L-GLUTAMATE.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
Inorganic salts or organic esters of phosphorous acid that contain the (3-)PO3 radical. (From Grant & Hackh's Chemical Dictionary, 5th ed)
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.
Amino-substituted glyoxylic acid derivative.
Enzymes that catalyze the transfer of nitrogenous groups, primarily amino groups, from a donor, generally an amino acid, to an acceptor, usually a 2-oxoacid. EC 2.6.
An amino acid produced in the urea cycle by the splitting off of urea from arginine.
Proteins prepared by recombinant DNA technology.

EPR spin trapping and 2-deoxyribose degradation studies of the effect of pyridoxal isonicotinoyl hydrazone (PIH) on *OH formation by the Fenton reaction. (1/202)

The search for effective iron chelating agents was primarily driven by the need to treat iron-loading refractory anemias such as beta-thalassemia major. However, there is a potential for therapeutic use of iron chelators in non-iron overload conditions. Iron can, under appropriate conditions, catalyze the production of toxic oxygen radicals which have been implicated in numerous pathologies and, hence, iron chelators may be useful as inhibitors of free radical-mediated tissue damage. We have developed the orally effective iron chelator pyridoxal isonicotinoyl hydrazone (PIH) and demonstrated that it inhibits iron-mediated oxyradical formation and their effects (e.g. 2-deoxyribose oxidative degradation, lipid peroxidation and plasmid DNA breaks). In this study we further characterized the mechanism of the antioxidant action of PIH and some of its analogs against *OH formation from the Fenton reaction. Using electron paramagnetic resonance (EPR) with 5, 5-dimethyl-1-pyrroline-N-oxide (DMPO) as a spin trap for *OH we showed that PIH and salicylaldehyde isonicotinoyl hydrazone (SIH) inhibited Fe(II)-dependent production of *OH from H2O2. Moreover, PIH protected 2-deoxyribose against oxidative degradation induced by Fe(II) and H2O2. The protective effect of PIH against both DMPO hydroxylation and 2-deoxyribose degradation was inversely proportional to Fe(II) concentration. However, PIH did not change the primary products of the Fenton reaction as indicated by EPR experiments on *OH-mediated ethanol radical formation. Furthermore, PIH dramatically enhanced the rate of Fe(II) oxidation to Fe(III) in the presence of oxygen, suggesting that PIH decreases the concentration of Fe(II) available for the Fenton reaction. These results suggest that PIH and SIH deserve further investigation as inhibitors of free-radical mediated tissue damage.  (+info)

The iron chelator pyridoxal isonicotinoyl hydrazone (PIH) and its analogues prevent damage to 2-deoxyribose mediated by ferric iron plus ascorbate. (2/202)

Iron chelating agents are essential for treating iron overload in diseases such as beta-thalassemia and are potentially useful for therapy in non-iron overload conditions, including free radical mediated tissue injury. Deferoxamine (DFO), the only drug available for iron chelation therapy, has a number of disadvantages (e.g., lack of intestinal absorption and high cost). The tridentate chelator pyridoxal isonicotinoyl hydrazone (PIH) has high iron chelation efficacy in vitro and in vivo with high selectivity and affinity for iron. It is relatively non-toxic, economical to synthesize and orally effective. We previously demonstrated that submillimolar levels of PIH and some of its analogues inhibit lipid peroxidation, ascorbate oxidation, 2-deoxyribose degradation, plasmid DNA strand breaks and 5,5-dimethylpyrroline-N-oxide (DMPO) hydroxylation mediated by either Fe(II) plus H(2)O(2) or Fe(III)-EDTA plus ascorbate. To further characterize the mechanism of PIH action, we studied the effects of PIH and some of its analogues on the degradation of 2-deoxyribose induced by Fe(III)-EDTA plus ascorbate. Compared with hydroxyl radical scavengers (DMSO, salicylate and mannitol), PIH was about two orders of magnitude more active in protecting 2-deoxyribose from degradation, which was comparable with some of its analogues and DFO. Competition experiments using two different concentrations of 2-deoxyribose (15 vs. 1.5 mM) revealed that hydroxyl radical scavengers (at 20 or 60 mM) were significantly less effective in preventing degradation of 2-deoxyribose at 15 mM than 2-deoxyribose at 1.5 mM. In contrast, 400 microM PIH was equally effective in preventing degradation of both 15 mM and 1.5 mM 2-deoxyribose. At a fixed Fe(III) concentration, increasing the concentration of ligands (either EDTA or NTA) caused a significant reduction in the protective effect of PIH towards 2-deoxyribose degradation. We also observed that PIH and DFO prevent 2-deoxyribose degradation induced by hypoxanthine, xanthine oxidase and Fe(III)-EDTA. The efficacy of PIH or DFO was inversely related to the EDTA concentration. Taken together, these results indicate that PIH (and its analogues) works by a mechanism different than the hydroxyl radical scavengers. It is likely that PIH removes Fe(III) from the chelates (either Fe(III)-EDTA or Fe(III)-NTA) and forms a Fe(III)-PIH(2) complex that does not catalyze oxyradical formation.  (+info)

Studies on mammalian ribonucleotide reductase inhibition by pyridoxal phosphate and the dialdehyde derivatives of adenosine, adenosine 5'-monophosphate, and adenosine 5'-triphosphate. (3/202)

Ribonucleotide reductase activity in a partially purified enzyme preparation from Ehrilich tumor cells was inhibited by the dialdehyde derivatives of adenosine, 5-adenylic acid, and adenosine 5-triphosphate (prepared by the periodate oxidation of adenosine 5-adenylic acid, and adenosine 5-triphosphate). The borohydride-reduced derivative of periodate-oxidized adenosine was not inhibitory to the ribonucleotide reductase activity, showing that the aldehyde moiety was important in the inhibitory interactions of these compounds. This suggested the formation of a Schiff base between the dialdehyde derivative and an amino group (presumably, the epsilon-amino group of lysine). Pyridoxal phosphate, which is known to inhibit enzymes that have lysyl residues in the catalytic or allosteric sites, was an inhibitor of ribonucleotide reductase. Pyridoxal, pyridoxamine phosphate, pyridoxamine, and pyridoxine were not inhibitors. Borohydride reduction of the enzyme in the presence of pyridoxal phosphate produced a protein fraction that had little reductase activity remaining. The inhibition by pyridoxal phosphate was not influenced by increasing the substrate concentration (cytidine 5-diphosphate or adenosine 5-diphosphate), but was diminished by increasing the ratio of allosteric effector to pyridoxal phosphate concentrations, suggesting an interaction of pyridoxal phosphate at the regulatory site of ribonucleotide reductase. The addition of adenosine 5-triphosphate to the pyridoxal phosphate-enzyme mixture, which was subsequently treated with borohydride, partially prevented the inhibition by pyridoxal phosphate. Heat treatment of the ribonucleotide reductase enzyme preparation in the presence of pyridoxal phosphate protected the enzyme against loss of cytidine 5-diphosphate and adenosine 5-diphosphate reductase activities.  (+info)

Development of potential iron chelators for the treatment of Friedreich's ataxia: ligands that mobilize mitochondrial iron. (4/202)

Friedreich's ataxia (FA) is a crippling neurodegenerative disease that is due to iron (Fe) overload within the mitochondrion. One therapeutic intervention may be the development of a chelator that could remove mitochondrial Fe. We have implemented the only well characterized model of mammalian mitochondrial Fe overload to examine the Fe chelation efficacy of novel chelators of the 2-pyridylcarboxaldehyde isonicotinoyl hydrazone (PCIH) class. In this model we utilize reticulocytes treated with the haem synthesis inhibitor succinylacetone which results in mitochondrial Fe-loading. Our experiments demonstrate that in contrast to desferrioxamine, several of the PCIH analogues show very high activity at mobilizing (59)Fe from (59)Fe-loaded reticulocytes. Further studies on these ligands in animals are clearly warranted considering their potential to treat FA.  (+info)

The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents, IV: The mechanisms involved in inhibiting cell-cycle progression. (5/202)

Some chelators of the pyridoxal isonicotinoyl hydrazone class have antiproliferative activity that is far greater than desferrioxamine (DFO). In this study, DFO was compared with one of the most active chelators (311) on the expression of molecules that play key roles in cell-cycle control. This was vital for understanding the role of iron (Fe) in cell-cycle progression and for designing chelators to treat cancer. Incubating cells with DFO, and especially 311, resulted in a decrease in the hyperphosphorylated form of the retinoblastoma susceptibility gene product (pRb). Chelators also decreased cyclins D1, D2, and D3, which bind with cyclin-dependent kinase 4 (cdk4) to phosphorylate pRb. The levels of cdk2 also decreased after incubation with DFO, and especially 311, which may be important for explaining the decrease in hyperphosphorylated pRb. Cyclins A and B1 were also decreased after incubation with 311 and, to a lesser extent, DFO. In contrast, cyclin E levels increased. These effects were prevented by presaturating the chelators with Fe. In contrast to DFO and 311, the ribonucleotide reductase inhibitor hydroxyurea increased the expression of all cyclins. Hence, the effect of chelators on cyclin expression was not due to their ability to inhibit ribonucleotide reductase. Although chelators induced a marked increase in WAF1 and GADD45 mRNA transcripts, there was no appreciable increase in their protein levels. Failure to translate these cell-cycle inhibitors may contribute to dysregulation of the cell cycle after exposure to chelators. (Blood. 2001;98:842-850)  (+info)

Properties of 4-ethenyl and 4-ethynyl analogs of pyridoxal phosphate and their reactions with the apo form of asparatate aminotransferase. (6/202)

The binding to apoaspartate aminotransferase of analogs of pyridoxal phosphate bearing vinyl, cis- and trans-methylvinyl, and ethynyl groups in place of the fomyl group of the coenzyme has been studied. Details of synthesis of the ethynyl compound are given. The absorption spectra of all of the compounds have been analyzed and pKa values have been determined. The positions of the absorption bands can be related to those of pyridoxine but with bathochromic shifts induced by the ethenyl and ethynyl groups. However, this shift is almost completely lacking for the cis-methylvinyl compound suggesting nonplanarity of the molecule. Binding of the analogs to the apoenzyme is accompanied by a strong bathochromic shift which, from a study of solvent effects on the free analogs, appears to indicate a hydrophobic environment on the enzyme. Nevertheless, the analogs are bound as dipolar ions exclusively. Binding is accompanied by a distinct perturbation of the protein spectrum in the aromatic region. An effect on the spectrum of 1 or more tryptophan residues is indicated. Bands of the bound analogs exhibit positive circular dichroism except for that of the 4-vinyl analog. The 4-ethynyl analog reacts in a more complex way, giving at least two successive products in addition to the initial complex. The final product is reducible by sodium borohydride, is released from the enzyme by boiling, and appears to have the properties of a Schiff base. We postulate that the addition of an amino group of the enzyme to the ethynyl group is followed by tautomeric rearrangement to a Schiff base in which the ring is in a p-quinonoid structure.  (+info)

Activation and inactivation of horse liver alcohol dehydrogenase with pyridoxal compounds. (7/202)

Pyridoxal compounds can either activate or inactivate horse liver alcohol dehydrogenase in differential labeling experiments. Amino groups outside of the active sites were modified with ethyl acetimidate, while the amino groups in the active sites were protected by the formation of the complex with NAD-plus and pyrazole. After removal of the NAD-plus and pyranzole, the partially acetimidylated enzyme was reductively alkylated with pyridoxal and NaBH4, with the incorporation of one pyridoxal group per subunit of the enzyme. The turnover numbers for the reaction of NAD-plus and ethanol increased by 15-fold, and for NADH and acetaldehyde by 32-fold. The Michaelis and inhibition constants increased 80-fold or more. Pyridoxal phosphate and NaBH4 also modified one group per subunit, but the turnover numbers decreased by 10-fold and the kinetic constants were intermediate between those obtained for pyridoxyl alcohol dehydrogenase and the partially acetimidylated enzyme. With native enzyme, the rates of dissociation of the enzyme-coenzyme complexes are rate-limiting in the catalytic reactions. The pyridoxyl enzyme is activated because the rates of dissociation of the enzyme-coenzyme complexes are increased. The rates of binding of coenzyme to phosphopyridoxyl enzyme have decreased due to the introduction of the negatively charged phosphate. The size of the group is not responsible for this decrease since these rates are not greatly decreased by the incorporation of pyridoxal. For both pyrodoxal and phosphopyridoxyl alcohol dehydrogenases, the interconversion of the ternary complex is at least partially rate-limiting. Chymotryptic-tryptic digestion of pryidoxyl enzyme produced a major peptide corresponding to residues 219 to 229, in which Lys 228 had reacted with pyridoxal. The same lysine residue reacted with pyridoxal phosphate.  (+info)

Technetium-99m-pyridoxylideneglutamate: a new hepatobiliary radiopharmaceutical. II. Clinical aspects. (8/202)

Technetium-99m-pyridoxylideneglutamate (99mTc-PG) is a nontoxic radiopharmaceutical that was found to undergo rapid biliary excretion in normal humans. The biliary tree and gallbladder were seen within 10-15 min of injection and by 20 min marked accumulation of radioactivity was noted in the gallbladder and gastrointestinal tract. Of ten "control" volunteers, seven had normal 99mTc-PG-cholescintigrams. In the remaining three, the gallbladder was not visualized. Gallbladder disease was not excluded in these three subjects. Of 24 patients referred for investigation of right upper quadrant abdominal pain, 13 proved to have gallbladder disease. All seven patients with acute cholecystitis and one of four patients with chronic cholecystitis had nonvisualization of the gallbladder on the cholescintigram whereas five patients with chronic cholecystitis or cholesterolosis had normal cholescintigrams. Six of the eight patients with nonvisualization of the gallbladder on cholescintigram had contrast radiologic studies (oral cholecystogram or intravenous cholangiogram or both), and in all six, nonvisualization of the gallbladder was also reported on the contrast study. cholescintigraphy was found to be greatly inferior to contrast radiologic studies in the detection of gallbladder stones. Eleven patients had complete extrahepatic biliary obstruction and this diagnosis was correctly made in all 11 by the cholescintigram. Fourteen patients had incomplete extrahepatic biliary obstruction. The correct diagnosis was made on the cholescintigram in seven but in the remaining seven it was not possible to distinguish between incomplete extrahepatic biliary obstruction and hepatocellular disease. Malignant lesions (carcinomas of head of pancreas, gallbladder, common bile duct or ampulla of Vater) were the cause of obstruction in 10 of the 25 patients with complete or incomplete obstruction and the diagnosis of obstruction due to malignancy was correctly made in 8 of these 10 by means of a scintigraphic equivalent to Courvoisier's sing. Finally, 11 patients had hepatocellular disease and a nonspecific pattern consistent with either imcomplete biliary obstruction or hepatocellular disease was observed on the cholescintigram in all 11. The 99mTc-PG cholescintigram is suggested for a role complementary to that of contrast radiologic studies in the preoperative investigation of patients with possible surgical disease of the biliary tract. Contrast radiologic techniques are advocated as being more appropriate in the nonjaundiced patient with suspected gallbladder disease whereas the 99mTc-PG cholescintigram is advocated as being more appropriate in the patient with jaundice. The value of the 99mTc-PG cholescintigram lies in the confidence with which complete extrahepatic biliary obstruction can be diagnosed. The "scintigraphic Courvoisier's sign" seems a useful indicator of malignant obstruction.  (+info)

Pyridoxal is a form of vitamin B6, specifically the alcohol form of pyridoxine. It is a cofactor for many enzymes involved in protein metabolism and synthesis of neurotransmitters. Pyridoxal can be converted to its active form, pyridoxal 5'-phosphate (PLP), which serves as a coenzyme in various biochemical reactions, including transamination, decarboxylation, and racemization/elimination reactions. Deficiency in vitamin B6 can lead to neurological disorders and impaired synthesis of amino acids and neurotransmitters.

