The removal of a carboxyl group, usually in the form of carbon dioxide, from a chemical compound.
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.
Catalyzes the decarboxylation of an alpha keto acid to an aldehyde and carbon dioxide. Thiamine pyrophosphate is an essential cofactor. In lower organisms, which ferment glucose to ethanol and carbon dioxide, the enzyme irreversibly decarboxylates pyruvate to acetaldehyde. EC 4.1.1.1.
Orotidine-5'-phosphate carboxy-lyase. Catalyzes the decarboxylation of orotidylic acid to yield uridylic acid in the final step of the pyrimidine nucleotide biosynthesis pathway. EC 4.1.1.23.
The coenzyme form of Vitamin B1 present in many animal tissues. It is a required intermediate in the PYRUVATE DEHYDROGENASE COMPLEX and the KETOGLUTARATE DEHYDROGENASE COMPLEX.
Colorless reduced precursors of porphyrins in which the pyrrole rings are linked by methylene (-CH2-) bridges.
Derivatives of OXALOACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that include a 2-keto-1,4-carboxy aliphatic structure.
Decarboxylated arginine, isolated from several plant and animal sources, e.g., pollen, ergot, herring sperm, octopus muscle.
Porphyrinogens which are intermediates in the heme biosynthesis. They have four methyl and four propionic acid side chains attached to the pyrrole rings. Coproporphyrinogens I and III are formed in the presence of uroporphyrinogen decarboxylase from the corresponding uroporphyrinogen. They can yield coproporphyrins by autooxidation or protoporphyrin by oxidative decarboxylation.
'Keto acids', also known as ketone bodies, are water-soluble compounds - acetoacetic acid, beta-hydroxybutyric acid, and acetone - that are produced during fat metabolism when liver glycogen stores are depleted, providing an alternative energy source for the brain and other organs in states of carbohydrate restriction or intense physical exertion.
Pyruvates, in the context of medical and biochemistry definitions, are molecules that result from the final step of glycolysis, containing a carboxylic acid group and an aldehyde group, playing a crucial role in cellular metabolism, including being converted into Acetyl-CoA to enter the Krebs cycle or lactate under anaerobic conditions.
An enzyme group with broad specificity. The enzymes decarboxylate a range of aromatic amino acids including dihydroxyphenylalanine (DOPA DECARBOXYLASE); TRYPTOPHAN; and HYDROXYTRYPTOPHAN.
An enzyme that catalyzes the decarboxylation of UROPORPHYRINOGEN III to coproporphyrinogen III by the conversion of four acetate groups to four methyl groups. It is the fifth enzyme in the 8-enzyme biosynthetic pathway of HEME. Several forms of cutaneous PORPHYRIAS are results of this enzyme deficiency as in PORPHYRIA CUTANEA TARDA; and HEPATOERYTHROPOIETIC PORPHYRIA.
Organic compounds containing the carboxy group (-COOH). This group of compounds includes amino acids and fatty acids. Carboxylic acids can be saturated, unsaturated, or aromatic.
A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)
An intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed)
5'-Uridylic acid. A uracil nucleotide containing one phosphate group esterified to the sugar moiety in the 2', 3' or 5' position.
An enzyme that catalyzes the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX by the conversion of two propionate groups to two vinyl groups. It is the sixth enzyme in the 8-enzyme biosynthetic pathway of HEME, and is encoded by CPO gene. Mutations of CPO gene result in HEREDITARY COPROPORPHYRIA.
A flavoring agent. It is the intermediate product in the two-step bioconversion of ferulic acid to vanillin. (J Biotechnol 1996;50(2-3):107-13).
Oxidoreductases that are specific for KETONES.
The rate dynamics in chemical or physical systems.
Inorganic salts or organic esters of phosphorous acid that contain the (3-)PO3 radical. (From Grant & Hackh's Chemical Dictionary, 5th ed)
Cells with the capacity to take up and decarboxylate the amine precursors DIHYDROXYPHENYLALANINE or 5-HYDROXYTRYPTOPHAN. This is a property of endocrine cells of neural and non-neural origin. APUDOMA is a general term collectively applied to tumors associated with APUD cells.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Derivatives of caproic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a carboxy terminated six carbon aliphatic structure.
Porphyrinogens which are intermediates in heme biosynthesis. They have four acetic acid and four propionic acid side chains attached to the pyrrole rings. Uroporphyrinogen I and III are formed from polypyrryl methane in the presence of uroporphyrinogen III cosynthetase and uroporphyrin I synthetase, respectively. They can yield uroporphyrins by autooxidation or coproporphyrinogens by decarboxylation.
An agent thought to have disinfectant properties and used as an expectorant. (From Martindale, The Extra Pharmacopoeia, 30th ed, p747)
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.
Analogs or derivatives of mandelic acid (alpha-hydroxybenzeneacetic acid).
A viscous, hygroscopic amino alcohol with an ammoniacal odor. It is widely distributed in biological tissue and is a component of lecithin. It is used as a surfactant, fluorimetric reagent, and to remove CO2 and H2S from natural gas and other gases.
A ferredoxin-containing enzyme that catalyzes the COENZYME A-dependent oxidative decarboxylation of PYRUVATE to acetyl-COENZYME A and CARBON DIOXIDE.
A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)
A genus of gram-negative, anaerobic cocci parasitic in the mouth and in the intestinal and respiratory tracts of man and other animals.
A beta-hydroxylated derivative of phenylalanine. The D-form of dihydroxyphenylalanine has less physiologic activity than the L-form and is commonly used experimentally to determine whether the pharmacological effects of LEVODOPA are stereospecific.
A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.
A general term collectively applied to tumors associated with the APUD CELLS series, irrespective of their specific identification.
Cytidine 5'-(trihydrogen diphosphate). A cytosine nucleotide containing two phosphate groups esterified to the sugar moiety. Synonyms: CRPP; cytidine pyrophosphate.
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to a serine moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and serine and 2 moles of fatty acids.
Substances capable of inhibiting, retarding or arresting the process of fermentation, acidification or other deterioration of foods.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
Pyruvate oxidase is an enzyme complex located within the mitochondrial matrix that catalyzes the oxidative decarboxylation of pyruvate into acetyl-CoA, thereby linking glycolysis to the citric acid cycle and playing a crucial role in cellular energy production.
A foul-smelling diamine formed by bacterial decarboxylation of lysine.
An order of gram-positive bacteria in the class Bacilli, that have the ability to ferment sugars to lactic acid. They are widespread in nature and commonly used to produce fermented foods.
A carboxy-lyase that catalyzes the decarboxylation of (S)-2-Methyl-3-oxopropanoyl-CoA to propanoyl-CoA. In microorganisms the reaction can be coupled to the vectorial transport of SODIUM ions across the cytoplasmic membrane.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A species of gram-positive, rod-shaped LACTIC ACID bacteria that is frequently used as starter culture in SILAGE fermentation, sourdough, and lactic-acid-fermented types of beer and wine.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.
Coenzyme A is an essential coenzyme that plays a crucial role in various metabolic processes, particularly in the transfer and activation of acetyl groups in important biochemical reactions such as fatty acid synthesis and oxidation, and the citric acid cycle.
Thiamine antagonist, antimetabolite.
A PYRIDOXAL PHOSPHATE dependent enzyme that catalyzes the decarboxylation of GLYCINE with the transfer of an aminomethyl group to the LIPOIC ACID moiety of the GLYCINE DECARBOXYLASE COMPLEX H-PROTEIN. Defects in P-protein are the cause of non-ketotic hyperglycinemia. It is one of four subunits of the glycine decarboxylase complex.
Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.
Mold and yeast inhibitor. Used as a fungistatic agent for foods, especially cheeses.
Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent.
Benzoate derivatives substituted by one or more hydroxy groups in any position on the benzene ring.
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 biotin-dependent enzyme belonging to the ligase family that catalyzes the addition of CARBON DIOXIDE to pyruvate. It is occurs in both plants and animals. Deficiency of this enzyme causes severe psychomotor retardation and ACIDOSIS, LACTIC in infants. EC 6.4.1.1.
Chemical compounds which yield hydrogen ions or protons when dissolved in water, whose hydrogen can be replaced by metals or basic radicals, or which react with bases to form salts and water (neutralization). An extension of the term includes substances dissolved in media other than water. (Grant & Hackh's Chemical Dictionary, 5th ed)
Cinnamates are organic compounds that contain a cinnamic acid moiety, widely used in pharmaceutical and cosmetic industries as esters, with various applications ranging from UV absorbers to local anesthetics and antimicrobial agents.
Malonates are organic compounds containing a malonate group, which is a dicarboxylic acid functional group with the structure -OC(CH2COOH)2, and can form salts or esters known as malonates.
Derivatives of adipic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,6-carboxy terminated aliphatic structure.
Valerates are salts or esters formed from the reaction between valerianic acid and a base, characterized by their tranquilizing and sedative properties, often used in pharmaceuticals and dietary supplements for promoting sleep and reducing anxiety.
An inhibitor of DOPA DECARBOXYLASE, preventing conversion of LEVODOPA to dopamine. It is used in PARKINSON DISEASE to reduce peripheral adverse effects of LEVODOPA. It has no antiparkinson actions by itself.
The removal of an amino group (NH2) from a chemical compound.
"Malate" is a term used in biochemistry to refer to a salt or ester of malic acid, a dicarboxylic acid found in many fruits and involved in the citric acid cycle, but it does not have a specific medical definition as such.
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.
Orotic acid, also known as pyrophosphoric acid dihydrate, is a organic compound that plays a role in the biosynthesis of pyrimidines, and elevated levels of orotic acid in urine can indicate certain genetic disorders or liver dysfunction.
Energy that is generated by the transfer of protons or electrons across an energy-transducing membrane and that can be used for chemical, osmotic, or mechanical work. Proton-motive force can be generated by a variety of phenomena including the operation of an electron transport chain, illumination of a PURPLE MEMBRANE, and the hydrolysis of ATP by a proton ATPase. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed, p171)
A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.
A water-soluble, enzyme co-factor present in minute amounts in every living cell. It occurs mainly bound to proteins or polypeptides and is abundant in liver, kidney, pancreas, yeast, and milk.
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to an ethanolamine moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and ethanolamine and 2 moles of fatty acids.
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)
A strong dicarboxylic acid occurring in many plants and vegetables. It is produced in the body by metabolism of glyoxylic acid or ascorbic acid. It is not metabolized but excreted in the urine. It is used as an analytical reagent and general reducing agent.
Derivatives of OXALIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that are derived from the ethanedioic acid structure.
Unstable isotopes of carbon that decay or disintegrate emitting radiation. C atoms with atomic weights 10, 11, and 14-16 are radioactive carbon isotopes.
A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that is not known to be pathogenic for man, animals, or plants. Its organisms are spoilers for beers and ciders and in sweet English ciders they are the causative agents of a secondary fermentation known as "cider sickness." The species Z. mobilis is used for experiments in molecular genetic studies.
An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.
The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.
A trihydroxybenzene or dihydroxy phenol that can be prepared by heating GALLIC ACID.
3-((4-Amino-2-methyl-5-pyrimidinyl)methyl)-5-(2- hydroxyethyl)-4-methylthiazolium chloride.
Porphyrins with four acetic acid and four propionic acid side chains attached to the pyrrole rings.
An autosomal dominant porphyria that is due to a deficiency of COPROPORPHYRINOGEN OXIDASE in the LIVER, the sixth enzyme in the 8-enzyme biosynthetic pathway of HEME. Clinical features include both neurological symptoms and cutaneous lesions. Patients excrete increased levels of porphyrin precursors, 5-AMINOLEVULINATE and COPROPORPHYRINS.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A flavoprotein enzyme that is responsible for the catabolism of LYSINE; HYDROXYLYSINE; and TRYPTOPHAN. It catalyzes the oxidation of GLUTARYL-CoA to crotonoyl-CoA using FAD as a cofactor. Glutaric aciduria type I is an inborn error of metabolism due to the deficiency of glutaryl-CoA dehydrogenase.
An amino acid produced in the urea cycle by the splitting off of urea from arginine.
An indirect sympathomimetic. Tyramine does not directly activate adrenergic receptors, but it can serve as a substrate for adrenergic uptake systems and monoamine oxidase so it prolongs the actions of adrenergic transmitters. It also provokes transmitter release from adrenergic terminals. Tyramine may be a neurotransmitter in some invertebrate nervous systems.
A LIPOIC ACID-containing protein that plays the pivotal role in the transfer of methylamine groups and reducing equivalents between the three enzymatic components of the glycine decarboxylase complex.
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.
A precursor of noradrenaline that is used in the treatment of parkinsonism. The racemic form (DL-threo-3,4-dihydroxyphenylserine) has also been used, and has been investigated in the treatment of orthostatic hypotension. There is a deficit of noradrenaline as well as of dopamine in Parkinson's disease and it has been proposed that this underlies the sudden transient freezing seen usually in advanced disease. Administration of DL-threo-3,4-dihydroxyphenylserine has been claimed to result in an improvement in this phenomenon but controlled studies have failed to demonstrate improvement. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995)
Glyoxylates are organic compounds that are intermediate products in the metabolic pathways responsible for the breakdown and synthesis of various molecules, including amino acids and carbohydrates, and are involved in several biochemical processes such as the glyoxylate cycle.
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.
A pyridoxal-phosphate protein, believed to be the rate-limiting compound in the biosynthesis of polyamines. It catalyzes the decarboxylation of ornithine to form putrescine, which is then linked to a propylamine moiety of decarboxylated S-adenosylmethionine to form spermidine.
Isocitrate is a chemical compound, an isomer of citric acid, which is a key intermediate in the tricarboxylic acid cycle (Krebs cycle) and is involved in energy production through cellular respiration in living organisms.

Microbial catabolism of vanillate: decarboxylation to guaiacol. (1/263)

A novel catabolic transformation of vanillic acid (4-hydroxy-3-methoxybenzoic acid) by microorganisms is reported. Several strains of Bacillus megaterium and a strain of Streptomyces are shown to convert vanillate to guaiacol (o-methoxyphenol) and CO2 by nonoxidative decarboxylation. Use of a modified most-probable-number procedure shows that numerous soils contain countable numbers (10(1) to 10(2) organisms per g of dry soil) of aerobic sporeformers able to convert vanillate to guaiacol. Conversion of vanillate to guaiacol by the microfloras of most-probable-number replicates was used as the criterion for scoring replicates positive or negative. Guaiacol was detected by thin-layer chromatography. These results indicate that the classic separations of catabolic pathways leading to specific ring-fashion substrates such as protocatechuate and catechol are often interconnectable by single enzymatic transformations, usually a decarboxylation.  (+info)

Characterization of two members of a novel malic enzyme class. (2/263)

The Gram-negative bacterium Rhizobium meliloti contains two distinct malic enzymes. We report the purification of the two isozymes to homogeneity, and their in vitro characterization. Both enzymes exhibit unusually high subunit molecular weights of about 82 kDa. The NAD(P)(+) specific malic enzyme [EC 1.1.1.39] exhibits positive co-operativity with respect to malate, but Michaelis-Menten type behavior with respect to the co-factors NAD(+) or NADP(+). The enzyme is subject to substrate inhibition, and shows allosteric regulation by acetyl-CoA, an effect that has so far only been described for some NADP(+) dependent malic enzymes. Its activity is positively regulated by succinate and fumarate. In contrast to the NAD(P)(+) specific malic enzyme, the NADP(+) dependent malic enzyme [EC 1.1.1.40] shows Michaelis-Menten type behavior with respect to malate and NADP(+). Apart from product inhibition, the enzyme is not subjected to any regulatory mechanism. Neither reductive carboxylation of pyruvate, nor decarboxylation of oxaloacetate, could be detected for either malic enzyme. Our characterization of the two R. meliloti malic enzymes therefore suggests a number of features uncharacteristic for malic enzymes described so far.  (+info)

Succinispira mobilis gen. nov., sp. nov., a succinate-decarboxylating anaerobic bacterium. (3/263)

A succinate-decarboxylating anaerobic bacterium, designated strain 19gly1T, was previously isolated from a mixed culture growing with glycolate. The almost complete sequence of the 16S rRNA gene (1495 nt) was determined for this strain. On the basis of 16S rRNA gene sequence homology, strain 19gly1T was identified as a member of the Sporomusa sub-branch of the 'low G+C' Gram-positive bacteria. Phylogenetic analysis showed that strain 19gly1T was most closely related to Succiniclasticum ruminis, Phascolarctobacterium faecium and Acidaminococcus fermentans. The use of different algorithms, such as least-squares or neighbour-joining analyses of Jukes-Cantor pairwise distances, or maximum-parsimony or maximum-likelihood analyses of the aligned sequence data, revealed that strain 19gly1T grouped as the most deeply branching lineage of the strain 19gly1T-Succiniclasticum- Acidaminococcus-Phascolarctobacterium cluster. The phenotypic characteristics of strain 19gly1T distinguish it from members of the genera Succiniclasticum, Phascolarctobacterium and Acidaminococcus, and the phylogenetic distances inferred from comparative analysis of the 16S rDNA sequences suggest that strain 19gly1T is a representative of a new genus. Accordingly, strain 19gly1T (= DSM 6222T) is proposed as the type strain of a new species within a new genus, Succinispira mobilis gen. nov., sp. nov.  (+info)