Pyridoxal phosphate (PLP) is the active form of vitamin B6 and functions as a cofactor in various enzymatic reactions in the human body. It plays a crucial role in the metabolism of amino acids, carbohydrates, lipids, and neurotransmitters. Pyridoxal phosphate is involved in more than 140 different enzyme-catalyzed reactions, making it one of the most versatile cofactors in human biochemistry.

As a cofactor, pyridoxal phosphate helps enzymes carry out their functions by facilitating chemical transformations in substrates (the molecules on which enzymes act). In particular, PLP is essential for transamination, decarboxylation, racemization, and elimination reactions involving amino acids. These processes are vital for the synthesis and degradation of amino acids, neurotransmitters, hemoglobin, and other crucial molecules in the body.

Pyridoxal phosphate is formed from the conversion of pyridoxal (a form of vitamin B6) by the enzyme pyridoxal kinase, using ATP as a phosphate donor. The human body obtains vitamin B6 through dietary sources such as whole grains, legumes, vegetables, nuts, and animal products like poultry, fish, and pork. It is essential to maintain adequate levels of pyridoxal phosphate for optimal enzymatic function and overall health.

Pyridoxal Kinase (PK) is an enzyme that plays a crucial role in the metabolism of amino acids. The medical definition of Pyridoxal Kinase is as follows:

Pyridoxal Kinase (PK, EC 2.7.1.35) is an enzyme involved in the activation of vitamin B6 (pyridoxine, pyridoxal, or pyridoxamine) and its derivatives. Specifically, PK catalyzes the phosphorylation of pyridoxal to form pyridoxal 5'-phosphate (PLP), which is the biologically active cofactor for many enzymes involved in amino acid metabolism, neurotransmitter synthesis, and other essential physiological processes.

In humans, there are two isoforms of Pyridoxal Kinase: PKL (liver-type) and PKR (rotype). Mutations in the PKL gene can lead to a rare autosomal recessive disorder called Pyridox(am)ine 5'-phosphate oxidase deficiency (PNPO Deficiency), which is characterized by seizures, developmental delay, and other neurological symptoms. This disorder results from impaired synthesis of the active form of vitamin B6, PLP, due to defective PK enzyme activity.

Pyridoxamine is a form of vitamin B6, which is a water-soluble vitamin that plays an essential role in the body's protein metabolism, neurotransmitter synthesis, and hemoglobin production. Pyridoxamine is a specific chemical compound that is a derivative of pyridoxine, another form of vitamin B6.

Pyridoxamine functions as a cofactor for various enzymes involved in the metabolism of amino acids, the building blocks of proteins. It helps to convert harmful homocysteine into the essential amino acid methionine, which is important for maintaining normal levels of homocysteine and supporting cardiovascular health.

Pyridoxamine has been studied for its potential role in treating or preventing certain medical conditions, such as diabetic nephropathy and neurodegenerative diseases, due to its antioxidant properties and ability to protect against protein glycation, a process that can damage tissues and contribute to aging and disease. However, more research is needed to establish its safety and efficacy for these uses.

Pyridoxine is the chemical name for Vitamin B6. According to the medical definition, Pyridoxine is a water-soluble vitamin that is part of the B-vitamin complex and is essential for the metabolism of proteins, carbohydrates, and fats. It plays a vital role in the regulation of homocysteine levels in the body, the formation of neurotransmitters such as serotonin and dopamine, and the synthesis of hemoglobin.

Pyridoxine can be found naturally in various foods, including whole grains, legumes, vegetables, nuts, seeds, meat, poultry, and fish. It is also available as a dietary supplement and may be prescribed by healthcare providers to treat or prevent certain medical conditions, such as vitamin B6 deficiency, anemia, seizures, and carpal tunnel syndrome.

Like other water-soluble vitamins, Pyridoxine cannot be stored in the body and must be replenished regularly through diet or supplementation. Excessive intake of Pyridoxine can lead to toxicity symptoms such as nerve damage, skin lesions, and light sensitivity.

Borohydrides are a class of chemical compounds that contain boron and hydrogen ions (H-). The most common borohydride is sodium borohydride (NaBH4), which is a white, solid compound often used in chemistry as a reducing agent. Borohydrides are known for their ability to donate hydride ions (H:-) in chemical reactions, making them useful for reducing various organic and inorganic compounds. Other borohydrides include lithium borohydride (LiBH4), potassium borohydride (KBH4), and calcium borohydride (Ca(BH4)2).

Pyridoxamine Phosphate Oxidase (PNPO) is an enzyme that is involved in the metabolism of the vitamin B6. The protein code for this enzyme is PNPO, and its systematic name is pyridoxamine 5'-phosphate:oxygen oxidoreductase (dephosphorylating).

The primary function of Pyridoxamine Phosphate Oxidase is to convert pyridoxamine phosphate (PMP) into pyridoxal 5'-phosphate (PLP), which is an active form of vitamin B6 and a cofactor for many enzymatic reactions in the body, particularly those involved in amino acid metabolism.

Deficiency or dysfunction of Pyridoxamine Phosphate Oxidase can lead to neurological disorders and seizures, as PLP is essential for the synthesis of neurotransmitters and other vital compounds in the brain.

Vitamin B6 deficiency refers to the condition in which there is an insufficient amount of vitamin B6 (pyridoxine) in the body. Vitamin B6 is an essential nutrient that plays a crucial role in various bodily functions, including protein metabolism, neurotransmitter synthesis, hemoglobin production, and immune function.

A deficiency in vitamin B6 can lead to several health issues, such as:

1. Anemia: Vitamin B6 is essential for the production of hemoglobin, a protein in red blood cells that carries oxygen throughout the body. A deficiency in this nutrient can lead to anemia, characterized by fatigue, weakness, and shortness of breath.
2. Peripheral neuropathy: Vitamin B6 deficiency can cause nerve damage, leading to symptoms such as numbness, tingling, and pain in the hands and feet.
3. Depression and cognitive impairment: Pyridoxine is necessary for the synthesis of neurotransmitters like serotonin and dopamine, which are involved in mood regulation. A deficiency in vitamin B6 can lead to depression, irritability, and cognitive decline.
4. Seizures: In severe cases, vitamin B6 deficiency can cause seizures due to the impaired synthesis of gamma-aminobutyric acid (GABA), an inhibitory neurotransmitter that helps regulate brain activity.
5. Skin changes: A deficiency in this nutrient can also lead to skin changes, such as dryness, scaling, and cracks around the mouth.

Vitamin B6 deficiency is relatively uncommon in developed countries but can occur in individuals with certain medical conditions, such as malabsorption syndromes, alcoholism, kidney disease, or those taking medications that interfere with vitamin B6 metabolism. Additionally, older adults, pregnant women, and breastfeeding mothers may have an increased need for this nutrient, making them more susceptible to deficiency.

Transaminases, also known as aminotransferases, are a group of enzymes found in various tissues of the body, particularly in the liver, heart, muscle, and kidneys. They play a crucial role in the metabolism of amino acids, the building blocks of proteins.

There are two major types of transaminases: aspartate aminotransferase (AST) and alanine aminotransferase (ALT). Both enzymes are normally present in low concentrations in the bloodstream. However, when tissues that contain these enzymes are damaged or injured, such as during liver disease or muscle damage, the levels of AST and ALT in the blood may significantly increase.

Measurement of serum transaminase levels is a common laboratory test used to assess liver function and detect liver injury or damage. Increased levels of these enzymes in the blood can indicate conditions such as hepatitis, liver cirrhosis, drug-induced liver injury, heart attack, and muscle disorders. It's important to note that while elevated transaminase levels may suggest liver disease, they do not specify the type or cause of the condition, and further diagnostic tests are often required for accurate diagnosis and treatment.

An apoenzyme is the protein component of an enzyme that is responsible for its catalytic activity. It combines with a cofactor, which can be either an organic or inorganic non-protein molecule, to form the active enzyme. The cofactor can be a metal ion or a small organic molecule called a coenzyme.

The term "apoenzyme" is used to describe the protein portion of an enzyme after it has lost its cofactor. When the apoenzyme combines with the cofactor, the active holoenzyme is formed, which is capable of carrying out the specific biochemical reaction for which the enzyme is responsible.

In some cases, the loss of a cofactor can result in the complete loss of enzymatic activity, while in other cases, the apoenzyme may retain some residual activity. The relationship between an apoenzyme and its cofactor is specific, meaning that each cofactor typically only binds to and activates one particular type of apoenzyme.

Medical Definition of Vitamin B6:

Vitamin B6, also known as pyridoxine, is a water-soluble vitamin that plays a crucial role in various bodily functions. It is involved in the process of making serotonin and norepinephrine, which are chemicals that transmit signals in the brain. Vitamin B6 is also necessary for the formation of myelin, a protein layer that forms around nerve cells. Additionally, it helps the body to metabolize proteins, carbohydrates, and fats, and is involved in the creation of red blood cells.

Vitamin B6 can be found in a wide variety of foods, including poultry, seafood, bananas, potatoes, and fortified cereals. A deficiency in vitamin B6 can lead to anemia, confusion, and a weakened immune system. On the other hand, excessive intake of vitamin B6 can cause nerve damage and skin lesions. It is important to maintain appropriate levels of vitamin B6 through a balanced diet and, if necessary, supplementation under the guidance of a healthcare provider.

Aspartate aminotransferases (ASTs) are a group of enzymes found in various tissues throughout the body, including the heart, liver, and muscles. They play a crucial role in the metabolic process of transferring amino groups between different molecules.

In medical terms, AST is often used as a blood test to measure the level of this enzyme in the serum. Elevated levels of AST can indicate damage or injury to tissues that contain this enzyme, such as the liver or heart. For example, liver disease, including hepatitis and cirrhosis, can cause elevated AST levels due to damage to liver cells. Similarly, heart attacks can also result in increased AST levels due to damage to heart muscle tissue.

It is important to note that an AST test alone cannot diagnose a specific medical condition, but it can provide valuable information when used in conjunction with other diagnostic tests and clinical evaluation.

Pyridoxic acid is the major metabolite of pyridoxine (vitamin B6) in the human body. It is the end product of vitamin B6 catabolism and is excreted in the urine. Pyridoxic acid is formed in the liver by the oxidation of 4-pyridoxic acid, which is a metabolic intermediate in the conversion of pyridoxal 5'-phosphate (the active form of vitamin B6) to 4-pyridoxic acid. Pyridoxic acid has no known coenzyme activity and serves as a marker for vitamin B6 status in the body.

L-serine dehydratase is an enzyme that plays a role in the metabolism of certain amino acids. Specifically, it catalyzes the conversion of L-serine to pyruvate and ammonia. This reaction is part of the pathway that breaks down L-serine to produce energy and intermediates for other biochemical processes in the body.

The systematic name for this enzyme is L-serine deaminase (pyruvate-forming). It is classified as a member of the lyase family of enzymes, which are characterized by their ability to catalyze the breaking of various chemical bonds using a cofactor to provide the energy needed for the reaction. In the case of L-serine dehydratase, the cofactor is a derivative of vitamin B6 called pyridoxal 5'-phosphate (PLP).

Deficiencies or mutations in the gene that encodes L-serine dehydratase can lead to various metabolic disorders, including hypermethioninemia and homocystinuria. These conditions are characterized by abnormal levels of certain amino acids in the blood and urine, which can have serious health consequences if left untreated.

I'm sorry for any confusion, but "picolines" is not a term commonly used in medical definitions. It is a term that refers to a group of chemical compounds known as methylated benzenes or xylenols. They have some industrial uses, but they are not typically relevant in the context of medical definitions or healthcare. If you have any questions related to medical terminology or health concerns, I'd be happy to try and help with those instead!

A lyase is a type of enzyme that catalyzes the breaking of various chemical bonds in a molecule, often resulting in the formation of two new molecules. Lyases differ from other types of enzymes, such as hydrolases and oxidoreductases, because they create double bonds or rings as part of their reaction mechanism.

In the context of medical terminology, lyases are not typically discussed on their own, but rather as a type of enzyme that can be involved in various biochemical reactions within the body. For example, certain lyases play a role in the metabolism of carbohydrates, lipids, and amino acids, among other molecules.

One specific medical application of lyase enzymes is in the diagnosis of certain genetic disorders. For instance, individuals with hereditary fructose intolerance (HFI) lack the enzyme aldolase B, which is a type of lyase that helps break down fructose in the liver. By measuring the activity of aldolase B in a patient's blood or tissue sample, doctors can diagnose HFI and recommend appropriate dietary restrictions to manage the condition.

Overall, while lyases are not a medical diagnosis or condition themselves, they play important roles in various biochemical processes within the body and can be useful in the diagnosis of certain genetic disorders.

A Schiff base is not a medical term per se, but rather a chemical concept that can be relevant in various scientific and medical fields. A Schiff base is a chemical compound that contains a carbon-nitrogen double bond with the nitrogen atom connected to an aryl or alkyl group, excluding hydrogen. This structure is also known as an azomethine.

The general formula for a Schiff base is R1R2C=NR3, where R1 and R2 are organic groups (aryl or alkyl), and R3 is a hydrogen atom or an organic group. These compounds can be synthesized by the condensation of a primary amine with a carbonyl compound, such as an aldehyde or ketone.

Schiff bases have been studied in various medical and biological contexts due to their potential bioactivities. Some Schiff bases exhibit antimicrobial, antifungal, anti-inflammatory, and anticancer properties. They can also serve as ligands for metal ions, forming complexes with potential applications in medicinal chemistry, such as in the development of new drugs or diagnostic agents.

Glycine hydroxymethyltransferase (GHMT or GHT) is an enzyme that plays a crucial role in the metabolic pathway called the methylation cycle, specifically in the synthesis of the amino acid serine and the conversion of glycine. It catalyzes the reversible reaction between glycine and methylene tetrahydrofolate (MTHF) to produce 5,10-methylenetetrahydrofolate and sarcosine.

The reaction can be represented as follows:
Glycine + MTHF ↔ Sarcosine + 5,10-methylenetetrahydrofolate

This enzyme is widely distributed in various tissues, including the liver, kidney, and pancreas. In addition to its role in amino acid metabolism, GHMT also contributes to the regulation of one-carbon metabolism, which is essential for methylation reactions, DNA synthesis, and cellular homeostasis.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Cysteine synthase is an enzyme involved in the biosynthesis of the amino acid cysteine. It catalyzes the reaction that combines O-acetylserine and hydrogen sulfide to produce cysteine and acetic acid. This enzyme plays a crucial role in maintaining the sulfur balance in cells, as cysteine is a sulfur-containing amino acid that is an important component of proteins and many other molecules in the body. There are two forms of cysteine synthase: one that is found in bacteria and plants, and another that is found in animals. The animal form of the enzyme is also known as cystathionine beta-synthase, and it has a broader specificity than the bacterial and plant forms, as it can also catalyze the reaction that produces cystathionine from serine and homocysteine.

Alanine racemase is an enzyme that catalyzes the conversion of the amino acid alanine between its two stereoisomeric forms, D-alanine and L-alanine. This enzyme plays a crucial role in the biosynthesis of peptidoglycan, a major component of bacterial cell walls. In humans, alanine racemase is found in the cytosol of many tissues, including the liver, kidneys, and brain. It is also an important enzyme in the metabolism of amino acids and has been implicated in various disease processes, including neurodegenerative disorders and cancer.