Interplay of organic and biological chemistry in understanding coenzyme mechanisms: example of thiamin diphosphate-dependent decarboxylations of 2-oxo acids. (4/263)

With the publication of the three-dimensional structures of several thiamin diphosphate-dependent enzymes, the chemical mechanism of their non-oxidative and oxidative decarboxylation reactions is better understood. Chemical models for these reactions serve a useful purpose to help evaluate the additional catalytic rate acceleration provided by the protein component. The ability to generate, and spectroscopically observe, the two key zwitterionic intermediates invoked in such reactions allowed progress to be made in elucidating the rates and mechanisms of the elementary steps leading to and from these intermediates. The need remains to develop chemical models, which accurately reflect the enzyme-bound conformation of this coenzyme.  (+info)

Characterization of a vanillic acid non-oxidative decarboxylation gene cluster from Streptomyces sp. D7. (5/263)

The genetics of non-oxidative decarboxylation of aromatic acids are poorly understood in both prokaryotes and eukaryotes. Although such reactions have been observed in numerous micro-organisms acting on a variety of substrates, the genes encoding enzymes responsible for these processes have not, to our knowledge, been reported in the literature. Here, the isolation of a streptomycete from soil (Streptomyces sp. D7) which efficiently converts 4-hydroxy-3-methoxybenzoic acid (vanillic acid) to 2-methoxyphenol (guaiacol) is described. Protein two-dimensional gel analysis revealed that several proteins were synthesized in response to vanillic acid. One of these was characterized by partial amino-terminal sequencing, leading to the cloning of a gene cluster from a genomic DNA lambda phage library, consisting of three ORFs, vdcB (602 bp), vdcC (1424 bp) and vdcD (239 bp). Protein sequence comparisons suggest that the product of vdcB (201 aa) is similar to phenylacrylate decarboxylase of yeast; the putative products of vdcC (475 aa) and vdcD (80 aa) are similar to hypothetical proteins of unknown function from various micro-organisms, and are found in a similar cluster in Bacillus subtilis. Northern blot analysis revealed the synthesis of a 2.5 kb mRNA transcript in vanillic-acid-induced cells, suggesting that the cluster is under the control of a single inducible promoter. Expression of the entire vdc gene cluster in Streptomyces lividans 1326 as a heterologous host resulted in that strain acquiring the ability to decarboxylate vanillic acid to guaiacol non-oxidatively. Both Streptomyces sp. strain D7 and recombinant S. lividans 1326 expressing the vdc gene cluster do not, however, decarboxylate structurally similar aromatic acids, suggesting that the system is specific for vanillic acid. This catabolic system may be useful as a component for pathway engineering research focused towards the production of valuable chemicals from forestry and agricultural by-products.  (+info)

Catabolism of alpha-ketoglutarate by a sucA mutant of Bradyrhizobium japonicum: evidence for an alternative tricarboxylic acid cycle. (6/263)

A complete tricarboxylic acid (TCA) cycle is generally considered necessary for energy production from the dicarboxylic acid substrates malate, succinate, and fumarate. However, a Bradyrhizobium japonicum sucA mutant that is missing alpha-ketoglutarate dehydrogenase is able to grow on malate as its sole source of carbon. This mutant also fixes nitrogen in symbiosis with soybean, where dicarboxylic acids are its principal carbon substrate. Using a flow chamber system to make direct measurements of oxygen consumption and ammonium excretion, we confirmed that bacteroids formed by the sucA mutant displayed wild-type rates of respiration and nitrogen fixation. Despite the absence of alpha-ketoglutarate dehydrogenase activity, whole cells of the mutant were able to decarboxylate alpha-[U-(14)C]ketoglutarate and [U-(14)C]glutamate at rates similar to those of wild-type B. japonicum, indicating that there was an alternative route for alpha-ketoglutarate catabolism. Because cell extracts from B. japonicum decarboxylated [U-(14)C]glutamate very slowly, the gamma-aminobutyrate shunt is unlikely to be the pathway responsible for alpha-ketoglutarate catabolism in the mutant. In contrast, cell extracts from both the wild type and mutant showed a coenzyme A (CoA)-independent alpha-ketoglutarate decarboxylation activity. This activity was independent of pyridine nucleotides and was stimulated by thiamine PP(i). Thin-layer chromatography showed that the product of alpha-ketoglutarate decarboxylation was succinic semialdehyde. The CoA-independent alpha-ketoglutarate decarboxylase, along with succinate semialdehyde dehydrogenase, may form an alternative pathway for alpha-ketoglutarate catabolism, and this pathway may enhance TCA cycle function during symbiotic nitrogen fixation.  (+info)

Decarboxylation of substituted cinnamic acids by lactic acid bacteria isolated during malt whisky fermentation. (7/263)

Seven strains of Lactobacillus isolated from malt whisky fermentations and representing Lactobacillus brevis, L. crispatus, L. fermentum, L. hilgardii, L. paracasei, L. pentosus, and L. plantarum contained genes for hydroxycinnamic acid (p-coumaric acid) decarboxylase. With the exception of L. hilgardii, these bacteria decarboxylated p-coumaric acid and/or ferulic acid, with the production of 4-vinylphenol and/or 4-vinylguaiacol, respectively, although the relative activities on the two substrates varied between strains. The addition of p-coumaric acid or ferulic acid to cultures of L. pentosus in MRS broth induced hydroxycinnamic acid decarboxylase mRNA within 5 min, and the gene was also induced by the indigenous components of malt wort. In a simulated distillery fermentation, a mixed culture of L. crispatus and L. pentosus in the presence of Saccharomyces cerevisiae decarboxylated added p-coumaric acid more rapidly than the yeast alone but had little activity on added ferulic acid. Moreover, we were able to demonstrate the induction of hydroxycinnamic acid decarboxylase mRNA under these conditions. However, in fermentations with no additional hydroxycinnamic acid, the bacteria lowered the final concentration of 4-vinylphenol in the fermented wort compared to the level seen in a pure-yeast fermentation. It seems likely that the combined activities of bacteria and yeast decarboxylate p-coumaric acid and then reduce 4-vinylphenol to 4-ethylphenol more effectively than either microorganism alone in pure cultures. Although we have shown that lactobacilli participate in the metabolism of phenolic compounds during malt whisky fermentations, the net result is a reduction in the concentrations of 4-vinylphenol and 4-vinylguaiacol prior to distillation.  (+info)

Induction of epithelial differentiation and DNA demethylation in hamster malignant oral keratinocyte by ornithine decarboxylase antizyme. (8/263)

The hamster ornithine decarboxylase antizyme (ODC-Az) cDNA was transfected into the hamster malignant oral keratinocyte cell line, HCPC-1. Ectopic expression of ODC-Az resulted in the reversion of malignant phenotypes and alteration of DNA methylation status of CCGG sites. The phenotypes examined include ODC enzymatic activity, doubling time, morphological change, anchorage dependent growth, tumorigenicity in nude mice, induction of epithelial differentiation marker protein (involucrin), and change of cell cycle position. Comparison of CCGG DNA methylation status of the ODC-Az and control vector transfectants revealed a significant increase in demethylation of 5-methyl cytosines (m5C) of CCGG sites in the ODC-Az transfectants. Ectopic expression of ODC-Az gene in hamster malignant oral keratinocytes led to reduce ODC activity and the subsequent demethylation of 5-methyl cytosines, presumably via the ODC/ polyamines/ decarboxylated S-adenosylmethionine (dc-AdoMet) pathways. Our data suggest that ODC-Az shared the same pathway of polyamines/ dc-AdoMet/DNA methyltransferase (DNA MTase). We propose that ODC-Az mediates a novel mechanism in tumor suppression by DNA demethylation and presumably re-activation of key cellular genes silenced by DNA hypermethylation during cancer development. Oncogene (2001) 20, 24 - 33.  (+info)

Decarboxylation is a chemical reaction that removes a carboxyl group from a molecule and releases carbon dioxide (CO2) as a result. In the context of medical chemistry, decarboxylation is a crucial process in the activation of certain acidic precursor compounds into their biologically active forms.

For instance, when discussing phytocannabinoids found in cannabis plants, decarboxylation converts non-psychoactive tetrahydrocannabinolic acid (THCA) into psychoactive delta-9-tetrahydrocannabinol (Δ9-THC) through the removal of a carboxyl group. This reaction typically occurs when the plant material is exposed to heat, such as during smoking or vaporization, or when it undergoes aging.

In summary, decarboxylation refers to the chemical process that removes a carboxyl group from a molecule and releases CO2, which can activate certain acidic precursor compounds into their biologically active forms in medical chemistry.

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.

Pyruvate decarboxylase is an enzyme that plays a crucial role in the cellular process of fermentation and gluconeogenesis. In medical and biochemical terms, pyruvate decarboxylase is defined as:

"An enzyme (EC 4.1.1.1) that catalyzes the decarboxylation of pyruvate to form acetaldehyde and carbon dioxide in the presence of thiamine pyrophosphate (TPP) as a cofactor. This reaction occurs during anaerobic metabolism, such as alcohol fermentation in yeast or bacteria, and helps to generate ATP and NADH for the cell's energy needs."

In humans, pyruvate decarboxylase is primarily found in the liver and kidneys, where it participates in gluconeogenesis – the process of generating new glucose molecules from non-carbohydrate precursors. The enzyme's activity is essential for maintaining blood glucose levels during fasting or low-carbohydrate intake.

Deficiencies in pyruvate decarboxylase can lead to metabolic disorders, such as pyruvate decarboxylase deficiency (PDC deficiency), which is characterized by lactic acidosis, developmental delays, and neurological issues. Proper diagnosis and management of these conditions often involve monitoring enzyme activity and glucose metabolism.

Orotidine-5’-phosphate decarboxylase (ODC) is an enzyme that is involved in the synthesis of pyrimidines, which are essential nucleotides required for the production of DNA and RNA. The gene that encodes this enzyme is called UMPS.

ODC catalyzes the decarboxylation of orotidine-5’-phosphate (OMP) to form uridine monophosphate (UMP), which is a precursor to other pyrimidines such as cytidine triphosphate (CTP) and thymidine triphosphate (TTP). This reaction is the fifth step in the de novo synthesis of pyrimidines.

Defects in the ODC enzyme can lead to a rare genetic disorder called orotic aciduria, which is characterized by an accumulation of orotic acid and orotidine in the urine, as well as neurological symptoms such as developmental delay, seizures, and ataxia. Treatment for this condition typically involves supplementation with uridine and a low-protein diet to reduce the production of excess orotic acid.

Thiamine pyrophosphate (TPP) is the active form of thiamine (vitamin B1) that plays a crucial role as a cofactor in various enzymatic reactions, particularly in carbohydrate metabolism. TPP is essential for the functioning of three key enzymes: pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase, and transketolase. These enzymes are involved in critical processes such as the conversion of pyruvate to acetyl-CoA, the oxidative decarboxylation of alpha-ketoglutarate in the Krebs cycle, and the pentose phosphate pathway, which is important for generating reducing equivalents (NADPH) and ribose sugars for nucleotide synthesis. A deficiency in thiamine or TPP can lead to severe neurological disorders, including beriberi and Wernicke-Korsakoff syndrome, which are often observed in alcoholics due to poor nutrition and impaired thiamine absorption.

Porphyrinogens are organic compounds that are the precursors to porphyrins, which are ring-shaped molecules found in many important biological molecules such as hemoglobin and cytochromes. Porphyrinogens are themselves derived from the condensation of four pyrrole molecules, and they undergo further reactions to form porphyrins.

In particular, porphyrinogens are intermediates in the biosynthesis of heme, which is a complex organic ring-shaped molecule that contains iron and plays a critical role in oxygen transport and storage in the body. Abnormalities in heme biosynthesis can lead to various medical conditions known as porphyrias, which are characterized by the accumulation of porphyrinogens and other intermediates in this pathway. These conditions can cause a range of symptoms, including neurological problems, skin sensitivity to light, and abdominal pain.

Oxaloacetates are organic compounds that are integral to the Krebs cycle, also known as the citric acid cycle, in biological energy production. Specifically, oxaloacetate is an important intermediate compound within this metabolic pathway, found in the mitochondria of cells.

In the context of a medical definition, oxaloacetates are not typically referred to directly. Instead, the term "oxaloacetic acid" might be used, which is the conjugate acid of the oxaloacetate ion. Oxaloacetic acid has the chemical formula C4H4O5 and appears in various biochemical reactions as a crucial component of cellular respiration.

The Krebs cycle involves several stages where oxaloacetic acid plays a significant role:

1. In the first step, oxaloacetic acid combines with an acetyl group (derived from acetyl-CoA) to form citric acid, releasing coenzyme A in the process. This reaction is catalyzed by citrate synthase.
2. Throughout subsequent steps of the cycle, citric acid undergoes a series of reactions that generate energy in the form of NADH and FADH2 (reduced forms of nicotinamide adenine dinucleotide and flavin adenine dinucleotide, respectively), as well as GTP (guanosine triphosphate).
3. At the end of the cycle, oxaloacetic acid is regenerated to continue the process anew. This allows for continuous energy production within cells.

In summary, while "oxaloacetates" isn't a standard term in medical definitions, it does refer to an essential component (oxaloacetic acid) of the Krebs cycle that plays a critical role in cellular respiration and energy production.

Agmatine is a natural decarboxylated derivative of the amino acid L-arginine. It is formed in the body through the enzymatic degradation of arginine by the enzyme arginine decarboxylase. Agmatine is involved in various biological processes, including serving as a neurotransmitter and neuromodulator in the central nervous system. It has been shown to play roles in regulating pain perception, insulin secretion, cardiovascular function, and cell growth. Agmatine can also interact with several receptors, such as imidazoline receptors, α2-adrenergic receptors, and NMDA receptors, which contributes to its diverse physiological effects.

Coproporphyrinogens are intermediates in the biosynthesis of heme, a complex molecule that is essential for various biological processes including oxygen transport and cellular respiration. There are two types of coproporphyrinogens: Coproporphyrinogen I and Coproporphyrinogen III.

Coproporphyrinogen I is an intermediate in the biosynthesis of siroheme, a porphyrin-like molecule that functions as a cofactor for enzymes involved in sulfur and nitrogen metabolism. It is produced from uroporphyrinogen III through the action of coproporphyrinogen oxidase.

Coproporphyrinogen III, on the other hand, is an intermediate in the biosynthesis of heme. It is produced from protoporphyrinogen IX through the action of coproporphyrinogen oxidase and then converted to protoporphyrin IX by the enzyme coproporphyrinogen III decarboxylase. Protoporphyrin IX is then converted to heme by the addition of iron in a reaction catalyzed by ferrochelatase.

Abnormal accumulation of coproporphyrinogens can occur due to various genetic and acquired disorders that affect enzymes involved in heme biosynthesis, leading to the accumulation of porphyrins and their precursors in tissues and bodily fluids. These conditions are known as porphyrias and can present with a variety of symptoms including neuropsychiatric manifestations, skin lesions, and gastrointestinal disturbances.

Keto acids, also known as ketone bodies, are not exactly the same as "keto acids" in the context of amino acid metabolism.

In the context of metabolic processes, ketone bodies are molecules that are produced as byproducts when the body breaks down fat for energy instead of carbohydrates. When carbohydrate intake is low, the liver converts fatty acids into ketone bodies, which can be used as a source of energy by the brain and other organs. The three main types of ketone bodies are acetoacetate, beta-hydroxybutyrate, and acetone.

However, in the context of amino acid metabolism, "keto acids" refer to the carbon skeletons of certain amino acids that remain after their nitrogen-containing groups have been removed during the process of deamination. These keto acids can then be converted into glucose or used in other metabolic pathways. For example, the keto acid produced from the amino acid leucine is called beta-ketoisocaproate.

Therefore, it's important to clarify the context when discussing "keto acids" as they can refer to different things depending on the context.

Pyruvate is a negatively charged ion or group of atoms, called anion, with the chemical formula C3H3O3-. It is formed from the decomposition of glucose and other sugars in the process of cellular respiration. Pyruvate plays a crucial role in the metabolic pathways that generate energy for cells.

In the cytoplasm, pyruvate is produced through glycolysis, where one molecule of glucose is broken down into two molecules of pyruvate, releasing energy and producing ATP (adenosine triphosphate) and NADH (reduced nicotinamide adenine dinucleotide).