Phosphorylases are enzymes that catalyze the phosphorolytic cleavage of a bond, often a glycosidic bond, in a carbohydrate molecule, releasing a sugar moiety and a phosphate group. This reaction is important in metabolic pathways such as glycogenolysis, where glycogen is broken down into glucose-1-phosphate by the action of glycogen phosphorylase. The resulting glucose-1-phosphate can then be further metabolized to produce energy. Phosphorylases are widely found in nature and play a crucial role in various biological processes, including energy metabolism and signal transduction.

Lysine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. Its chemical formula is (2S)-2,6-diaminohexanoic acid. Lysine is necessary for the growth and maintenance of tissues in the body, and it plays a crucial role in the production of enzymes, hormones, and antibodies. It is also essential for the absorption of calcium and the formation of collagen, which is an important component of bones and connective tissue. Foods that are good sources of lysine include meat, poultry, fish, eggs, and dairy products.

Tyrosine Phenol-Lyase (TyrP or TAL) is not typically defined as a medical term, but rather a biochemical one. It is an enzyme found in bacteria that catalyzes the breakdown of the amino acid L-tyrosine into p-coumaric acid and ammonia. This reaction is part of the tyrosine degradation pathway, which is a series of biochemical reactions that break down L-tyrosine into smaller molecules for energy production or biosynthesis of other compounds.

Medically, understanding the function of Tyrosine Phenol-Lyase can be important in fields such as microbiology and infectious disease, as inhibiting this enzyme may offer a way to control certain bacterial infections. However, it is not a term commonly used in medical diagnosis or treatment.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

D-Alanine transaminase (DAT or Dalat) is an enzyme that catalyzes the reversible transfer of an amino group from D-alanine to α-ketoglutarate, producing pyruvate and D-glutamate. It is found in various bacteria and plays a role in their metabolism. However, it is not typically considered a medically significant enzyme in humans, as it is not commonly used as a clinical marker of liver or other organ function.

Tryptophanase is not a medical term per se, but rather a biochemical term used to describe an enzyme. However, I can provide a biochemical definition for you:

Tryptophanase (TPase or TnaA) is a pyridoxal-phosphate (PLP) dependent enzyme found in certain bacteria, such as Escherichia coli, that catalyzes the breakdown of the essential amino acid tryptophan into several compounds. The primary reaction catalyzed by tryptophanase is the conversion of L-tryptophan to indole, pyruvate, and ammonia. This reaction also produces ATP and ADP as co-products.

The production of indole from tryptophan by tryptophanase has diagnostic value in microbiology, as the presence of indole in a culture medium can indicate the growth of certain bacterial species that produce this enzyme.

Tryptophan synthase is a bacterial enzyme that catalyzes the final step in the biosynthesis of the essential amino acid tryptophan. It is a complex enzyme composed of two types of subunits, α and β, which form an αββα tetrameric structure.

Tryptophan synthase catalyzes the conversion of indole-3-glycerol phosphate (IGP) and L-serine into tryptophan through two separate reactions that occur in a coordinated manner within the active site of the enzyme. In the first reaction, the α subunit catalyzes the breakdown of IGP into indole and glyceraldehyde-3-phosphate (G3P). The indole molecule then moves through a tunnel to the active site of the β subunit, where it is combined with L-serine to form tryptophan in the second reaction.

The overall reaction catalyzed by tryptophan synthase is:

Indole-3-glycerol phosphate + L-serine → L-tryptophan + glyceraldehyde-3-phosphate

Tryptophan synthase plays a critical role in the biosynthesis of tryptophan, which is an essential amino acid that cannot be synthesized by humans and must be obtained through diet. Defects in tryptophan synthase can lead to various genetic disorders, such as hyperbeta-alaninemia and tryptophanuria.

Phosphorylase b is a form of the enzyme glycogen phosphorylase, which is involved in the breakdown of glycogen, a large polymer of glucose, to glucose-1-phosphate. This enzyme plays a crucial role in carbohydrate metabolism, particularly during muscle contraction and liver glycogenolysis (the process of breaking down glycogen in the liver to release glucose into the bloodstream).

Phosphorylase b is an inactive form of the enzyme that can be converted to its active form, phosphorylase a, through the addition of a phosphate group by another enzyme called phosphorylase kinase. This conversion is part of a signaling cascade that activates glycogen breakdown in response to hormonal signals (such as epinephrine or glucagon) and metabolic demands (like muscle contraction).

The interconversion between phosphorylase b and phosphorylase a is an essential mechanism for regulating glycogen metabolism, allowing the body to rapidly respond to changing energy needs.

Carboxy-lyases are a class of enzymes that catalyze the removal of a carboxyl group from a substrate, often releasing carbon dioxide in the process. These enzymes play important roles in various metabolic pathways, such as the biosynthesis and degradation of amino acids, sugars, and other organic compounds.

Carboxy-lyases are classified under EC number 4.2 in the Enzyme Commission (EC) system. They can be further divided into several subclasses based on their specific mechanisms and substrates. For example, some carboxy-lyases require a cofactor such as biotin or thiamine pyrophosphate to facilitate the decarboxylation reaction, while others do not.

Examples of carboxy-lyases include:

1. Pyruvate decarboxylase: This enzyme catalyzes the conversion of pyruvate to acetaldehyde and carbon dioxide during fermentation in yeast and other organisms.
2. Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO): This enzyme is essential for photosynthesis in plants and some bacteria, as it catalyzes the fixation of carbon dioxide into an organic molecule during the Calvin cycle.
3. Phosphoenolpyruvate carboxylase: Found in plants, algae, and some bacteria, this enzyme plays a role in anaplerotic reactions that replenish intermediates in the citric acid cycle. It catalyzes the conversion of phosphoenolpyruvate to oxaloacetate and inorganic phosphate.
4. Aspartate transcarbamylase: This enzyme is involved in the biosynthesis of pyrimidines, a class of nucleotides. It catalyzes the transfer of a carboxyl group from carbamoyl aspartate to carbamoyl phosphate, forming cytidine triphosphate (CTP) and fumarate.
5. Urocanase: Found in animals, this enzyme is involved in histidine catabolism. It catalyzes the conversion of urocanate to formiminoglutamate and ammonia.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

Cystathionine beta-synthase (CBS) is an enzyme that plays a crucial role in the metabolic pathway responsible for the production of the amino acid cysteine from homocysteine. CBS catalyzes the condensation of serine with homocysteine to form cystathionine, which is subsequently hydrolyzed to cysteine and alpha-ketobutyrate by another enzyme called cystathionine gamma-lyase.

CBS requires the cofactor pyridoxal 5'-phosphate (PLP) for its activity and is primarily located in the liver, where it helps regulate homocysteine levels in the body. Elevated levels of homocysteine have been linked to various health issues, including cardiovascular disease and neurological disorders.

In addition to its role in cysteine synthesis, CBS also contributes to the transsulfuration pathway, which is involved in the detoxification of methionine and the production of glutathione, an essential antioxidant in the body. Genetic mutations in the CBS gene can lead to conditions such as homocystinuria, a rare inherited metabolic disorder characterized by elevated levels of homocysteine and methionine in the blood and urine.

Spectrophotometry, Ultraviolet (UV-Vis) is a type of spectrophotometry that measures how much ultraviolet (UV) and visible light is absorbed or transmitted by a sample. It uses a device called a spectrophotometer to measure the intensity of light at different wavelengths as it passes through a sample. The resulting data can be used to determine the concentration of specific components within the sample, identify unknown substances, or evaluate the physical and chemical properties of materials.

UV-Vis spectroscopy is widely used in various fields such as chemistry, biology, pharmaceuticals, and environmental science. It can detect a wide range of substances including organic compounds, metal ions, proteins, nucleic acids, and dyes. The technique is non-destructive, meaning that the sample remains unchanged after the measurement.

In UV-Vis spectroscopy, the sample is placed in a cuvette or other container, and light from a source is directed through it. The light then passes through a monochromator, which separates it into its component wavelengths. The monochromatic light is then directed through the sample, and the intensity of the transmitted or absorbed light is measured by a detector.

The resulting absorption spectrum can provide information about the concentration and identity of the components in the sample. For example, if a compound has a known absorption maximum at a specific wavelength, its concentration can be determined by measuring the absorbance at that wavelength and comparing it to a standard curve.

Overall, UV-Vis spectrophotometry is a versatile and powerful analytical technique for quantitative and qualitative analysis of various samples in different fields.

Tyrosine decarboxylase is an enzyme that catalyzes the decarboxylation of the amino acid tyrosine to form the biogenic amine tyramine. The reaction occurs in the absence of molecular oxygen and requires pyridoxal phosphate as a cofactor. Tyrosine decarboxylase is found in various bacteria, fungi, and plants, and it plays a role in the biosynthesis of alkaloids and other natural products. In humans, tyrosine decarboxylase is not normally present, but its activity has been detected in some tumors and is associated with the production of neurotransmitters in neuronal cells.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Cystathionine is a non-proteinogenic amino acid, which means that it is not used in the synthesis of proteins. It is an intermediate in the biosynthetic pathway that converts the amino acid methionine to cysteine in the body. This process involves the removal of a sulfur atom from methionine, resulting in the formation of cystathionine. Further breakdown of cystathionine leads to the production of cysteine and another amino acid called alpha-ketobutyrate.

Cystathionine plays a crucial role in the metabolism of certain sulfur-containing amino acids, and its levels are regulated by an enzyme called cystathionine beta-synthase (CBS). Genetic defects or deficiencies in this enzyme can result in a disorder known as homocystinuria, which is characterized by the accumulation of homocysteine and methionine in the body and an increased risk of various health complications.

In summary, cystathionine is a biologically important amino acid that functions as an intermediate in the conversion of methionine to cysteine, and its levels are tightly regulated by enzymatic processes in the body.

In the field of organic chemistry, imines are a class of compounds that contain a functional group with the general structure =CR-NR', where C=R and R' can be either alkyl or aryl groups. Imines are also commonly referred to as Schiff bases. They are formed by the condensation of an aldehyde or ketone with a primary amine, resulting in the loss of a molecule of water.

It is important to note that imines do not have a direct medical application, but they can be used as intermediates in the synthesis of various pharmaceuticals and bioactive compounds. Additionally, some imines have been found to exhibit biological activity, such as antimicrobial or anticancer properties. However, these are areas of ongoing research and development.

Semicarbazides are organic compounds that contain the functional group -NH-CO-NH-NH2. They are derivatives of hydrazine and carbamic acid, with the general structure (CH3)NHCSNH2. Semicarbazides are widely used in the synthesis of various chemical compounds, including heterocyclic compounds, pharmaceuticals, and agrochemicals.

In a medical context, semicarbazides themselves do not have any therapeutic use. However, they can be used in the preparation of certain drugs or drug intermediates. For example, semicarbazones, which are derivatives of semicarbazides, can be used to synthesize some antituberculosis drugs.

It is worth noting that semicarbazides and their derivatives have been found to have mutagenic and carcinogenic properties in some studies. Therefore, they should be handled with care in laboratory settings, and exposure should be minimized to reduce potential health risks.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

Ornithine-oxo-acid transaminase (OAT), also known as ornithine aminotransferase, is a urea cycle enzyme that catalyzes the reversible transfer of an amino group from ornithine to α-ketoglutarate, producing glutamate semialdehyde and glutamate. This reaction is an essential part of the urea cycle, which is responsible for the detoxification of ammonia in the body. Deficiencies in OAT can lead to a genetic disorder called ornithine transcarbamylase deficiency (OTCD), which can cause hyperammonemia and neurological symptoms.

5-Aminolevulinate synthase (ALAS) is an enzyme that catalyzes the first step in heme biosynthesis, a metabolic pathway that produces heme, a porphyrin ring with an iron atom at its center. Heme is a crucial component of hemoglobin, cytochromes, and other important molecules in the body.

ALAS exists in two forms: ALAS1 and ALAS2. ALAS1 is expressed in all tissues, while ALAS2 is primarily expressed in erythroid cells (precursors to red blood cells). The reaction catalyzed by ALAS involves the condensation of glycine and succinyl-CoA to form 5-aminolevulinate.

Deficiencies or mutations in the ALAS2 gene can lead to a rare genetic disorder called X-linked sideroblastic anemia, which is characterized by abnormal red blood cell maturation and iron overload in mitochondria.

4-Aminobutyrate transaminase (GABA transaminase or GABA-T) is an enzyme that catalyzes the reversible transfer of an amino group from 4-aminobutyrate (GABA) to 2-oxoglutarate, forming succinic semialdehyde and glutamate. This enzyme plays a crucial role in the metabolism of the major inhibitory neurotransmitter gamma-aminobutyric acid (GABA) in the central nervous system. Inhibition of GABA transaminase is a therapeutic strategy for the treatment of various neurological disorders, such as epilepsy and anxiety, due to its ability to increase GABA levels in the brain.

Coenzymes are small organic molecules that assist enzymes in catalyzing chemical reactions within cells. They typically act as carriers of specific atoms or groups of atoms during enzymatic reactions, facilitating the conversion of substrates into products. Coenzymes often bind temporarily to enzymes at the active site, forming an enzyme-coenzyme complex.

Coenzymes are usually derived from vitamins or minerals and are essential for maintaining proper metabolic functions in the body. Examples of coenzymes include nicotinamide adenine dinucleotide (NAD+), flavin adenine dinucleotide (FAD), and coenzyme A (CoA). When a coenzyme is used up in a reaction, it must be regenerated or replaced for the enzyme to continue functioning.

In summary, coenzymes are vital organic compounds that work closely with enzymes to facilitate biochemical reactions, ensuring the smooth operation of various metabolic processes within living organisms.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Carbon-sulfur lyases are a class of enzymes that catalyze the cleavage of carbon-sulfur bonds in organic compounds, resulting in the formation of a new double bond. These enzymes play important roles in various biological processes, including the metabolism of sulfur-containing amino acids and the biosynthesis of certain cofactors and secondary metabolites.

Carbon-sulfur lyases are classified under EC number 4.4.1, which includes enzymes that catalyze the formation of carbon-carbon bonds by means other than those involving oxidoreductases. Within this class, carbon-sulfur lyases are further divided into several subcategories based on their specific reaction mechanisms and substrate specificities.

One example of a carbon-sulfur lyase is cysteine desulfurase (EC 2.8.1.7), which catalyzes the formation of alanine and a persulfide group from L-cysteine, releasing elemental sulfur as a byproduct. This enzyme plays a critical role in the biosynthesis of iron-sulfur clusters, which are essential cofactors for many proteins involved in electron transfer reactions.

Another example is 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2), which catalyzes the formation of a persulfide group on a cysteine residue in the enzyme itself, using 3-mercaptopyruvate as a sulfur donor. This enzyme is involved in the biosynthesis of various secondary metabolites containing sulfur atoms, such as allicin in garlic and penicillamine in certain fungi.

Overall, carbon-sulfur lyases are important enzymes that play critical roles in various biological processes involving the cleavage or formation of carbon-sulfur bonds.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Fluorescence spectrometry is a type of analytical technique used to investigate the fluorescent properties of a sample. It involves the measurement of the intensity of light emitted by a substance when it absorbs light at a specific wavelength and then re-emits it at a longer wavelength. This process, known as fluorescence, occurs because the absorbed energy excites electrons in the molecules of the substance to higher energy states, and when these electrons return to their ground state, they release the excess energy as light.

Fluorescence spectrometry typically measures the emission spectrum of a sample, which is a plot of the intensity of emitted light versus the wavelength of emission. This technique can be used to identify and quantify the presence of specific fluorescent molecules in a sample, as well as to study their photophysical properties.

Fluorescence spectrometry has many applications in fields such as biochemistry, environmental science, and materials science. For example, it can be used to detect and measure the concentration of pollutants in water samples, to analyze the composition of complex biological mixtures, or to study the properties of fluorescent nanomaterials.

Affinity labels are chemical probes or reagents that can selectively and covalently bind to a specific protein or biomolecule based on its biological function or activity. These labels contain a functional group that interacts with the target molecule, often through non-covalent interactions such as hydrogen bonding, van der Waals forces, or ionic bonds. Once bound, the label then forms a covalent bond with the target molecule, allowing for its isolation and further study.

Affinity labels are commonly used in biochemistry and molecular biology research to identify and characterize specific proteins, enzymes, or receptors. They can be designed to bind to specific active sites, binding pockets, or other functional regions of a protein, allowing researchers to study the structure-function relationships of these molecules.

One example of an affinity label is a substrate analogue that contains a chemically reactive group. This type of affinity label can be used to identify and characterize enzymes by binding to their active sites and forming a covalent bond with the enzyme. The labeled enzyme can then be purified and analyzed to determine its structure, function, and mechanism of action.

Overall, affinity labels are valuable tools for studying the properties and functions of biological molecules in vitro and in vivo.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Isoniazid is an antimicrobial medication used for the prevention and treatment of tuberculosis (TB). It is a first-line medication, often used in combination with other TB drugs, to kill the Mycobacterium tuberculosis bacteria that cause TB. Isoniazid works by inhibiting the synthesis of mycolic acids, which are essential components of the bacterial cell wall. This leads to bacterial death and helps to control the spread of TB.

Isoniazid is available in various forms, including tablets, capsules, and liquid solutions. It can be taken orally or given by injection. The medication is generally well-tolerated, but it can cause side effects such as peripheral neuropathy, hepatitis, and skin rashes. Regular monitoring of liver function tests and supplementation with pyridoxine (vitamin B6) may be necessary to prevent or manage these side effects.

It is important to note that Isoniazid is not effective against drug-resistant strains of TB, and its use should be guided by the results of drug susceptibility testing. Additionally, it is essential to complete the full course of treatment as prescribed to ensure the successful eradication of the bacteria and prevent the development of drug-resistant strains.

Homocystinuria is a genetic disorder characterized by the accumulation of homocysteine and its metabolites in the body due to a deficiency in the enzyme cystathionine beta-synthase (CBS). This enzyme is responsible for converting homocysteine to cystathionine, which is a critical step in the metabolic pathway that breaks down methionine.

As a result of this deficiency, homocysteine levels in the blood increase and can lead to various health problems, including neurological impairment, ocular abnormalities (such as ectopia lentis or dislocation of the lens), skeletal abnormalities (such as Marfan-like features), and vascular complications.

Homocystinuria can be diagnosed through newborn screening or by measuring homocysteine levels in the blood or urine. Treatment typically involves a low-methionine diet, supplementation with vitamin B6 (pyridoxine), betaine, and/or methylcobalamin (a form of vitamin B12) to help reduce homocysteine levels and prevent complications associated with the disorder.

Dopa decarboxylase (DDC) is an enzyme that plays a crucial role in the synthesis of dopamine and serotonin, two important neurotransmitters in the human body. This enzyme is responsible for converting levodopa (L-DOPA), an amino acid precursor, into dopamine, a critical neurotransmitter involved in movement regulation, motivation, reward, and mood.

The gene that encodes dopa decarboxylase is DDC, located on chromosome 7p12.2-p12.1. The enzyme is widely expressed throughout the body, including the brain, kidneys, liver, and gut. In addition to its role in neurotransmitter synthesis, dopa decarboxylase also contributes to the metabolism of certain drugs, such as levodopa and carbidopa, which are used in the treatment of Parkinson's disease.

Deficiencies or mutations in the DDC gene can lead to various neurological disorders, including aromatic L-amino acid decarboxylase deficiency (AADCD), a rare autosomal recessive disorder characterized by decreased levels of dopamine and serotonin. Symptoms of AADCD may include developmental delay, movement disorders, seizures, autonomic dysfunction, and oculogyric crises.

Cystathionine gamma-lyase (CSE or CGL) is an enzyme that plays a role in the metabolism of sulfur-containing amino acids, specifically methionine and cysteine. It catalyzes the conversion of cystathionine to cysteine, releasing α-ketobutyrate and ammonia as byproducts. This reaction also results in the formation of hydrogen sulfide (H2S), a gaseous signaling molecule that has been implicated in various physiological and pathophysiological processes.

Cystathionine gamma-lyase is primarily expressed in the liver, kidney, and brain, and its activity is regulated by several factors, including the availability of its substrates and allosteric modulators like S-adenosylmethionine (SAM) and homocysteine. Dysregulation of CSE has been associated with various diseases, such as cardiovascular disorders, neurodegenerative conditions, and cancer. Therefore, understanding the function and regulation of cystathionine gamma-lyase is crucial for developing novel therapeutic strategies targeting these diseases.

Sideroblastic anemia is a type of anemia characterized by the presence of ringed sideroblasts in the bone marrow. Ringed sideroblasts are red blood cell precursors that have an abnormal amount of iron accumulated in their mitochondria, which forms a ring around the nucleus. This results in the production of abnormal hemoglobin and impaired oxygen transport.

Sideroblastic anemia can be classified as congenital or acquired. Congenital sideroblastic anemias are caused by genetic defects that affect heme synthesis or mitochondrial function, while acquired sideroblastic anemias are associated with various conditions such as myelodysplastic syndromes, chronic alcoholism, lead toxicity, and certain medications.

Symptoms of sideroblastic anemia may include fatigue, weakness, shortness of breath, and pallor. Diagnosis is typically made through a bone marrow aspiration and biopsy, which can identify the presence of ringed sideroblasts. Treatment depends on the underlying cause but may include iron chelation therapy, vitamin B6 supplementation, or blood transfusions.

Glutarates are compounds that contain a glutaric acid group. Glutaric acid is a carboxylic acid with a five-carbon chain and two carboxyl groups at the 1st and 5th carbon positions. Glutarates can be found in various substances, including certain foods and medications.

In a medical context, glutarates are sometimes used as ingredients in pharmaceutical products. For example, sodium phenylbutyrate, which is a salt of phenylbutyric acid and butyric acid, contains a glutaric acid group and is used as a medication to treat urea cycle disorders.

Glutarates can also be found in some metabolic pathways in the body, where they play a role in energy production and other biochemical processes. However, abnormal accumulation of glutaric acid or its derivatives can lead to certain medical conditions, such as glutaric acidemia type I, which is an inherited disorder of metabolism that can cause neurological symptoms and other health problems.

Alpha-ketoglutaric acid, also known as 2-oxoglutarate, is not an acid in the traditional sense but is instead a key molecule in the Krebs cycle (citric acid cycle), which is a central metabolic pathway involved in cellular respiration. Alpha-ketoglutaric acid is a crucial intermediate in the process of converting carbohydrates, fats, and proteins into energy through oxidation. It plays a vital role in amino acid synthesis and the breakdown of certain amino acids. Additionally, it serves as an essential cofactor for various enzymes involved in numerous biochemical reactions within the body. Any medical conditions or disorders related to alpha-ketoglutaric acid would typically be linked to metabolic dysfunctions or genetic defects affecting the Krebs cycle.

Apoproteins are the protein components of lipoprotein complexes, which are responsible for transporting fat molecules, such as cholesterol and triglycerides, throughout the body. Apoproteins play a crucial role in the metabolism of lipids by acting as recognition signals that allow lipoproteins to interact with specific receptors on cell surfaces.

There are several different types of apoproteins, each with distinct functions. For example, apolipoprotein A-1 (apoA-1) is the major protein component of high-density lipoproteins (HDL), which are responsible for transporting excess cholesterol from tissues to the liver for excretion. Apolipoprotein B (apoB) is a large apoprotein found in low-density lipoproteins (LDL), very low-density lipoproteins (VLDL), and lipoprotein(a). ApoB plays a critical role in the assembly and secretion of VLDL from the liver, and it also mediates the uptake of LDL by cells.

Abnormalities in apoprotein levels or function can contribute to the development of various diseases, including cardiovascular disease, diabetes, and Alzheimer's disease. Therefore, measuring apoprotein levels in the blood can provide valuable information for diagnosing and monitoring these conditions.

Erythrocytes, also known as red blood cells (RBCs), are the most common type of blood cell in circulating blood in mammals. They are responsible for transporting oxygen from the lungs to the body's tissues and carbon dioxide from the tissues to the lungs.

Erythrocytes are formed in the bone marrow and have a biconcave shape, which allows them to fold and bend easily as they pass through narrow blood vessels. They do not have a nucleus or mitochondria, which makes them more flexible but also limits their ability to reproduce or repair themselves.

In humans, erythrocytes are typically disc-shaped and measure about 7 micrometers in diameter. They contain the protein hemoglobin, which binds to oxygen and gives blood its red color. The lifespan of an erythrocyte is approximately 120 days, after which it is broken down in the liver and spleen.

Abnormalities in erythrocyte count or function can lead to various medical conditions, such as anemia, polycythemia, and sickle cell disease.

Circular dichroism (CD) is a technique used in physics and chemistry to study the structure of molecules, particularly large biological molecules such as proteins and nucleic acids. It measures the difference in absorption of left-handed and right-handed circularly polarized light by a sample. This difference in absorption can provide information about the three-dimensional structure of the molecule, including its chirality or "handedness."

In more technical terms, CD is a form of spectroscopy that measures the differential absorption of left and right circularly polarized light as a function of wavelength. The CD signal is measured in units of millidegrees (mdeg) and can be positive or negative, depending on the type of chromophore and its orientation within the molecule.

CD spectra can provide valuable information about the secondary and tertiary structure of proteins, as well as the conformation of nucleic acids. For example, alpha-helical proteins typically exhibit a strong positive band near 190 nm and two negative bands at around 208 nm and 222 nm, while beta-sheet proteins show a strong positive band near 195 nm and two negative bands at around 217 nm and 175 nm.

CD spectroscopy is a powerful tool for studying the structural changes that occur in biological molecules under different conditions, such as temperature, pH, or the presence of ligands or other molecules. It can also be used to monitor the folding and unfolding of proteins, as well as the binding of drugs or other small molecules to their targets.

Biocatalysis is the use of living organisms or their components, such as enzymes, to accelerate chemical reactions. In other words, it is the process by which biological systems, including cells, tissues, and organs, catalyze chemical transformations. Biocatalysts, such as enzymes, can increase the rate of a reaction by lowering the activation energy required for the reaction to occur. They are highly specific and efficient, making them valuable tools in various industries, including pharmaceuticals, food and beverage, and biofuels.

In medicine, biocatalysis is used in the production of drugs, such as antibiotics and hormones, as well as in diagnostic tests. Enzymes are also used in medical treatments, such as enzyme replacement therapy for genetic disorders that affect enzyme function. Overall, biocatalysis plays a critical role in many areas of medicine and healthcare.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Aldehydes are a class of organic compounds characterized by the presence of a functional group consisting of a carbon atom bonded to a hydrogen atom and a double bonded oxygen atom, also known as a formyl or aldehyde group. The general chemical structure of an aldehyde is R-CHO, where R represents a hydrocarbon chain.

Aldehydes are important in biochemistry and medicine as they are involved in various metabolic processes and are found in many biological molecules. For example, glucose is converted to pyruvate through a series of reactions that involve aldehyde intermediates. Additionally, some aldehydes have been identified as toxicants or environmental pollutants, such as formaldehyde, which is a known carcinogen and respiratory irritant.

Formaldehyde is also commonly used in medical and laboratory settings for its disinfectant properties and as a fixative for tissue samples. However, exposure to high levels of formaldehyde can be harmful to human health, causing symptoms such as coughing, wheezing, and irritation of the eyes, nose, and throat. Therefore, appropriate safety measures must be taken when handling aldehydes in medical and laboratory settings.

Tyrosine transaminase, also known as tyrosine aminotransferase or TAT, is an enzyme that plays a crucial role in the metabolism of the amino acid tyrosine. This enzyme catalyzes the transfer of an amino group from tyrosine to a ketoacid, such as alpha-ketoglutarate, resulting in the formation of a new amino acid, glutamate, and a ketone derivative of tyrosine.

Tyrosine transaminase is primarily found in the liver and its activity can be used as a biomarker for liver function. Increased levels of this enzyme in the blood may indicate liver damage or disease, such as hepatitis or cirrhosis. Therefore, measuring tyrosine transaminase activity is often part of routine liver function tests.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

I'm sorry for any confusion, but "xanthurenates" is not a recognized term in medicine or physiology. It seems that you might be referring to "xanthurenic acid," which is a metabolic byproduct produced during the breakdown of the amino acid tryptophan. An accumulation of xanthurenic acid can occur due to certain genetic disorders, such as Hartnup disease or defects in the coenzyme Q10 synthesis pathway. However, without more context, it's difficult for me to provide a precise definition related to your specific question. If you could provide additional information, I would be happy to help further!

Vitamin B Complex refers to a group of water-soluble vitamins that play essential roles in cell metabolism, cellular function, and formation of red blood cells. This complex includes 8 distinct vitamins, all of which were originally thought to be the same vitamin when first discovered. They are now known to have individual structures and specific functions.

1. Vitamin B1 (Thiamin): Necessary for energy production and nerve function.
2. Vitamin B2 (Riboflavin): Involved in energy production and growth.
3. Vitamin B3 (Niacin): Assists in energy production, DNA repair, and acts as a co-factor for various enzymes.
4. Vitamin B5 (Pantothenic Acid): Plays a role in the synthesis of Coenzyme A, which is vital for fatty acid metabolism.
5. Vitamin B6 (Pyridoxine): Needed for protein metabolism, neurotransmitter synthesis, hemoglobin formation, and immune function.
6. Vitamin B7 (Biotin): Involved in fatty acid synthesis, glucose metabolism, and nail and hair health.
7. Vitamin B9 (Folate or Folic Acid): Essential for DNA replication, cell division, and the production of red blood cells.
8. Vitamin B12 (Cobalamin): Necessary for nerve function, DNA synthesis, and the production of red blood cells.

These vitamins are often found together in various foods, and a balanced diet usually provides sufficient amounts of each. Deficiencies can lead to specific health issues related to the functions of each particular vitamin.

"Swine" is a common term used to refer to even-toed ungulates of the family Suidae, including domestic pigs and wild boars. However, in a medical context, "swine" often appears in the phrase "swine flu," which is a strain of influenza virus that typically infects pigs but can also cause illness in humans. The 2009 H1N1 pandemic was caused by a new strain of swine-origin influenza A virus, which was commonly referred to as "swine flu." It's important to note that this virus is not transmitted through eating cooked pork products; it spreads from person to person, mainly through respiratory droplets produced when an infected person coughs or sneezes.

Glycine is a simple amino acid that plays a crucial role in the body. According to the medical definition, glycine is an essential component for the synthesis of proteins, peptides, and other biologically important compounds. It is also involved in various metabolic processes, such as the production of creatine, which supports muscle function, and the regulation of neurotransmitters, affecting nerve impulse transmission and brain function. Glycine can be found as a free form in the body and is also present in many dietary proteins.

Iron chelating agents are medications that bind to iron in the body, forming a stable complex that can then be excreted from the body. These agents are primarily used to treat iron overload, a condition that can occur due to frequent blood transfusions or certain genetic disorders such as hemochromatosis. By reducing the amount of iron in the body, these medications can help prevent or reduce damage to organs such as the heart and liver. Examples of iron chelating agents include deferoxamine, deferasirox, and deferiprone.

Riboflavin, also known as vitamin B2, is a water-soluble vitamin that plays a crucial role in energy production and cellular function, growth, and development. It is essential for the metabolism of carbohydrates, fats, and proteins, and it helps to maintain healthy skin, hair, and nails. Riboflavin is involved in the production of energy by acting as a coenzyme in various redox reactions. It also contributes to the maintenance of the mucous membranes of the digestive tract and promotes iron absorption.