In the mitochondria, pyruvate can be further metabolized through the citric acid cycle (also known as the Krebs cycle) to produce more ATP. The process involves the conversion of pyruvate into acetyl-CoA, which then enters the citric acid cycle and undergoes a series of reactions that generate energy in the form of ATP, NADH, and FADH2 (reduced flavin adenine dinucleotide).

Overall, pyruvate is an important intermediate in cellular respiration and plays a central role in the production of energy for cells.

Aromatic-L-amino-acid decarboxylases (ALADs) are a group of enzymes that play a crucial role in the synthesis of neurotransmitters and biogenic amines in the body. These enzymes catalyze the decarboxylation of aromatic L-amino acids, such as L-dopa, L-tryptophan, and L-phenylalanine, to produce corresponding neurotransmitters or biogenic amines, including dopamine, serotonin, and histamine, respectively.

There are two main types of ALADs in humans: dopa decarboxylase (DDC) and tryptophan hydroxylase (TPH). DDC is responsible for the conversion of L-dopa to dopamine, which is a crucial neurotransmitter involved in movement regulation. TPH, on the other hand, catalyzes the rate-limiting step in serotonin synthesis by converting L-tryptophan to 5-hydroxytryptophan (5-HTP), which is then converted to serotonin by another enzyme called aromatic amino acid decarboxylase.

Deficiencies or mutations in ALADs can lead to various neurological and psychiatric disorders, such as Parkinson's disease, dopa-responsive dystonia, and depression. Therefore, understanding the function and regulation of ALADs is essential for developing effective therapies for these conditions.

Uroporphyrinogen decarboxylase is a vital enzyme in the biosynthetic pathway of heme, which is a crucial component of hemoglobin in red blood cells. This enzyme is responsible for catalyzing the decarboxylation of uroporphyrinogen III, a colorless porphyrinogen, to produce coproporphyrinogen III, a brownish-red porphyrinogen.

The reaction involves the sequential removal of four carboxyl groups from the four acetic acid side chains of uroporphyrinogen III, resulting in the formation of coproporphyrinogen III. This enzyme's activity is critical for the normal biosynthesis of heme, and any defects or deficiencies in its function can lead to various porphyrias, a group of metabolic disorders characterized by the accumulation of porphyrins and their precursors in the body.

The gene responsible for encoding uroporphyrinogen decarboxylase is UROD, located on chromosome 1p34.1. Mutations in this gene can lead to a deficiency in the enzyme's activity, causing an autosomal recessive disorder known as congenital erythropoietic porphyria (CEP), also referred to as Günther's disease. This condition is characterized by severe photosensitivity, hemolytic anemia, and scarring or thickening of the skin.

Carboxylic acids are organic compounds that contain a carboxyl group, which is a functional group made up of a carbon atom doubly bonded to an oxygen atom and single bonded to a hydroxyl group. The general formula for a carboxylic acid is R-COOH, where R represents the rest of the molecule.

Carboxylic acids can be found in various natural sources such as in fruits, vegetables, and animal products. Some common examples of carboxylic acids include formic acid (HCOOH), acetic acid (CH3COOH), propionic acid (C2H5COOH), and butyric acid (C3H7COOH).

Carboxylic acids have a variety of uses in industry, including as food additives, pharmaceuticals, and industrial chemicals. They are also important intermediates in the synthesis of other organic compounds. In the body, carboxylic acids play important roles in metabolism and energy production.

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.

Pyruvic acid, also known as 2-oxopropanoic acid, is a key metabolic intermediate in both anaerobic and aerobic respiration. It is a carboxylic acid with a ketone functional group, making it a β-ketoacid. In the cytosol, pyruvate is produced from glucose during glycolysis, where it serves as a crucial link between the anaerobic breakdown of glucose and the aerobic process of cellular respiration in the mitochondria.

During low oxygen availability or high energy demands, pyruvate can be converted into lactate through anaerobic glycolysis, allowing for the continued production of ATP (adenosine triphosphate) without oxygen. In the presence of adequate oxygen and functional mitochondria, pyruvate is transported into the mitochondrial matrix where it undergoes oxidative decarboxylation to form acetyl-CoA by the enzyme pyruvate dehydrogenase complex (PDC). This reaction also involves the reduction of NAD+ to NADH and the release of CO2. Acetyl-CoA then enters the citric acid cycle, where it is further oxidized to produce energy in the form of ATP, NADH, FADH2, and GTP (guanosine triphosphate) through a series of enzymatic reactions.

In summary, pyruvic acid is a vital metabolic intermediate that plays a significant role in energy production pathways, connecting glycolysis to both anaerobic and aerobic respiration.

Uridine Monophosphate (UMP) is a nucleotide that is a constituent of RNA (Ribonucleic Acid). It consists of a nitrogenous base called Uridine, linked to a sugar molecule (ribose) and a phosphate group. UMP plays a crucial role in various biochemical reactions within the body, including energy transfer and cellular metabolism. It is also involved in the synthesis of other nucleotides and serves as an important precursor in the production of genetic material during cell division.

Coproporphyrinogen Oxidase is a mitochondrial enzyme that plays a crucial role in the biosynthesis of heme, which is an essential component of hemoglobin and other hemoproteins. This enzyme catalyzes the oxidative decarboxylation of coproporphyrinogen III to protoporphyrinogen IX, a key step in the heme biosynthetic pathway.

Deficiency or dysfunction of Coproporphyrinogen Oxidase can lead to a rare genetic disorder known as Hereditary Coproporphyria (HCP), which is characterized by the accumulation of coproporphyrinogen III and its derivative, coproporphyrin, in various tissues and body fluids. This accumulation can result in a range of symptoms, including abdominal pain, neurological disturbances, and skin manifestations.

Vanillic Acid is not a medical term, but it is a chemical compound with the name 4-hydroxy-3-methoxybenzoic acid. It is a type of phenolic acid that occurs naturally in some foods and plants, including vanilla beans, pineapples, and certain types of mushrooms.

Vanillic Acid has been studied for its potential antioxidant, anti-inflammatory, and neuroprotective properties. However, it is not considered a medication or a medical treatment and does not have a specific medical definition.

Ketone oxidoreductases are a group of enzymes that catalyze the conversion of ketones to corresponding alcohols or vice versa, through the process of reduction or oxidation. These enzymes play an essential role in various metabolic pathways and biochemical reactions within living organisms.

In the context of medical research and diagnostics, ketone oxidoreductases have gained attention for their potential applications in the development of biosensors to detect and monitor blood ketone levels, particularly in patients with diabetes. Elevated levels of ketones in the blood (known as ketonemia) can indicate a serious complication called diabetic ketoacidosis, which requires prompt medical attention.

One example of a ketone oxidoreductase is the enzyme known as d-beta-hydroxybutyrate dehydrogenase (d-BDH), which catalyzes the conversion of d-beta-hydroxybutyrate to acetoacetate. This reaction is part of the metabolic pathway that breaks down fatty acids for energy production, and it becomes particularly important during periods of low carbohydrate availability or insulin deficiency, as seen in diabetes.

Understanding the function and regulation of ketone oxidoreductases can provide valuable insights into the pathophysiology of metabolic disorders like diabetes and contribute to the development of novel therapeutic strategies for their management.

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.

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!

APUD cells are a type of neuroendocrine cell that originated from the neural crest and are widely distributed throughout the body. The term "APUD" is an acronym for "Amine Precursor Uptake and Decarboxylation," which describes the ability of these cells to take up and decarboxylate amino acid precursors to produce biologically active amines, such as serotonin, histamine, and catecholamines.

APUD cells are capable of synthesizing, storing, and releasing hormones or neurotransmitters in response to various stimuli. They can be found in several endocrine and neural tissues, including the thyroid gland, adrenal medulla, pituitary gland, pancreas, lungs, and gastrointestinal tract.

In the gastrointestinal tract, APUD cells are often referred to as enterochromaffin cells or Kulchitsky cells. They play a crucial role in regulating gut motility, secretion, and blood flow through the release of hormones such as serotonin, gastrin, and somatostatin.

It's worth noting that the APUD cell concept has been largely replaced by the more comprehensive neuroendocrine system concept, which encompasses a broader range of cells with neurosecretory functions.

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.

"Caproates" is not a term commonly used in medical terminology. It appears to be a derivative of "caproic acid," which is an organic compound with the formula CH3CH2CH2CH2CO2H. Caproic acid is one of several saturated fatty acids that are abundant in animal fats and have a distinctive rancid odor when they spoil or break down.

However, I was unable to find any specific medical definition or use of the term "caproates" in the context of medicine or healthcare. It is possible that this term may be used in a different field or context, such as chemistry or biochemistry. If you have more information about the context in which you encountered this term, I may be able to provide a more accurate answer.

Uroporphyrinogens are organic compounds that are intermediate products in the synthesis of heme, which is a crucial component of hemoglobin and other important molecules in the body. Specifically, uroporphyrinogens are tetrapyrroles, which means they contain four pyrrole rings linked together. They have eight carboxylic acid side chains and two propionic acid side chains.

There are two types of uroporphyrinogens: Type I and Type III. Uroporphyrinogen III is the precursor to heme, while uroporphyrinogen I is a dead-end metabolite that is not used in heme synthesis. Defects in the enzymes involved in heme biosynthesis can lead to various porphyrias, which are genetic disorders characterized by the accumulation of porphyrins and their precursors in the body.

Guaiacol is not a medical term per se, but it is a chemical compound with potential applications in the medical field. Here's a general definition:

Guaiacol (also known as 2-methoxyphenol) is an organic compound that belongs to the class of phenols. It is a colorless or slightly yellow oily liquid with a characteristic smoky odor, and it is soluble in alcohol and ether but only sparingly soluble in water. Guaiacol occurs naturally in the smoke of wood fires and is also found in certain plants, such as guaiacum and creosote bush. It has antimicrobial properties and is used in some medical and industrial applications, including as a precursor for the synthesis of other chemicals.

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.

I'm sorry for any confusion, but "Mandelic Acids" is not a recognized medical term or concept in dermatology or medicine. Mandelic acid, however, is a type of chemical compound used in skincare products for various purposes such as exfoliation and reducing hyperpigmentation. It is an aromatic hydroxyacetic acid derived from mandelic almonds. If you have any questions about skincare ingredients or treatments, I'd be happy to help clarify those for you!

Ethanolamine is an organic compound that is a primary amine and a secondary alcohol. It is a colorless, viscous liquid with an odor similar to ammonia. Ethanolamine is used in the manufacture of a wide variety of products including detergents, pharmaceuticals, polishes, inks, textiles, and plastics. In the body, ethanolamine is a component of many important molecules, such as phosphatidylethanolamine, which is a major constituent of cell membranes. It is also involved in the synthesis of neurotransmitters and hormones.

I believe you may have meant to ask for the definition of "pyruvate dehydrogenase complex" rather than "pyruvate synthase," as I couldn't find any relevant medical information regarding a specific enzyme named "pyruvate synthase."

Pyruvate dehydrogenase complex (PDC) is a crucial enzyme complex in the human body, playing an essential role in cellular energy production. PDC is located within the mitochondrial matrix and catalyzes the oxidative decarboxylation of pyruvate, the end product of glycolysis, into acetyl-CoA. This process connects the glycolytic pathway to the citric acid cycle (Krebs cycle) and enables the continuation of aerobic respiration for efficient energy production in the form of ATP.

The pyruvate dehydrogenase complex consists of three main enzymes: pyruvate dehydrogenase (E1), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3). Additionally, two accessory proteins, E3-binding protein (E3BP) and protein X, are part of the complex. These enzymes work together to facilitate the conversion of pyruvate into acetyl-CoA, CO2, and NADH. Dysfunction in the pyruvate dehydrogenase complex can lead to various metabolic disorders and neurological symptoms.

The Pyruvate Dehydrogenase Complex (PDC) is a multi-enzyme complex that plays a crucial role in cellular energy metabolism. It is located in the mitochondrial matrix and catalyzes the oxidative decarboxylation of pyruvate, the end product of glycolysis, into acetyl-CoA. This reaction links the carbohydrate metabolism (glycolysis) to the citric acid cycle (Krebs cycle), enabling the continuation of energy production in the form of ATP through oxidative phosphorylation.

The Pyruvate Dehydrogenase Complex consists of three main enzymes: pyruvate dehydrogenase (E1), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3). Additionally, two regulatory enzymes are associated with the complex: pyruvate dehydrogenase kinase (PDK) and pyruvate dehydrogenase phosphatase (PDP). These regulatory enzymes control the activity of the PDC through reversible phosphorylation and dephosphorylation, allowing the cell to adapt to varying energy demands and substrate availability.

Deficiencies or dysfunctions in the Pyruvate Dehydrogenase Complex can lead to various metabolic disorders, such as pyruvate dehydrogenase deficiency, which may result in neurological impairments and lactic acidosis due to disrupted energy metabolism.

Veillonella is a genus of Gram-negative, anaerobic, non-spore-forming, coccoid or rod-shaped bacteria. These bacteria are commonly found as normal flora in the human mouth, intestines, and female genital tract. They are known to be obligate parasites, meaning they rely on other organisms for nutrients and energy. Veillonella species are often associated with dental caries and have been implicated in various infections such as bacteremia, endocarditis, pneumonia, and wound infections, particularly in immunocompromised individuals or those with underlying medical conditions. Proper identification of Veillonella species is important for the diagnosis and treatment of these infections.

Dihydroxyphenylalanine is not a medical term per se, but it is a chemical compound that is often referred to in the context of biochemistry and neuroscience. It is also known as levodopa or L-DOPA for short.

L-DOPA is a precursor to dopamine, a neurotransmitter that plays a critical role in regulating movement, emotion, and cognition. In the brain, L-DOPA is converted into dopamine through the action of an enzyme called tyrosine hydroxylase.

L-DOPA is used medically to treat Parkinson's disease, a neurological disorder characterized by motor symptoms such as tremors, rigidity, and bradykinesia (slowness of movement). In Parkinson's disease, the dopamine-producing neurons in the brain gradually degenerate, leading to a deficiency of dopamine. By providing L-DOPA as a replacement therapy, doctors can help alleviate some of the symptoms of the disease.

It is important to note that L-DOPA has potential side effects and risks, including nausea, dizziness, and behavioral changes. Long-term use of L-DOPA can also lead to motor complications such as dyskinesias (involuntary movements) and fluctuations in response to the medication. Therefore, it is typically used in combination with other medications and under the close supervision of a healthcare provider.

Carbon dioxide (CO2) is a colorless, odorless gas that is naturally present in the Earth's atmosphere. It is a normal byproduct of cellular respiration in humans, animals, and plants, and is also produced through the combustion of fossil fuels such as coal, oil, and natural gas.

In medical terms, carbon dioxide is often used as a respiratory stimulant and to maintain the pH balance of blood. It is also used during certain medical procedures, such as laparoscopic surgery, to insufflate (inflate) the abdominal cavity and create a working space for the surgeon.

Elevated levels of carbon dioxide in the body can lead to respiratory acidosis, a condition characterized by an increased concentration of carbon dioxide in the blood and a decrease in pH. This can occur in conditions such as chronic obstructive pulmonary disease (COPD), asthma, or other lung diseases that impair breathing and gas exchange. Symptoms of respiratory acidosis may include shortness of breath, confusion, headache, and in severe cases, coma or death.

An "apudoma" is a term that refers to a type of neuroendocrine tumor that originates from cells known as "APUD (Amine Precursor Uptake and Decarboxylation) cells." These cells are capable of taking up and decarboxylating amine precursors, which are substances that can be converted into neurotransmitters or hormones.

Apudomas can occur in various organs throughout the body, including the pancreas, lung, thyroid, and gastrointestinal tract. Some examples of apudomas include:

* Pancreatic neuroendocrine tumors (PNETs) or islet cell tumors
* Small cell lung cancer
* Medullary thyroid carcinoma
* Merkel cell carcinoma
* Carcinoid tumors

These tumors can produce and secrete a variety of hormones and neurotransmitters, leading to a range of clinical symptoms. Treatment options for apudomas may include surgery, radiation therapy, chemotherapy, or targeted therapies that are designed to specifically target the abnormal cells.

Cytidine diphosphate (CDP) is a nucleotide that is a constituent of coenzymes and plays a role in the synthesis of lipids, such as phosphatidylcholine and sphingomyelin, which are important components of cell membranes. It is formed from cytidine monophosphate (CMP) through the addition of a second phosphate group by the enzyme CTP synthase. CDP can also be converted to other nucleotides, such as uridine diphosphate (UDP) and deoxythymidine diphosphate (dTDP), through the action of various enzymes. These nucleotides play important roles in the biosynthesis of carbohydrates, lipids, and other molecules in the cell.