Riboflavin can be found in a variety of foods, including milk, cheese, leafy green vegetables, liver, kidneys, legumes, yeast, mushrooms, and almonds. It is sensitive to light and heat, so exposure to these elements can lead to its degradation and loss of vitamin activity.

Deficiency in riboflavin is rare but can occur in individuals with poor dietary intake or malabsorption disorders. Symptoms of riboflavin deficiency include inflammation of the mouth and tongue, anemia, skin disorders, and neurological symptoms such as confusion and mood changes. Riboflavin supplements are available for those who have difficulty meeting their daily requirements through diet alone.

Hemoglobin C disease is a genetic disorder that affects the structure and function of hemoglobin, a protein in red blood cells responsible for carrying oxygen throughout the body. The disease is caused by a mutation in the gene that produces the beta-globin chain of hemoglobin, resulting in the production of an abnormal form of hemoglobin called Hemoglobin C (HbC).

People with Hemoglobin C disease inherit one copy of the HbC gene from each parent. This means they have two copies of the mutated gene and produce mostly Hemoglobin C, instead of the normal Hemoglobin A. The presence of Hemoglobin C can cause the red blood cells to become rigid and fragile, leading to a condition called hemolytic anemia.

Symptoms of Hemoglobin C disease may include fatigue, weakness, shortness of breath, pale skin, jaundice, and dark urine. The severity of the symptoms can vary widely from person to person, with some individuals experiencing mild symptoms and others having more severe complications.

Hemoglobin C disease is a chronic condition that requires ongoing medical management, including regular monitoring of hemoglobin levels, iron status, and other blood parameters. Treatment may include blood transfusions, folic acid supplementation, and medications to manage symptoms such as anemia and pain.

It's important to note that Hemoglobin C disease is not the same as sickle cell disease, which is another genetic disorder that affects hemoglobin structure and function. While both conditions can cause hemolytic anemia, they are caused by different mutations in the beta-globin gene and have distinct clinical features and management approaches.

Phosphotransferases are a group of enzymes that catalyze the transfer of a phosphate group from a donor molecule to an acceptor molecule. This reaction is essential for various cellular processes, including energy metabolism, signal transduction, and biosynthesis.

The systematic name for this group of enzymes is phosphotransferase, which is derived from the general reaction they catalyze: D-donor + A-acceptor = D-donor minus phosphate + A-phosphate. The donor molecule can be a variety of compounds, such as ATP or a phosphorylated protein, while the acceptor molecule is typically a compound that becomes phosphorylated during the reaction.

Phosphotransferases are classified into several subgroups based on the type of donor and acceptor molecules they act upon. For example, kinases are a subgroup of phosphotransferases that transfer a phosphate group from ATP to a protein or other organic compound. Phosphatases, another subgroup, remove phosphate groups from molecules by transferring them to water.

Overall, phosphotransferases play a critical role in regulating many cellular functions and are important targets for drug development in various diseases, including cancer and neurological disorders.

Glyceraldehyde 3-phosphate (G3P) is a crucial intermediate in both glycolysis and gluconeogenesis metabolic pathways. It is an triose sugar phosphate, which means it contains three carbon atoms and has a phosphate group attached to it.

In the glycolysis process, G3P is produced during the third step of the process from the molecule dihydroxyacetone phosphate (DHAP) via the enzyme triosephosphate isomerase. In the following steps, G3P is converted into 1,3-bisphosphoglycerate, which eventually leads to the production of ATP and NADH.

In gluconeogenesis, G3P is produced from the reverse reaction of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase, using the molecule dihydroxyacetone phosphate (DHAP) as a starting point. G3P is then converted into glucose-6-phosphate, which can be further metabolized or released from the cell.

It's important to note that Glyceraldehyde 3-Phosphate plays a key role in energy production and carbohydrate metabolism.

I'm sorry for any confusion, but "Hydro-Lyases" is not a recognized medical term or category in biochemistry. It seems like there might be a misunderstanding or a typo in the term.

In biochemistry, "lyases" are enzymes that catalyze the removal of groups from substrates by means other than hydrolysis or oxidation, often forming a double bond or a ring-forming reaction. They are classified and named based on the type of bond they break.

If you meant to ask about a specific enzyme or reaction, could you please provide more context or clarify the term? I'd be happy to help further with accurate information.

I'm sorry for any confusion, but "spectrum analysis" is not a commonly used medical term. Spectrum analysis is a term that is more frequently used in the fields of physics, mathematics, and engineering to describe the process of breaking down a signal or a wave into its different frequencies and amplitudes, creating a visual representation called a spectrum.

If you have any concerns about a medical issue, I would recommend consulting with a healthcare professional for accurate information and guidance.

Histidine Decarboxylase is a medical term that refers to an enzyme found in various organisms, including humans. This enzyme plays a crucial role in the conversion of the amino acid L-histidine into histamine, which is a biogenic amine that acts as a neurotransmitter and inflammatory mediator in the human body.

Histidine decarboxylase is found in several tissues, including the central nervous system, gastrointestinal tract, and skin. It requires pyridoxal 5'-phosphate (PLP) as a cofactor for its enzymatic activity. Abnormal levels or activity of histidine decarboxylase have been implicated in several medical conditions, including allergic reactions, inflammation, and neuropsychiatric disorders.

Inhibitors of histidine decarboxylase are being investigated as potential therapeutic agents for the treatment of various diseases, such as mast cell-mediated disorders, gastrointestinal disorders, and neurological conditions associated with abnormal histamine levels.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

Starch phosphorylase is an enzyme that catalyzes the phosphorolytic cleavage of alpha-1,4 glycosidic bonds in starch and related polysaccharides, releasing alpha-D-glucose 1-phosphate molecules. It is found in various tissues, including muscle and liver, and plays a role in carbohydrate metabolism by helping to regulate the breakdown and synthesis of glycogen, which is a storage form of glucose.

The enzyme works by transferring a phosphate group from inorganic phosphate to the terminal alpha-1,4 linked glucosyl residue of the substrate, resulting in the formation of glucose 1-phosphate and a shortened polysaccharide chain. This reaction is reversible, allowing the enzyme to also participate in glycogen synthesis by adding glucose units to the non-reducing end of the glycogen molecule.

Starch phosphorylase is important for maintaining normal blood glucose levels and providing energy to cells during periods of fasting or exercise. Deficiencies in this enzyme can lead to metabolic disorders, such as glycogen storage disease type VI (Hers disease), which is characterized by the accumulation of abnormal glycogen molecules in the liver and muscle tissue.

Alcohol oxidoreductases are a class of enzymes that catalyze the oxidation of alcohols to aldehydes or ketones, while reducing nicotinamide adenine dinucleotide (NAD+) to NADH. These enzymes play an important role in the metabolism of alcohols and other organic compounds in living organisms.

The most well-known example of an alcohol oxidoreductase is alcohol dehydrogenase (ADH), which is responsible for the oxidation of ethanol to acetaldehyde in the liver during the metabolism of alcoholic beverages. Other examples include aldehyde dehydrogenases (ALDH) and sorbitol dehydrogenase (SDH).

These enzymes are important targets for the development of drugs used to treat alcohol use disorder, as inhibiting their activity can help to reduce the rate of ethanol metabolism and the severity of its effects on the body.

Homocysteine is an amino acid that is formed in the body during the metabolism of another amino acid called methionine. It's an important intermediate in various biochemical reactions, including the synthesis of proteins, neurotransmitters, and other molecules. However, elevated levels of homocysteine in the blood (a condition known as hyperhomocysteinemia) have been linked to several health issues, such as cardiovascular disease, stroke, and cognitive decline.

Homocysteine can be converted back to methionine with the help of vitamin B12 and a cofactor called betaine, or it can be converted to another amino acid called cystathionine with the help of vitamin B6 and folate (vitamin B9). Imbalances in these vitamins and other factors can lead to an increase in homocysteine levels.

It is crucial to maintain normal homocysteine levels for overall health, as high levels may contribute to the development of various diseases. Regular monitoring and maintaining a balanced diet rich in folate, vitamin B6, and vitamin B12 can help regulate homocysteine levels and reduce the risk of related health issues.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Intramolecular transferases are a specific class of enzymes that catalyze the transfer of a functional group from one part of a molecule to another within the same molecule. These enzymes play a crucial role in various biochemical reactions, including the modification of complex carbohydrates, lipids, and nucleic acids. By facilitating intramolecular transfers, these enzymes help regulate cellular processes, signaling pathways, and metabolic functions.

The systematic name for this class of enzymes is: [donor group]-transferring intramolecular transferases. The classification system developed by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) categorizes them under EC 2.5. This category includes enzymes that transfer alkyl or aryl groups, other than methyl groups; methyl groups; hydroxylyl groups, including glycosyl groups; and various other specific functional groups.

Examples of intramolecular transferases include:

1. Protein kinases (EC 2.7.11): Enzymes that catalyze the transfer of a phosphate group from ATP to a specific amino acid residue within a protein, thereby regulating protein function and cellular signaling pathways.
2. Glycosyltransferases (EC 2.4): Enzymes that facilitate the transfer of glycosyl groups between donor and acceptor molecules; some of these enzymes can catalyze intramolecular transfers, playing a role in the biosynthesis and modification of complex carbohydrates.
3. Methyltransferases (EC 2.1): Enzymes that transfer methyl groups between donor and acceptor molecules; some of these enzymes can catalyze intramolecular transfers, contributing to the regulation of gene expression and other cellular processes.

Understanding the function and regulation of intramolecular transferases is essential for elucidating their roles in various biological processes and developing targeted therapeutic strategies for diseases associated with dysregulation of these enzymes.

Hypophosphatasia is a rare inherited metabolic disorder characterized by defective bone mineralization due to deficiency of alkaline phosphatase, an enzyme that is crucial for the formation of strong and healthy bones. This results in skeletal abnormalities, including softening and weakening of the bones (rickets in children and osteomalacia in adults), premature loss of teeth, and an increased risk of fractures.

The disorder can vary widely in severity, from mild cases with few symptoms to severe forms that can lead to disability or even be life-threatening in infancy. Hypophosphatasia is caused by mutations in the ALPL gene, which provides instructions for making the tissue non-specific alkaline phosphatase (TNSALP) enzyme. Inheritance is autosomal recessive, meaning an individual must inherit two copies of the mutated gene (one from each parent) to have the condition.

Dialysis is a medical treatment that is used to remove waste and excess fluid from the blood when the kidneys are no longer able to perform these functions effectively. This life-sustaining procedure uses a specialized machine, called a dialyzer or artificial kidney, to filter the blood outside of the body and return clean, chemically balanced blood back into the body.

There are two main types of dialysis: hemodialysis and peritoneal dialysis.

1. Hemodialysis: In this method, a patient's blood is passed through an external filter (dialyzer) that removes waste products, toxins, and excess fluids. The cleaned blood is then returned to the body with the help of a specialized machine. Hemodialysis typically requires access to a large vein, often created by a surgical procedure called an arteriovenous (AV) fistula or graft. Hemodialysis sessions usually last for about 3-5 hours and are performed three times a week in a clinical setting, such as a dialysis center or hospital.
2. Peritoneal Dialysis: This method uses the lining of the patient's own abdomen (peritoneum) as a natural filter to clean the blood. A sterile dialysate solution is introduced into the peritoneal cavity via a permanently implanted catheter. The solution absorbs waste products and excess fluids from the blood vessels lining the peritoneum through a process called diffusion. After a dwell time, usually several hours, the used dialysate is drained out and replaced with fresh dialysate. This process is known as an exchange and is typically repeated multiple times throughout the day or night, depending on the specific type of peritoneal dialysis (continuous ambulatory peritoneal dialysis or automated peritoneal dialysis).

Both methods have their advantages and disadvantages, and the choice between them depends on various factors, such as a patient's overall health, lifestyle, and personal preferences. Dialysis is a life-saving treatment for people with end-stage kidney disease or severe kidney dysfunction, allowing them to maintain their quality of life and extend their lifespan until a kidney transplant becomes available or their kidney function improves.

A skin cream is not a medical term per se, but it generally refers to a topical emollient preparation intended for application to the skin. It contains a mixture of water, oil, and active ingredients, which are formulated to provide various benefits such as moisturizing, protecting, soothing, or treating specific skin conditions. The exact definition and composition may vary depending on the product's intended use and formulation.

Examples of active ingredients in skin creams include:

1. Moisturizers (e.g., glycerin, hyaluronic acid) - help to retain water in the skin, making it feel softer and smoother.
2. Emollients (e.g., shea butter, coconut oil, petrolatum) - provide a protective barrier that helps prevent moisture loss and soften the skin.
3. Humectants (e.g., urea, lactic acid, alpha-hydroxy acids) - attract water from the environment or deeper layers of the skin to hydrate the surface.
4. Anti-inflammatory agents (e.g., hydrocortisone, aloe vera) - help reduce redness, swelling, and itching associated with various skin conditions.
5. Antioxidants (e.g., vitamin C, vitamin E, green tea extract) - protect the skin from free radical damage and environmental stressors that can lead to premature aging.
6. Sunscreen agents (e.g., zinc oxide, titanium dioxide, chemical filters) - provide broad-spectrum protection against UVA and UVB rays.
7. Skin lighteners (e.g., hydroquinone, kojic acid, arbutin) - help reduce the appearance of hyperpigmentation and even out skin tone.
8. Acne treatments (e.g., benzoyl peroxide, salicylic acid, retinoids) - target acne-causing bacteria, unclog pores, and regulate cell turnover to prevent breakouts.

It is essential to choose a skin cream based on your specific skin type and concerns, as well as any medical conditions or allergies you may have. Always consult with a dermatologist or healthcare provider before starting a new skincare regimen.

Serine is an amino acid, which is a building block of proteins. More specifically, it is a non-essential amino acid, meaning that the body can produce it from other compounds, and it does not need to be obtained through diet. Serine plays important roles in the body, such as contributing to the formation of the protective covering of nerve fibers (myelin sheath), helping to synthesize another amino acid called tryptophan, and taking part in the metabolism of fatty acids. It is also involved in the production of muscle tissues, the immune system, and the forming of cell structures. Serine can be found in various foods such as soy, eggs, cheese, meat, peanuts, lentils, and many others.

Purinergic P2 receptor antagonists are pharmaceutical agents that block the activity of P2 receptors, which are a type of cell surface receptor that binds extracellular nucleotides such as ATP and ADP. These receptors play important roles in various physiological processes, including neurotransmission, inflammation, and platelet aggregation.

P2 receptors are divided into two main subfamilies: P2X and P2Y. The P2X receptors are ligand-gated ion channels that allow the flow of ions across the cell membrane upon activation, while the P2Y receptors are G protein-coupled receptors that activate intracellular signaling pathways.

Purinergic P2 receptor antagonists are used in clinical medicine to treat various conditions, such as chronic pain, urinary incontinence, and cardiovascular diseases. For example, the P2X3 receptor antagonist gefapixant is being investigated for the treatment of refractory chronic cough, while the P2Y12 receptor antagonists clopidogrel and ticagrelor are used to prevent thrombosis in patients with acute coronary syndrome.

Overall, purinergic P2 receptor antagonists offer a promising therapeutic approach for various diseases by targeting specific receptors involved in pathological processes.

In the context of medicine, "chemistry" often refers to the field of study concerned with the properties, composition, and structure of elements and compounds, as well as their reactions with one another. It is a fundamental science that underlies much of modern medicine, including pharmacology (the study of drugs), toxicology (the study of poisons), and biochemistry (the study of the chemical processes that occur within living organisms).

In addition to its role as a basic science, chemistry is also used in medical testing and diagnosis. For example, clinical chemistry involves the analysis of bodily fluids such as blood and urine to detect and measure various substances, such as glucose, cholesterol, and electrolytes, that can provide important information about a person's health status.