Phosphatidylserines are a type of phospholipids that are essential components of the cell membrane, particularly in the brain. They play a crucial role in maintaining the fluidity and permeability of the cell membrane, and are involved in various cellular processes such as signal transduction, protein anchorage, and apoptosis (programmed cell death). Phosphatidylserines contain a polar head group made up of serine amino acids and two non-polar fatty acid tails. They are abundant in the inner layer of the cell membrane but can be externalized to the outer layer during apoptosis, where they serve as signals for recognition and removal of dying cells by the immune system. Phosphatidylserines have been studied for their potential benefits in various medical conditions, including cognitive decline, Alzheimer's disease, and depression.

Food preservatives are substances added to foods to prevent or slow down spoilage caused by microorganisms such as bacteria, yeasts, and molds, or to retard quality deterioration due to oxidation or other chemical reactions. They work by inhibiting the growth of microorganisms, preventing enzymatic reactions that cause spoilage, or scavenging oxygen that can lead to food degradation. Examples of commonly used food preservatives include sodium benzoate, potassium sorbate, sulfites, and nitrites. It is important to note that while food preservatives play a crucial role in maintaining the safety and quality of our food supply, excessive consumption of certain preservatives may have adverse health effects.

Malate Dehydrogenase (MDH) is an enzyme that plays a crucial role in the Krebs cycle, also known as the citric acid cycle or tricarboxylic acid (TCA) cycle. It catalyzes the reversible oxidation of malate to oxaloacetate, while simultaneously reducing NAD+ to NADH. This reaction is essential for energy production in the form of ATP and NADH within the cell.

There are two main types of Malate Dehydrogenase:

1. NAD-dependent Malate Dehydrogenase (MDH1): Found primarily in the cytoplasm, this isoform plays a role in the malate-aspartate shuttle, which helps transfer reducing equivalents between the cytoplasm and mitochondria.
2. FAD-dependent Malate Dehydrogenase (MDH2): Located within the mitochondrial matrix, this isoform is involved in the Krebs cycle for energy production.

Abnormal levels of Malate Dehydrogenase enzyme can be indicative of certain medical conditions or diseases, such as myocardial infarction (heart attack), muscle damage, or various types of cancer. Therefore, MDH enzyme activity is often assessed in diagnostic tests to help identify and monitor these health issues.

Pyruvate oxidase is not a term that has a widely recognized medical definition. However, pyruvate oxidase is an enzyme that plays a role in the metabolism of glucose in cells. It is involved in the conversion of pyruvate, a product of glycolysis, into acetyl-CoA, which can then be used in the citric acid cycle (also known as the Krebs cycle) to generate energy in the form of ATP.

Pyruvate oxidase is found in the mitochondria of cells and requires molecular oxygen (O2) to function. It catalyzes the following reaction:

pyruvate + CoA + NAD+ + H2O → acetyl-CoA + CO2 + NADH + H+

Deficiencies in pyruvate oxidase have been associated with certain metabolic disorders, such as pyruvate dehydrogenase deficiency and Leigh syndrome. However, these conditions are typically caused by defects in other enzymes involved in the metabolism of pyruvate rather than pyruvate oxidase itself.

Cadaverine is a foul-smelling organic compound that is produced by the breakdown of certain amino acids in dead bodies. It is formed through the decarboxylation of lysine, an essential amino acid, and is characterized by its strong, unpleasant odor. Cadaverine is often used as a forensic indicator of decomposition and is also being studied for its potential role in various physiological processes, such as inflammation and cancer.

Lactobacillales is an order of predominantly gram-positive, facultatively anaerobic or aerotolerant, rod-shaped bacteria. They are non-spore forming and often occur in pairs or chains. Lactobacillales are commonly found in various environments such as plants, sewage, dairy products, and the gastrointestinal and genitourinary tracts of humans and animals.

They are known for their ability to produce lactic acid as a major metabolic end product, hence the name "lactic acid bacteria." This characteristic makes them essential in food fermentation processes, including the production of yogurt, cheese, sauerkraut, and other fermented foods.

Within Lactobacillales, there are several families, including Aerococcaceae, Carnobacteriaceae, Enterococcaceae, Lactobacillaceae, Leuconostocaceae, and Streptococcaceae. Many species within these families have significant roles in human health and disease, either as beneficial probiotics or as pathogenic agents causing various types of infections.

Methylmalonyl-CoA decarboxylase is a mitochondrial enzyme that plays a crucial role in the metabolism of certain amino acids and fatty acids. Specifically, it catalyzes the conversion of methylmalonyl-CoA to propionyl-CoA through the decarboxylation of the thioester bond.

The reaction is as follows:

Methylmalonyl-CoA → Propionyl-CoA + CO2

This enzyme requires biotin as a cofactor, and its activity is reduced in individuals with methylmalonic acidemia, a rare inherited metabolic disorder caused by mutations in the MMAB or MCEE genes that encode subunits of the methylmalonyl-CoA decarboxylase enzyme complex.

Deficiency of this enzyme leads to an accumulation of methylmalonic acid and methylmalonyl-CoA, which can cause metabolic acidosis, hyperammonemia, and other symptoms associated with the disorder.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Lactobacillus brevis is a species of gram-positive, rod-shaped, facultatively anaerobic bacteria that belongs to the lactic acid bacteria group. It is commonly found in various environments such as plants, soil, and fermented foods like sauerkraut, pickles, and sourdough bread. Lactobacillus brevis is also part of the normal microbiota of the human gastrointestinal tract and vagina.

This bacterium is known for its ability to produce lactic acid as a metabolic end-product, which contributes to the preservation and fermentation of food. Lactobacillus brevis can also produce other compounds with potential health benefits, such as bacteriocins, which have antibacterial properties against certain pathogenic bacteria.

In some cases, Lactobacillus brevis has been investigated for its probiotic potential, although more research is needed to fully understand its effects on human health. It's important to note that while some strains of Lactobacillus brevis may have beneficial properties, others can cause infections in individuals with weakened immune systems or underlying medical conditions.

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.

Coenzyme A, often abbreviated as CoA or sometimes holo-CoA, is a coenzyme that plays a crucial role in several important chemical reactions in the body, particularly in the metabolism of carbohydrates, fatty acids, and amino acids. It is composed of a pantothenic acid (vitamin B5) derivative called pantothenate, an adenosine diphosphate (ADP) molecule, and a terminal phosphate group.

Coenzyme A functions as a carrier molecule for acetyl groups, which are formed during the breakdown of carbohydrates, fatty acids, and some amino acids. The acetyl group is attached to the sulfur atom in CoA, forming acetyl-CoA, which can then be used as a building block for various biochemical pathways, such as the citric acid cycle (Krebs cycle) and fatty acid synthesis.

In summary, Coenzyme A is a vital coenzyme that helps facilitate essential metabolic processes by carrying and transferring acetyl groups in the body.

Oxythiamine is not a medication or a condition, but rather a chemical compound. It is an oxidized form of thiamine (vitamin B1), which means it has been changed by the addition of oxygen molecules. Oxythiamine is used in research to study the effects of thiamine deficiency and to investigate the role of thiamine in various biological processes. It is not used as a medication in humans or animals.

Carbon isotopes are variants of the chemical element carbon that have different numbers of neutrons in their atomic nuclei. The most common and stable isotope of carbon is carbon-12 (^{12}C), which contains six protons and six neutrons. However, carbon can also come in other forms, known as isotopes, which contain different numbers of neutrons.

Carbon-13 (^{13}C) is a stable isotope of carbon that contains seven neutrons in its nucleus. It makes up about 1.1% of all carbon found on Earth and is used in various scientific applications, such as in tracing the metabolic pathways of organisms or in studying the age of fossilized materials.

Carbon-14 (^{14}C), also known as radiocarbon, is a radioactive isotope of carbon that contains eight neutrons in its nucleus. It is produced naturally in the atmosphere through the interaction of cosmic rays with nitrogen gas. Carbon-14 has a half-life of about 5,730 years, which makes it useful for dating organic materials, such as archaeological artifacts or fossils, up to around 60,000 years old.

Carbon isotopes are important in many scientific fields, including geology, biology, and medicine, and are used in a variety of applications, from studying the Earth's climate history to diagnosing medical conditions.

Sorbic acid is a chemical compound that is commonly used as a preservative in various food and cosmetic products. Medically, it's not typically used as a treatment for any specific condition. However, its preservative properties help prevent the growth of bacteria, yeast, and mold, which can improve the safety and shelf life of certain medical supplies such as ointments and eye drops.

The chemical structure of sorbic acid is that of a carboxylic acid with two double bonds, making it a unsaturated fatty acid. It's naturally found in some fruits like rowanberries and serviceberries, but most commercial sorbic acid is synthetically produced.