Overall, chemistry plays a critical role in understanding the mechanisms of diseases, developing new treatments, and improving diagnostic tests and techniques.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Carbon-oxygen lyases are a class of enzymes that catalyze the breaking of a carbon-oxygen bond using a molecule of water (H2O), resulting in the formation of an alcohol and a carbonyl group. These enzymes play important roles in various metabolic pathways, including the breakdown of carbohydrates, lipids, and amino acids.

The term "carbon-oxygen lyase" is used to describe enzymes that use a lytic cleavage mechanism to break a carbon-oxygen bond, as opposed to other types of enzymes that use oxidative or reductive mechanisms. These enzymes typically require the presence of cofactors such as metal ions or organic molecules to facilitate the reaction.

Carbon-oxygen lyases can be further classified based on the type of substrate they act upon and the specific reaction they catalyze. For example, some carbon-oxygen lyases are involved in the conversion of glyceraldehyde 3-phosphate to dihydroxyacetone phosphate during glycolysis, while others are involved in the breakdown of lignin, a complex polymer found in plant cell walls.

It's worth noting that carbon-oxygen lyases can also be classified as EC 4.2.1 under the Enzyme Commission (EC) numbering system, which provides a standardized nomenclature for enzymes based on the type of reaction they catalyze.

Edible plants are those that can be safely consumed by humans and other animals as a source of nutrition. They have various parts (such as fruits, vegetables, seeds, roots, stems, and leaves) that can be used for food after being harvested and prepared properly. Some edible plants have been cultivated and domesticated for agricultural purposes, while others are gathered from the wild. It is important to note that not all plants are safe to eat, and some may even be toxic or deadly if consumed. Proper identification and knowledge of preparation methods are crucial before consuming any plant material.

Chemical phenomena refer to the changes and interactions that occur at the molecular or atomic level when chemicals are involved. These phenomena can include chemical reactions, in which one or more substances (reactants) are converted into different substances (products), as well as physical properties that change as a result of chemical interactions, such as color, state of matter, and solubility. Chemical phenomena can be studied through various scientific disciplines, including chemistry, biochemistry, and physics.

A Structure-Activity Relationship (SAR) in the context of medicinal chemistry and pharmacology refers to the relationship between the chemical structure of a drug or molecule and its biological activity or effect on a target protein, cell, or organism. SAR studies aim to identify patterns and correlations between structural features of a compound and its ability to interact with a specific biological target, leading to a desired therapeutic response or undesired side effects.

By analyzing the SAR, researchers can optimize the chemical structure of lead compounds to enhance their potency, selectivity, safety, and pharmacokinetic properties, ultimately guiding the design and development of novel drugs with improved efficacy and reduced toxicity.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

Serine C-palmitoyltransferase (SCPT) is an enzyme responsible for the rate-limiting step in the biosynthesis of sphingolipids, a type of lipid found in cell membranes. Sphingolipids play crucial roles in signal transduction and cell regulation. The enzyme catalyzes the condensation of serine and palmitoyl-CoA to form 3-ketosphinganine, which is then reduced to sphinganine and further modified to produce various sphingolipids. There are two main forms of SCPT, known as SCPT1 and SCPT2, which differ in their subcellular localization and substrate specificity. Defects in the genes encoding these enzymes can lead to serious inherited disorders affecting multiple organ systems, such as hereditary sensory neuropathy type 1 (HSAN1) and forms of ichthyosis.

Glutaminase is an enzyme that catalyzes the conversion of L-glutamine, which is a type of amino acid, into glutamate and ammonia. This reaction is an essential part of nitrogen metabolism in many organisms, including humans. There are several forms of glutaminase found in different parts of the body, with varying properties and functions.

In humans, there are two major types of glutaminase: mitochondrial and cytosolic. Mitochondrial glutaminase is primarily found in the kidneys and brain, where it plays a crucial role in energy metabolism by converting glutamine into glutamate, which can then be further metabolized to produce ATP (adenosine triphosphate), a major source of cellular energy.

Cytosolic glutaminase, on the other hand, is found in many tissues throughout the body and is involved in various metabolic processes, including nucleotide synthesis and protein degradation.

Glutaminase activity has been implicated in several disease states, including cancer, where some tumors have been shown to have elevated levels of glutaminase expression, allowing them to use glutamine as a major source of energy and growth. Inhibitors of glutaminase are currently being investigated as potential therapeutic agents for the treatment of cancer.

Aminooxyacetic acid (AOAA) is a chemical compound that is an irreversible inhibitor of pyridoxal phosphate-dependent enzymes. Pyridoxal phosphate is a cofactor involved in several important biochemical reactions, including the transamination of amino acids. By inhibiting these enzymes, AOAA can alter the normal metabolism of amino acids and other related compounds in the body.

AOAA has been studied for its potential therapeutic uses, such as in the treatment of neurodegenerative disorders like Huntington's disease and epilepsy. However, more research is needed to fully understand its mechanisms of action and potential side effects before it can be used as a routine therapy.

It is important to note that AOAA is not a naturally occurring substance in the human body and should only be used under medical supervision.

Gallium is not a medical term, but it's a chemical element with the symbol Ga and atomic number 31. It is a soft, silvery-blue metal that melts at a temperature just above room temperature. In medicine, gallium compounds such as gallium nitrate and gallium citrate are used as radiopharmaceuticals for diagnostic purposes in nuclear medicine imaging studies, particularly in the detection of inflammation, infection, and some types of cancer.

For example, Gallium-67 is a radioactive isotope that can be injected into the body to produce images of various diseases such as abscesses, osteomyelitis (bone infection), and tumors using a gamma camera. The way gallium distributes in the body can provide valuable information about the presence and extent of disease.

Therefore, while gallium is not a medical term itself, it has important medical applications as a diagnostic tool in nuclear medicine.

L-Lysine 6-Transaminase, also known as L-lysine alpha-ketoglutarate transaminase or AKTA, is an enzyme that catalyzes the transfer of an amino group from L-lysine to alpha-ketoglutarate, resulting in the formation of L-glutamate and saccharopine. This enzyme plays a role in the metabolism of lysine, an essential amino acid, in various organisms including bacteria, yeast, and plants. In humans, this enzyme is not present, but other transaminases such as aspartate transaminase (AST) and alanine transaminase (ALT) are used to indirectly assess liver function.

Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.

During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.

There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.

I'm sorry for any confusion, but "Phosphites" is not a term commonly used in medical definitions. It is a term more frequently used in chemistry and biochemistry, where it refers to salts or esters of phosphorous acid in which the phosphorus has an oxidation state of +3. If you're looking for information on a medical topic, could you please provide more context or clarify what you're asking? I'm here to help!

Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.

Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.

Adenosine diphosphate (ADP) is a chemical compound that plays a crucial role in energy transfer within cells. It is a nucleotide, which consists of a adenosine molecule (a sugar molecule called ribose attached to a nitrogenous base called adenine) and two phosphate groups.

In the cell, ADP functions as an intermediate in the conversion of energy from one form to another. When a high-energy phosphate bond in ADP is broken, energy is released and ADP is converted to adenosine triphosphate (ATP), which serves as the main energy currency of the cell. Conversely, when ATP donates a phosphate group to another molecule, it is converted back to ADP, releasing energy for the cell to use.

ADP also plays a role in blood clotting and other physiological processes. In the coagulation cascade, ADP released from damaged red blood cells can help activate platelets and initiate the formation of a blood clot.

Cysteine is a semi-essential amino acid, which means that it can be produced by the human body under normal circumstances, but may need to be obtained from external sources in certain conditions such as illness or stress. Its chemical formula is HO2CCH(NH2)CH2SH, and it contains a sulfhydryl group (-SH), which allows it to act as a powerful antioxidant and participate in various cellular processes.

Cysteine plays important roles in protein structure and function, detoxification, and the synthesis of other molecules such as glutathione, taurine, and coenzyme A. It is also involved in wound healing, immune response, and the maintenance of healthy skin, hair, and nails.

Cysteine can be found in a variety of foods, including meat, poultry, fish, dairy products, eggs, legumes, nuts, seeds, and some grains. It is also available as a dietary supplement and can be used in the treatment of various medical conditions such as liver disease, bronchitis, and heavy metal toxicity. However, excessive intake of cysteine may have adverse effects on health, including gastrointestinal disturbances, nausea, vomiting, and headaches.

Amino acid isomerases are a class of enzymes that catalyze the conversion of one amino acid stereoisomer to another. These enzymes play a crucial role in the metabolism and biosynthesis of amino acids, which are the building blocks of proteins.

Amino acids can exist in two forms, called L- and D-stereoisomers, based on the spatial arrangement of their constituent atoms around a central carbon atom. While most naturally occurring amino acids are of the L-configuration, some D-amino acids are also found in certain proteins and peptides, particularly in bacteria and lower organisms.

Amino acid isomerases can convert one stereoisomer to another by breaking and reforming chemical bonds in a process that requires energy. This conversion can be important for the proper functioning of various biological processes, such as protein synthesis, neurotransmitter metabolism, and immune response.

Examples of amino acid isomerases include proline racemase, which catalyzes the interconversion of L-proline and D-proline, and serine hydroxymethyltransferase, which converts L-serine to D-serine. These enzymes are essential for maintaining the balance of amino acids in living organisms and have potential therapeutic applications in various diseases, including neurodegenerative disorders and cancer.

I'm sorry for any confusion, but "Oxamic Acid" is not a recognized term in medical terminology or pharmacology. It might be a chemical compound that you're interested in, and its scientific definition is as follows:

Oxamic acid, systematically named as ethanedioloic acid or oxalic acid diethyl ester, is an organic compound with the formula (CH3CH2)2C(COOH)2. It is a colorless liquid that is used as a solvent and in the manufacture of other chemicals.

If you're looking for medical information or definitions related to a different term, please let me know and I would be happy to help!

Nitrogenous group transferases are a class of enzymes that catalyze the transfer of nitrogen-containing groups from one molecule to another. These enzymes play a crucial role in various metabolic pathways, including the biosynthesis and degradation of amino acids, nucleotides, and other nitrogen-containing compounds.

The term "nitrogenous group" refers to any chemical group that contains nitrogen atoms. Examples of nitrogenous groups include amino groups (-NH2), amide groups (-CONH2), and cyano groups (-CN). Transferases that move these groups from one molecule to another are classified as nitrogenous group transferases.

These enzymes typically require cofactors such as ATP, NAD+, or other small molecules to facilitate the transfer of the nitrogenous group. They follow the general reaction mechanism of a transferase enzyme, where the substrate (donor) binds to the active site of the enzyme and transfers its nitrogenous group to an acceptor molecule, resulting in the formation of a new product.

Examples of nitrogenous group transferases include:

* Glutamine synthetase, which catalyzes the conversion of glutamate to glutamine by adding an ammonia group (-NH3) from ATP.
* Aspartate transcarbamylase, which catalyzes the transfer of a carbamoyl group (-CO-NH2) from carbamoyl phosphate to aspartate during pyrimidine biosynthesis.
* Argininosuccinate synthetase, which catalyzes the formation of argininosuccinate by transferring an aspartate group from aspartate to citrulline during the urea cycle.

Understanding nitrogenous group transferases is essential for understanding various metabolic pathways and their regulation in living organisms.

Ornithine is not a medical condition but a naturally occurring alpha-amino acid, which is involved in the urea cycle, a process that eliminates ammonia from the body. Here's a brief medical/biochemical definition of Ornithine:

Ornithine (NH₂-CH₂-CH₂-CH(NH₃)-COOH) is an α-amino acid without a carbon atom attached to the amino group, classified as a non-proteinogenic amino acid because it is not encoded by the standard genetic code and not commonly found in proteins. It plays a crucial role in the urea cycle, where it helps convert harmful ammonia into urea, which can then be excreted by the body through urine. Ornithine is produced from the breakdown of arginine, another amino acid, via the enzyme arginase. In some medical and nutritional contexts, ornithine supplementation may be recommended to support liver function, wound healing, or muscle growth, but its effectiveness for these uses remains a subject of ongoing research and debate.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

... that are capable of producing pyridoxal. Pyridoxal is involved in what is believed to be the most ancient reaction of aerobic ... Pyridoxal is one form of vitamin B6. Some medically relevant bacteria, such as those in the genera Granulicatella and ... Pyridoxal phosphate "Protein Domain Structure Uncovers the Origin of Aerobic Metabolism and the Rise of Planetary Oxygen", ... In in vitro culture, these pyridoxal-dependent bacteria may only grow in areas surrounding colonies of bacteria from other ...
... (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic ... Pyridoxal phosphate has numerous roles in human body. A few examples below: Metabolism and biosynthesis of serotonin. Pyridoxal ... Pyridoxal phosphate is a cofactor of ornithine carboxylase. Transamination. Pyridoxal phosphate takes part in decomposition and ... PLP is synthesized from pyridoxal by the enzyme pyridoxal kinase, requiring one ATP molecule. PLP is metabolized in the liver. ...
In enzymology, a pyridoxal oxidase (EC 1.2.3.8) is an enzyme that catalyzes the chemical reaction pyridoxal + H2O + O2 ⇌ {\ ... I. Preliminary studies of pyridoxal oxidase". Mol. Gen. Genet. 180 (2): 449-453. doi:10.1007/BF00425861. Portal: Biology v t e ... The systematic name of this enzyme class is pyridoxal:oxygen 4-oxidoreductase. This enzyme participates in vitamin B6 ... Hanly EW (1980). "Preliminary characterization and physical properties of pyridoxal oxidase activity from Drosophila ...
Other names in common use include pyridoxal kinase (phosphorylating), pyridoxal 5-phosphate-kinase, pyridoxal phosphokinase, ... In enzymology, a pyridoxal kinase (EC 2.7.1.35) is an enzyme that catalyzes the chemical reaction ATP + pyridoxal ⇌ {\ ... displaystyle \rightleftharpoons } ADP + pyridoxal 5'-phosphate Thus, the two substrates of this enzyme are ATP and pyridoxal, ... "Biosynthesis of pyridoxal phosphate by liver sections of rat in vitro". Byull. Eksp. Biol. Med. 22: 40-43. Portal: Biology v t ...
The enzyme pyridoxal phosphatase (EC 3.1.3.74) catalyzes the reaction pyridoxal 5′-phosphate + H2O ⇌ {\displaystyle \ ... Jang, Y.M.; Kim, DW; Kang, TC; Won, MH; Baek, NI; Moon, BJ; Choi, SY; Kwon, OS (2003). "Human pyridoxal phosphatase. Molecular ... The systematic name is pyridoxal-5′-phosphate phosphohydrolase. Other names in common use include vitamine B6 (pyridoxine) ... Fonda ML, Zhang YN (1995). "Kinetic mechanism and divalent metal activation of human erythrocyte pyridoxal phosphatase". Arch. ...
In enzymology, a pyridoxal 4-dehydrogenase (EC 1.1.1.107) is an enzyme that catalyzes the chemical reaction pyridoxal + NAD+ ... The systematic name of this enzyme class is pyridoxal:NAD+ 4-oxidoreductase. This enzyme is also called pyridoxal dehydrogenase ... Pyridoxal dehydrogenase and 4-pyridoxolactonase". J. Biol. Chem. 244 (10): 2585-9. PMID 4306030. Portal: Biology v t e (EC 1.1. ... displaystyle \rightleftharpoons } 4-pyridoxolactone + NADH + H+ Thus, the two substrates of this enzyme are pyridoxal and NAD+ ...
... (trade name Sedalipid) is a hypolipidemic agent. Schuitemaker GE, van der Pol GA, ... Aretz CP, Dinant GJ (2001). "A placebo-controlled, double-blind, randomised trial of magnesium-pyridoxal-5'-phosphate-glutamate ...
Group I pyridoxal-dependent decarboxylases Group II pyridoxal-dependent decarboxylases Group IV pyridoxal-dependent ... Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on amino acid sequence. Group ... The major domain contains a conserved lysine residue, which is the site of attachment of the pyridoxal-phosphate group. ... In molecular biology, group III pyridoxal-dependent decarboxylases are a family of bacterial enzymes comprising ornithine ...
Group I pyridoxal-dependent decarboxylases Group III pyridoxal-dependent decarboxylases Group IV pyridoxal-dependent ... Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on amino acid sequence. Group ... In molecular biology, group II pyridoxal-dependent decarboxylases are family of enzymes including aromatic-L-amino-acid ... Sandmeier E, Hale TI, Christen P (May 1994). "Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid ...
Group I pyridoxal-dependent decarboxylases Group II pyridoxal-dependent decarboxylases Group III pyridoxal-dependent ... Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on amino acid sequence. Group ... The proteins contain a conserved lysine residue which is known, in mouse ODC to be the site of attachment of the pyridoxal- ... In molecular biology, group IV pyridoxal-dependent decarboxylases are a family of enzymes comprising ornithine decarboxylase EC ...
Group II pyridoxal-dependent decarboxylases Group III pyridoxal-dependent decarboxylases Group IV pyridoxal-dependent ... GDC consists of four proteins P, H, L and T. Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into ... The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor, carbon dioxide is released and ... In molecular biology, the group I pyridoxal-dependent decarboxylases, also known as glycine cleavage system P-proteins, are a ...
Pyridoxal 5′-phosphate synthase (glutamine hydrolysing) (EC 4.3.3.6, PdxST) is an enzyme with systematic name D-ribose 5- ... Pyridoxal+5'-phosphate+synthase+(glutamine+hydrolyzing) at the U.S. National Library of Medicine Medical Subject Headings (MeSH ... Hanes JW, Keresztes I, Begley TP (July 2008). "13C NMR snapshots of the complex reaction coordinate of pyridoxal phosphate ... Raschle T, Amrhein N, Fitzpatrick TB (September 2005). "On the two components of pyridoxal 5'-phosphate synthase from Bacillus ...
"Pyridoxal phosphate". Pubchem. Retrieved 2018-03-09. Gillner DM, Becker DP, Holz RC (February 2013). "Lysine biosynthesis in ... It employs the cofactor pyridoxal phosphate, also known as PLP, which participates in numerous enzymatic transamination, ... Portal: Biology (EC 4.1.1, Pyridoxal phosphate enzymes, Enzymes of known structure). ...
Pyridoxal Phosphate Enzymology. 1814 (11): 1405-6. doi:10.1016/j.bbapap.2011.08.007. PMID 21871586. Yennawar NH, Islam MM, ... Like other transaminase enzymes (as well as many enzymes of other classes), BCATs require the cofactor pyridoxal-5'-phosphate ( ... Toney MD (November 2011). "Pyridoxal phosphate enzymology". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. ...
Pyridoxal kinase is an enzyme that in humans is encoded by the PDXK gene. The protein encoded by this gene phosphorylates ... "Entrez Gene: PDXK pyridoxal (pyridoxine, vitamin B6) kinase". Chern CJ, Beutler E (1976). "Biochemical and electrophoretic ... 2004). "Expression of a novel pyridoxal kinase mRNA splice variant, PKH-T, in human testis". Asian J. Androl. 6 (2): 83-91. ... Hanna MC, Turner AJ, Kirkness EF (May 1997). "Human pyridoxal kinase. cDNA cloning, expression, and modulation by ligands of ...
HINA has been used as an analogue of pyridoxal 5′-phosphate, the active form of the coenzyme vitamin B6. It is an especially ... Harris, C.; Johnson, R.; Metzler, D. (1976). "Band-shape analysis and resolution of electronic spectra of pyridoxal phosphate ... doi:10.1016/0304-5102(91)85059-B. Nakamoto, Kazuo; Martell, A. E. (1959). "Pyridoxine and Pyridoxal Analogs. IV. Ultraviolet ... Heinert, Dietrich; Martell, Arthur E. (1958). "Studies on pyridoxine and pyridoxal analogs-I". Tetrahedron. 3: 49-61. doi: ...
"Pyridoxal phosphate-dependent decarboxylase". InterPro. Toney MD (January 2005). "Reaction specificity in pyridoxal phosphate ... HDC contains several regions that are sequentially and structurally similar to those in a number of other pyridoxal-dependent ... The enzyme employs a pyridoxal 5'-phosphate (PLP) cofactor, in similarity to many amino acid decarboxylases. Eukaryotes, as ... Histidine decarboxylase is a group II pyridoxal-dependent decarboxylase, along with aromatic-L-amino-acid decarboxylase, and ...
The enzyme belongs to the γ-family of PLP-dependent enzymes due to its use of a pyridoxal-5'-phosphate (PLP) cofactor to cleave ... Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A (September 1996). "Crystal structure of the pyridoxal-5'-phosphate ... John RA (April 1995). "Pyridoxal phosphate-dependent enzymes". Biochimica et Biophysica Acta (BBA) - Protein Structure and ... Alexander FW, Sandmeier E, Mehta PK, Christen P (February 1994). "Evolutionary relationships among pyridoxal-5'-phosphate- ...
The process consumes a proton in the decarboxylation and employs a pyridoxal-5'-phosphate (PLP) cofactor, similar to other ... John RA (April 1995). "Pyridoxal phosphate-dependent enzymes". Biochimica et Biophysica Acta (BBA) - Protein Structure and ... EC 4.1.1, Pyridoxal phosphate enzymes, Enzymes of known structure). ... Toney MD (January 2005). "Reaction specificity in pyridoxal phosphate enzymes". Archives of Biochemistry and Biophysics. 433 (1 ...
pdxJ plays a role in the DXP-dependent pathway of pyridoxal phosphate. The DXP-dependent pathway is found predominantly in ... Mukherjee T, Hanes J, Tews I, Ealick SE, Begley TP (November 2011). "Pyridoxal phosphate: biosynthesis and catabolism". ... Mittenhuber G (January 2001). "Phylogenetic analyses and comparative genomics of vitamin B6 (pyridoxine) and pyridoxal ... a vitamer of pyridoxal phosphate). In the first step of this condensation reaction, the amine group of HAP forms a Schiff base ...
Pyridoxal dehydrogenase and 4-pyridoxolactonase". J. Biol. Chem. 244 (10): 2585-9. PMID 4306030. Portal: Biology v t e ( ...
It employs one cofactor, pyridoxal phosphate. As of late 2007, 6 structures have been solved for this class of enzymes, with ... Portal: Biology v t e (Articles with short description, Short description matches Wikidata, EC 2.6.1, Pyridoxal phosphate ...
Portal: Biology v t e (Articles with short description, Short description is different from Wikidata, EC 2.6.1, Pyridoxal ... It employs one cofactor, pyridoxal phosphate. HAYAISHI O, NISHIZUKA Y, TATIBANA M, TAKESHITA M, KUNO S (1961). "Enzymatic ...
Portal: Biology v t e (EC 2.6.1, Pyridoxal phosphate enzymes, Enzymes of unknown structure, All stub articles, EC 2.6 stubs). ... It employs one cofactor, pyridoxal phosphate. MEISTER A, FRASER PE (1954). "Enzymatic formation of L-asparagine by ...
Portal: Biology v t e (EC 2.6.1, Pyridoxal phosphate enzymes, Enzymes of known structure, All stub articles, EC 2.6 stubs). ... It employs one cofactor, pyridoxal phosphate. As of late 2007, 11 structures have been solved for this class of enzymes, with ...
Portal: Biology v t e (EC 2.9.1, Pyridoxal phosphate enzymes, Enzymes of unknown structure, All stub articles, Transferase ... It employs one cofactor, pyridoxal phosphate. Forchhammer K, Bock A (1991). "Selenocysteine synthase from Escherichia coli. ...
It employs one cofactor, pyridoxal phosphate. As of late 2007, 5 structures have been solved for this class of enzymes, with ... Portal: Biology v t e (Protein pages needing a picture, Genes on human chromosome 17, EC 4.1.2, Pyridoxal phosphate enzymes, ...
It employs one cofactor, pyridoxal phosphate. Ichihara A, Ichihara EA, Suda M (1960). "Metabolism of L-lysine by bacterial ... Portal: Biology v t e (Articles with short description, Short description matches Wikidata, EC 2.6.1, Pyridoxal phosphate ...
Portal: Biology v t e (EC 2.6.1, Pyridoxal phosphate enzymes, Enzymes of known structure, All stub articles, EC 2.6 stubs). ... It employs one cofactor, pyridoxal phosphate. As of late 2007, 8 structures have been solved for this class of enzymes, with ...
Portal: Biology v t e (EC 4.1.1, Pyridoxal phosphate enzymes, Enzymes of unknown structure, All stub articles, EC 4.1 stubs). ... The systematic name of this enzyme class is aminobenzoate carboxy-lyase (aniline-forming). It employs one cofactor, pyridoxal ...
... that are capable of producing pyridoxal. Pyridoxal is involved in what is believed to be the most ancient reaction of aerobic ... Pyridoxal is one form of vitamin B6. Some medically relevant bacteria, such as those in the genera Granulicatella and ... Pyridoxal phosphate "Protein Domain Structure Uncovers the Origin of Aerobic Metabolism and the Rise of Planetary Oxygen", ... In in vitro culture, these pyridoxal-dependent bacteria may only grow in areas surrounding colonies of bacteria from other ...
Pyridoxal 5-phosphate-dependent epilepsy is a condition that involves seizures beginning soon after birth or, in some cases, ... Pyridoxal 5-phosphate-dependent epilepsy is a condition that involves seizures beginning soon after birth or, in some cases, ... Mutations in the PNPO gene cause pyridoxal 5-phosphate-dependent epilepsy. The PNPO gene provides instructions for producing ... It is not clear how the lack of PLP affects the brain and leads to the seizures that are characteristic of pyridoxal 5- ...
Pyridoxalkinase1,2-ETHANEDIOL2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOLDI(HYDROXYETHYL)ETHERMAGNESIUM IONPHOSPHATE ION
The coenzyme pyridoxal phosphate mediates in the catalysis of metabolic reactions of D- and L- amino acids. Although much work ... The coenzyme pyridoxal phosphate mediates in the catalysis of metabolic reactions of D- and L- amino acids. Although much work ...
E177S MUTANT OF THE PYRIDOXAL-5-PHOSPHATE ENZYME D-AMINO ACID AMINOTRANSFERASE ... PYRIDOXAL-5-PHOSPHATE. C8 H10 N O6 P. NGVDGCNFYWLIFO-UHFFFAOYSA-N. Interactions *Focus chain E [auth A] ... E177S MUTANT OF THE PYRIDOXAL-5-PHOSPHATE ENZYME D-AMINO ACID AMINOTRANSFERASE. *PDB DOI: https://doi.org/10.2210/pdb1G2W/pdb ...
Phosphate And On The Activity Of The Decarboxylase Of Aromatic Amino Acids As Well As Of Other Pyridoxal Phosphate-dependent ... Georgi H Effect Of Neurotropic Agents On Total Pyridoxal, ... The level of pyridoxal phosphate was only partially parallel. ... "Effect Of Neurotropic Agents On Total Pyridoxal, Phosphate And On The Activity Of The Decarboxylase Of Aromatic Amino Acids As ... Thereby, the latter is neither regularly related to corresponding variations of the total cerebral pyridoxal phosphate nor to ...
Improve your day-to-day wellness with Natural Factors BioCoenzymated Pyridoxal 5-phospahte B6 50 mg 30 Veg Caps from Swanson ... BioCoenzymated™ Pyridoxal 5-phosphate from Natural Factors delivers a potent 50 mg of vitamin B6 per serving. Coenzymated ... BioCoenzymated™ Pyridoxal 5-phosphate from Natural Factors delivers a potent 50 mg of vitamin B6 per serving. Coenzymated ...
Protein target information for Pyridoxal 5-phosphate synthase subunit PdxT (Streptococcus pneumoniae 70585). Find diseases ...
L-methylfolate/pyridoxal 5′-phosphate/methylcobalamin), frequency-based adverse effects, comprehensive interactions, ... encoded search term (L-methylfolate/pyridoxal 5-phosphate/methylcobalamin (Metanx)) and L-methylfolate/pyridoxal 5-phosphate/ ...
Protective effect of pyridoxal-5-phosphate (MC-1) on perioperative myocardial infarction is independent of aortic cross clamp ... Protective effect of pyridoxal-5-phosphate (MC-1) on perioperative myocardial infarction is independent of aortic cross clamp ... Pyridoxal-5-phosphate (MC-1), blocking purinergic receptors and intracellular influx of calcium, was shown to decrease the ...
Pyridoxal (vitamin B-6 aldehyde) thiosemicarbazone (B6TSC) is deprotonated to its anion (B6TSC - H+) in basic solution at pH = ... Pyridoxal (vitamin B-6 aldehyde) thiosemicarbazone (B6TSC) is deprotonated to its anion (B6TSC - H+) in basic solution at pH = ... Intraligand fluorescence of Zn(II) and Pt(II) complexes of pyridoxal thiosemicarbazone ... METAL-COMPLEXES; SPECTROSCOPIC PROPERTIES; LUMINESCENCE; Fluorescence; Pyridoxal thiosemicarbazone; Zinc(II); Platinum(II). ...
... is a source of vitamin B6 in the form of pyridoxal-5-phosphate (PLP). As the most biologically active form ... EACH CAPSULE CONTAINS: Vitamin B6 (pyridoxal-5-phosphate).....................50 mg Non-Medicinal Ingredients: Cellulose, ...
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Pyridoxal-5-phosphate Vitamin B6 has to be converted by the body to the active form pyridoxal-5-phosphate for the body to ... Active B6 Pyridoxal (formerly Pyridoxal-5-Phosphate) Metabolically active form of vitamin B6 to assist with the metabolism of ... Genestra Active B6 Pyridoxal (formerly Pyridoxal-5-Phosphate) by Genestra - Co-enzymatic vitamin Bs: The bodys natural active ... Vitamin B6 (pyridoxal-5-phosphate) - 50 mg. Vitamine B6 (5-phosphate de pyridoxal) - 50 mg ...
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Genestra Manufacturers - Energetic B6 Pyridoxal - Pyridoxal-5-Phosphate (P5P) Complement - 60 Capsules. $16.50. Buy Now ... Pyridoxal 5-Phosphate 100 mg - 90 Vegetarian Capsules - P5P Activated Vitamin B6 - Extremely Bioavailable. $13.35. Buy Now ... Life Extension Pyridoxal 5-Phosphate 100 Mg Vegetarian Capsules, 60-Rely, packaging could range. $16.50. Buy Now ... Finest Naturals P5P Vitamin B6 (Pyridoxal 5 Phosphate) 100 mg/Serving - 120 Tablets - an Energetic Type of Vitamin B6.. $8.99. ...
Fluorescent Turn-On Sensing of Zinc(II) and Alkaline Phosphatase Activity Using a Pyridoxal-5-Phosphate Derived Schiff Base. ... Ca2+ functions as a molecular switch that controls the mutually exclusive complex formation of pyridoxal phosphatase with CIB1 ... Maintenance of cellular vitamin B6 levels and mitochondrial oxidative function depend on pyridoxal 5-phosphate homeostasis ... Improved cognition, mild anxiety-like behavior and decreased motor performance in pyridoxal phosphatase-deficient mice. ...
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LBXPLP - Pyridoxal 5-phosphate (nmol/L). Variable Name: LBXPLP. SAS Label: Pyridoxal 5-phosphate (nmol/L). English Text: ... Pyridoxal 5-phosphate (Vitamin B6) for 2005-2006 and 2003-2004:. There was a change in pyridoxal 5-phosphate (Vitamin B6) ... Pyridoxal 5-phosphate (nmol/L). Target: Both males and females 1 YEARS - 150 YEARS. Code or Value. Value Description. Count. ... In 2003-2004, plasma pyridoxal 5-phosphate (PLP) was performed using a homogeneous, enzymatic assay by A/C Diagnostics. In ...
The Life Extension products label says Vitamin B6 (as pyridoxal-5-phosphate) 100 mg. The Source Naturals products label ... says Vitamin B6 60 mg (from 100 mg pyridoxal-5-phosphate). Both products are advertised as 100... ...
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P-5-P by Seeking Health provides 25 mg of pyridoxal 5-phosphate (P-5-P), known as the active or coenzyme form of vitamin ... P-5-P by Seeking Health provides 25 mg of pyridoxal 5-phosphate (P-5-P), known as the "active" or "coenzyme" form of vitamin ... P-5-P by Seeking Health provides 25 mg of pyridoxal 5-phosphate (P-5-P), known as the "active" or "coenzyme" form of vitamin ...
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Toms Pyridoxal 5 Phosphate (P5P). As a dietary supplement, adults take 1 capsule twice daily. This product contains NO yeast, ... Pyridoxal 5 Phosphate (P5P). Adding the right supplements to an individuals diet can greatly increase their overall health. ... Pyridoxal 5-Phosphate has been proven to be up to ten times more effective than its inactive form,Vitamin B6, making it an ... Since Pyridoxal 5-Phosphate is easily absorbed by the body it begins to work almost immediately once ingested. The co-enzyme is ...
10 Foods High in Vitamin B6 , pyridoxal. Are you looking to improve your overall health and wellness? If so, you might want to ... Vitamin B6, also known as pyridoxal, is one of the essential B vitamins that play a crucial role in various bodily functions. ... consider incorporating foods rich in Vitamin B6, also known as pyridoxal, into your diet. Vitamin B6 is a water-soluble vitamin ...
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Pyridoxal-5-Phosphate Home » Archives for Pyridoxal-5-Phosphate Targeted Nutritional Interventions. Posted on January 1, 2012 ...
P-5-P by Seeking Health provides 25 mg of pyridoxal 5-phosphate (P-5-P), known as the active or coenzyme form of vitamin ... P-5-P (Pyridoxal 5-Phosphate) 100 Capsules. $13.95. $11.95. P-5-P by Seeking Health provides 25 mg of pyridoxal 5′-phosphate (P ... Be the first to review "P-5-P (Pyridoxal 5-Phosphate) 100 Capsules" Cancel reply. Your email address will not be published. ... P-5-P by Seeking Health provides 25 mg of pyridoxal 5′-phosphate (P-5-P), known as the "active" or "coenzyme" form of vitamin ...
  • Pyridoxal phosphate "Protein Domain Structure Uncovers the Origin of Aerobic Metabolism and the Rise of Planetary Oxygen", Gustavo Caetano-Anolles et al. (wikipedia.org)
  • Pyridoxal 5'-phosphate-dependent epilepsy is a condition that involves seizures beginning soon after birth or, in some cases, before birth. (medlineplus.gov)
  • Anticonvulsant drugs, which are usually given to control seizures, are ineffective in people with pyridoxal 5'-phosphate-dependent epilepsy. (medlineplus.gov)
  • Instead, individuals with this type of epilepsy are medically treated with large daily doses of pyridoxal 5'-phosphate (a form of vitamin B6). (medlineplus.gov)
  • Even though seizures can be controlled with pyridoxal 5'-phosphate, neurological problems such as developmental delay and learning disorders may still occur. (medlineplus.gov)
  • Mutations in the PNPO gene cause pyridoxal 5'-phosphate-dependent epilepsy. (medlineplus.gov)
  • This enzyme is involved in the conversion (metabolism) of vitamin B6 derived from food (in the form of pyridoxine and pyridoxamine) to the active form of vitamin B6 called pyridoxal 5'-phosphate (PLP). (medlineplus.gov)
  • It is not clear how the lack of PLP affects the brain and leads to the seizures that are characteristic of pyridoxal 5'-phosphate-dependent epilepsy. (medlineplus.gov)
  • Pyridoxal phosphate-dependent neonatal epileptic encephalopathy. (medlineplus.gov)
  • The coenzyme pyridoxal phosphate mediates in the catalysis of metabolic reactions of D- and L- amino acids. (europa.eu)
  • 1) Rats received single intraperitoneal injections of various neuroactive chemicals in order to compare the changes of gross behaviour and the level of pyridoxal phosphate as well as the activity of decarboxylase of aromatic amino acids, of glutamate decarboxylase and of tyrosine transaminase in the brain. (erowid.org)
  • The level of pyridoxal phosphate was only partially parallel. (erowid.org)
  • Pyridoxal phosphate was increased during or after maximal behavioural changes by pentobarbitone and chlorpromazine only. (erowid.org)
  • Thereby, the latter is neither regularly related to corresponding variations of the total cerebral pyridoxal phosphate nor to hitherto described alterations of the monoamine turnover nor to effects on other vitamin B6-dependent enzymes. (erowid.org)
  • BioCoenzymated™ Pyridoxal 5'-phosphate from Natural Factors delivers a potent 50 mg of vitamin B6 per serving. (swansonvitamins.com)
  • Pyridoxal-5-phosphate (MC-1), blocking purinergic receptors and intracellular influx of calcium, was shown to decrease the incidence of perioperative myocardial infarction in the prospective, randomized, double-blinded MC-1 to Eliminate Necrosis and Damage in CABG (MEND-CABG) clinical trial. (minervamedica.it)
  • Active B 6 Pyridoxal is a source of vitamin B 6 in the form of pyridoxal-5-phosphate (PLP). (atriumpro.ca)
  • Genestra Active B6 Pyridoxal (formerly Pyridoxal-5-Phosphate) by Genestra - Co-enzymatic vitamin B's: The body's natural active form for energy production and metabolism. (vitaminon.com)
  • The ACTIVE vitamin B's utilize premium source ingredients such as methylcobalamin, Metafolin, riboflavin-5-phosphate and pyridoxal-5-phosphate. (vitaminon.com)
  • Active B6 Pyridoxal (formerly Pyridoxal-5-Phosphate) Metabolically active form of vitamin B6 to assist with the metabolism of proteins, fats and carbohydrates. (vitaminon.com)
  • Pyridoxal-5-phosphate Vitamin B6 has to be converted by the body to the active form pyridoxal-5-phosphate for the body to utilize it. (vitaminon.com)
  • Pyridoxal-5-Phosphate, a biologically active form of vitamin B6, provides 50 mg of Pyridoxal-5-Phosphate per each capsule. (expertnutrition.com)
  • Finest Naturals P5P Vitamin B6 (Pyridoxal 5 Phosphate) 100 mg/Serving - 120 Tablets - an Energetic Type of Vitamin B6. (healthigg.com)
  • There was a change in pyridoxal 5'-phosphate (Vitamin B6) methods from 2003-2004 to 2005-2006. (cdc.gov)
  • In 2003-2004, plasma pyridoxal 5'-phosphate (PLP) was performed using a homogeneous, enzymatic assay by A/C Diagnostics. (cdc.gov)
  • The Source Naturals product's label says 'Vitamin B6 60 mg (from 100 mg pyridoxal-5'-phosphate). (phoenixrising.me)
  • P-5-P by Seeking Health provides 25 mg of pyridoxal 5'-phosphate (P-5-P), known as the "active" or "coenzyme" form of vitamin B6, in an easy-to-swallow vegetarian capsule. (proactivehealthcare.co.uk)
  • Although the vitamin is often sold in its inactive form it can also be purchased as an active co-enzyme that's known as Pyridoxal 5-Phosphate. (martinavenue.com)
  • Vitamin B6 is an essential vitamin that's converted into it's active form, known as Pyridoxal 5-Phosphate or P5P in short, by the liver. (martinavenue.com)
  • Pyridoxal 5-Phosphate has been proven to be up to ten times more effective than it's inactive form,Vitamin B6, making it an overall superior supplement. (martinavenue.com)
  • Since Pyridoxal 5-Phosphate is easily absorbed by the body it begins to work almost immediately once ingested. (martinavenue.com)
  • By taking a daily Pyridoxal 5-Phosphate supplement individuals can enhance their overall health and improve their body's natural functioning. (martinavenue.com)
  • Genestra - Active B6 Pyridoxal - 60 vegetarian Capsule(s) - NPN: 80001110 -- Active B6 Pyridoxal is a source of vitamin B6 in the form of pyridoxal-5-phosphate (PLP). (ahealthyyou.ca)
  • Pyridoxal 5′-phosphate (PLP), an active form of vitamin B6/ pyridoxine is the coenzyme of amino acid metabolism. (fmect.com)
  • as a component in the reaction mixture for ornithine decarboxylase (ODC) activity assay as a standard to quantify the concentration of pyridoxal 5′-phosphate (PLP) in cerebrospinal fluid (CSF) of children as a dietary supplement to study its effects on the lethal phenotype of mutant flies. (fmect.com)
  • Pyridoxal-5-Phosphate, which is the converted and easy-to-assimilate form of vitamin B6 , is supplied along with magnesium, an essential nutrient that assists B6 in its metabolic activity. (autismsupplementscenter.com)
  • Our project has been centered on discovering a specific inhibitor for LMW-PTP using analogs of Pyridoxal 5' Phosphate (PLP), a known inhibitor. (csbsju.edu)
  • For example, pyridoxal phosphate, a form of vitamin B 6 , in aqueous solution is predicted to have an equilibrium favoring a tautomeric form in which a proton is transferred from the phenolic -OH group to the nitrogen atom. (wikipedia.org)
  • Natural Factors B6 Biocoenzymide Pyridoxal 5-Phosphate 50 is a unique blend of high-tech, biocompatible synergistic vitamin B6 and phytonutrients for active support of the nervous system, energy metabolism, the conversion of carbohydrates, fats and proteins into energy and the production of neurotransmitters that influence cognition and emotional well-being. (drnutrition.com)
  • Histidine decarboxylase is a pyridoxal 5'-phosphate enzyme catalyzing the conversion of histidine to histamine, a bioactive molecule exerting its role in many modulatory processes. (unipd.it)
  • Direct biomarkers measure B6 vitamers in plasma/serum, urine and erythrocytes, and among these plasma pyridoxal 5'-phosphate (PLP) is most commonly used. (nih.gov)
  • 100 mg of pyridoxal 5′-phosphate, a metabolically active B6 is included in Life Extension Mix. (consumerhealthdigest.com)
  • Vitamin-B6 status was evaluated using the erythrocyte glutamic-pyruvic-transaminase (EGPT) assay and quantification of plasma pyridoxal-5'-phosphate. (cdc.gov)
  • They are metabolized in the body to pyridoxal phosphate, which acts as a coenzyme in many important reactions in blood, central nervous system, and skin metabolism. (msdmanuals.com)
  • During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE). (bvsalud.org)
  • Of note, synthesis of ALT is dependent on vitamin B6 (pyridoxal phosphate) and will be decreased in the setting of low vitamin B6 and cirrhosis. (medscape.com)
  • Both AST and ALT are dependent on vitamin B6 (pyridoxal phosphate). (medscape.com)
  • Pyridoxal is one form of vitamin B6. (wikipedia.org)
  • Pyridoxal (vitamin B-6 aldehyde) thiosemicarbazone (B6TSC) is deprotonated to its anion (B6TSC - H+) in basic solution at pH = 9. (uni-regensburg.de)
  • Pyridoxal-5-phosophate is the active co-enzyme form of vitamin B6 and thus more readily used by the body. (vitaminon.com)
  • If so, you might want to consider incorporating foods rich in Vitamin B6, also known as pyridoxal, into your diet. (ferraramarket.com)
  • P-5-P (Pyridoxal 5 Phos) 50mg - 5-fosfat-piridoxal reprezintă forma de coenzimă a vitaminei B6. (suplimenteoriginale.ro)
  • Some medically relevant bacteria, such as those in the genera Granulicatella and Abiotrophia, require pyridoxal for growth. (wikipedia.org)
  • Pyridoxal is involved in what is believed to be the most ancient reaction of aerobic metabolism on Earth, about 2.9 billion years ago, a forerunner of the Great Oxidation Event. (wikipedia.org)
  • Pyridoxal phosphate-dependent neonatal epileptic encephalopathy. (medlineplus.gov)
  • which is catalyzed by the enzyme pyridoxal kinase. (hmdb.ca)
  • Pyridox(am)ine-5'-phosphate oxidase converts pyridoxine phosphate and pyridoxamine phosphate to pyridoxal phosphate, a cofactor in many metabolic reactions, including neurotransmitter synthesis. (nih.gov)
  • 25. Pyridoxal phosphate inhibits pituitary cell proliferation and hormone secretion. (nih.gov)
  • They are metabolized in the body to pyridoxal phosphate, which acts as a coenzyme in many important reactions in blood, central nervous system, and skin metabolism. (msdmanuals.com)
  • Mutations in the PNPO gene cause pyridoxal 5'-phosphate-dependent epilepsy. (medlineplus.gov)
  • Pyridoxal 5'-phosphate-dependent epilepsy is a condition that involves seizures beginning soon after birth or, in some cases, before birth. (medlineplus.gov)
  • Anticonvulsant drugs, which are usually given to control seizures, are ineffective in people with pyridoxal 5'-phosphate-dependent epilepsy. (medlineplus.gov)
  • It is not clear how the lack of PLP affects the brain and leads to the seizures that are characteristic of pyridoxal 5'-phosphate-dependent epilepsy. (medlineplus.gov)
  • In 2003-2004, plasma pyridoxal 5'-phosphate (PLP) was performed using a homogeneous, enzymatic assay by A/C Diagnostics. (cdc.gov)
  • 2021. https://www.tabers.com/tabersonline/view/Tabers-Dictionary/763366/all/pyridoxal_5_phosphate__pyridoxal_phosphate. (tabers.com)
  • Pyridoxal is involved in what is believed to be the most ancient reaction of aerobic metabolism on Earth, about 2.9 billion years ago, a forerunner of the Great Oxidation Event. (wikipedia.org)
  • Pyridoxal phosphate "Protein Domain Structure Uncovers the Origin of Aerobic Metabolism and the Rise of Planetary Oxygen", Gustavo Caetano-Anolles et al. (wikipedia.org)
  • Pyridoxamine and pyridoxal are more effective than pyridoxine in rescuing folding-defective variants of human alanine:glyoxylate aminotransferase causing primary hyperoxaluria type I. (univr.it)
  • A family with a mutation in the pyridox(am)ine-5'-phosphate oxidase gene presenting with neonatal seizures unresponsive to pyridoxine and anticonvulsant treatment but responsive to pyridoxal phosphate is described. (nih.gov)
  • The B6 -vitamer Pyridoxal is a Sensitizer of UVA-induced Genotoxic Stress in Human Primary Keratinocytes and Reconstructed Epidermis. (nih.gov)
  • Here, we report that the B6 -vitamer pyridoxal is a sensitizer of genotoxic stress in human adult primary keratinocytes (HEKa) and reconstructed epidermis. (nih.gov)
  • In addition to activational phosphorylation indicative of genotoxic stress [p53 (Ser15) and γ-H2AX (Ser139)], comet analysis indicated the formation of Fpg-sensitive oxidative DNA lesions, observable only after combined exposure to pyridoxal and UVA. (nih.gov)
  • In in vitro culture, these pyridoxal-dependent bacteria may only grow in areas surrounding colonies of bacteria from other genera ("satellitism") that are capable of producing pyridoxal. (wikipedia.org)