Food-grade sorbic acid is generally recognized as safe (GRAS) by the U.S. Food and Drug Administration (FDA), and it has a wide range of applications in food preservation, including baked goods, cheeses, wines, and fruit juices. In cosmetics, it's often used to prevent microbial growth in products like creams, lotions, and makeup.

It is important to note that some people may have allergic reactions to sorbic acid or its salts (sorbates), so caution should be exercised when introducing new products containing these substances into personal care routines or diets.

Acetyl Coenzyme A, often abbreviated as Acetyl-CoA, is a key molecule in metabolism, particularly in the breakdown and oxidation of carbohydrates, fats, and proteins to produce energy. It is a coenzyme that plays a central role in the cellular process of transforming the energy stored in the chemical bonds of nutrients into a form that the cell can use.

Acetyl-CoA consists of an acetyl group (two carbon atoms) linked to coenzyme A, a complex organic molecule. This linkage is facilitated by an enzyme called acetyltransferase. Once formed, Acetyl-CoA can enter various metabolic pathways. In the citric acid cycle (also known as the Krebs cycle), Acetyl-CoA is further oxidized to release energy in the form of ATP, NADH, and FADH2, which are used in other cellular processes. Additionally, Acetyl-CoA is involved in the biosynthesis of fatty acids, cholesterol, and certain amino acids.

In summary, Acetyl Coenzyme A is a vital molecule in metabolism that connects various biochemical pathways for energy production and biosynthesis.

Hydroxybenzoates are the salts or esters of hydroxybenzoic acids. They are commonly used as preservatives in food, cosmetics, and pharmaceutical products due to their antimicrobial and antifungal properties. The most common examples include methylparaben, ethylparaben, propylparaben, and butylparaben. These compounds work by inhibiting the growth of bacteria and fungi, thereby increasing the shelf life and safety of various products. However, there has been some concern about their potential health effects, including possible hormonal disruption, and their use in certain applications is being re-evaluated.

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.

Pyruvate carboxylase is a biotin-containing enzyme that plays a crucial role in gluconeogenesis, the process of generating new glucose molecules from non-carbohydrate sources. The enzyme catalyzes the conversion of pyruvate to oxaloacetate, an important intermediate in several metabolic pathways, particularly in the liver, kidneys, and brain.

The reaction catalyzed by pyruvate carboxylase is as follows:

Pyruvate + CO2 + ATP + H2O → Oxaloacetate + ADP + Pi + 2H+

In this reaction, pyruvate reacts with bicarbonate (HCO3-) to form oxaloacetate, consuming one molecule of ATP in the process. The generation of oxaloacetate provides a key entry point for non-carbohydrate precursors, such as lactate and certain amino acids, to enter the gluconeogenic pathway.

Pyruvate carboxylase deficiency is a rare but severe genetic disorder that can lead to neurological impairment and developmental delays due to the disruption of energy metabolism in the brain.

In medical terms, acids refer to a class of chemicals that have a pH less than 7 and can donate protons (hydrogen ions) in chemical reactions. In the context of human health, acids are an important part of various bodily functions, such as digestion. However, an imbalance in acid levels can lead to medical conditions. For example, an excess of hydrochloric acid in the stomach can cause gastritis or peptic ulcers, while an accumulation of lactic acid due to strenuous exercise or decreased blood flow can lead to muscle fatigue and pain.

Additionally, in clinical laboratory tests, certain substances may be tested for their "acidity" or "alkalinity," which is measured using a pH scale. This information can help diagnose various medical conditions, such as kidney disease or diabetes.

Cinnamates are organic compounds that are derived from cinnamic acid. They contain a carbon ring with a double bond and a carboxylic acid group, making them aromatic acids. Cinnamates are widely used in the perfume industry due to their pleasant odor, and they also have various applications in the pharmaceutical and chemical industries.

In a medical context, cinnamates may be used as topical medications for the treatment of skin conditions such as fungal infections or inflammation. For example, cinnamate esters such as cinoxacin and ciclopirox are commonly used as antifungal agents in creams, lotions, and shampoos. These compounds work by disrupting the cell membranes of fungi, leading to their death.

Cinnamates may also have potential therapeutic benefits for other medical conditions. For instance, some studies suggest that cinnamate derivatives may have anti-inflammatory, antioxidant, and neuroprotective properties, making them promising candidates for the development of new drugs to treat diseases such as Alzheimer's and Parkinson's. However, more research is needed to confirm these effects and determine their safety and efficacy in humans.

"Malonates" is not a recognized medical term. However, in chemistry, malonates refer to salts or esters of malonic acid, a dicarboxylic acid with the formula CH2(COOH)2. Malonic acid and its derivatives have been used in the synthesis of various pharmaceuticals and chemicals, but they are not typically associated with any specific medical condition or treatment. If you have encountered the term "malonates" in a medical context, it may be helpful to provide more information or seek clarification from the source.

Adipates are a group of chemical compounds that are esters of adipic acid. Adipic acid is a dicarboxylic acid with the formula (CH₂)₄(COOH)₂. Adipates are commonly used as plasticizers in the manufacture of polyvinyl chloride (PVC) products, such as pipes, cables, and flooring. They can also be found in cosmetics, personal care products, and some food additives.

Adipates are generally considered to be safe for use in consumer products, but like all chemicals, they should be used with caution and in accordance with recommended guidelines. Some adipates have been shown to have potential health effects, such as endocrine disruption and reproductive toxicity, at high levels of exposure. Therefore, it is important to follow proper handling and disposal procedures to minimize exposure.

"Valerates" is not a recognized medical term. However, it may refer to a salt or ester of valeric acid, which is a carboxylic acid with the formula CH3CH2CH2CO2H. Valeric acid and its salts and esters are used in pharmaceuticals and perfumes. Valerates can have a sedative effect and are sometimes used as a treatment for anxiety or insomnia. One example is sodium valerate, which is used in the manufacture of some types of medical-grade polyester. Another example is diethyl valerate, an ester of valeric acid that is used as a flavoring agent and solvent.

Carbidopa is a peripheral decarboxylase inhibitor used in the treatment of Parkinson's disease. It works by preventing the conversion of levodopa to dopamine outside of the brain, allowing more levodopa to reach the brain and reduce the symptoms of Parkinson's disease. Carbidopa is often combined with levodopa in medication formulations and is available under various brand names, such as Sinemet.

Here are some key points about carbidopa:

* It is a peripheral decarboxylase inhibitor that prevents the conversion of levodopa to dopamine outside of the brain.
* Carbidopa is often combined with levodopa in medication formulations for the treatment of Parkinson's disease.
* By preventing the conversion of levodopa to dopamine outside of the brain, more levodopa can reach the brain and reduce the symptoms of Parkinson's disease.
* Common side effects of carbidopa include nausea, vomiting, and orthostatic hypotension.
* Carbidopa should be used under the guidance of a healthcare professional and dosed appropriately to minimize side effects and maximize therapeutic benefit.

Deamination is a biochemical process that refers to the removal of an amino group (-NH2) from a molecule, especially from an amino acid. This process typically results in the formation of a new functional group and the release of ammonia (NH3). Deamination plays a crucial role in the metabolism of amino acids, as it helps to convert them into forms that can be excreted or used for energy production. In some cases, deamination can also lead to the formation of toxic byproducts, which must be efficiently eliminated from the body to prevent harm.

I'm sorry for any confusion, but "Malates" is not a recognized term in medical terminology. It's possible there may be a spelling mistake or it could be a slang term or an abbreviation that is not widely recognized. If you have more context or information, I'd be happy to try and help further.

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.

Orotic acid, also known as pyrmidine carboxylic acid, is a organic compound that plays a role in the metabolic pathway for the biosynthesis of pyrimidines, which are nitrogenous bases found in nucleotides and nucleic acids such as DNA and RNA. Orotic acid is not considered to be a vitamin, but it is sometimes referred to as vitamin B13 or B15, although these designations are not widely recognized by the scientific community.

In the body, orotic acid is converted into orotidine monophosphate (OMP) by the enzyme orotate phosphoribosyltransferase. OMP is then further metabolized to form uridine monophosphate (UMP), a pyrimidine nucleotide that is an important precursor for the synthesis of RNA and other molecules.

Elevated levels of orotic acid in the urine, known as orotic aciduria, can be a sign of certain genetic disorders that affect the metabolism of pyrimidines. These conditions can lead to an accumulation of orotic acid and other pyrimidine precursors in the body, which can cause a range of symptoms including developmental delays, neurological problems, and kidney stones. Treatment for these disorders typically involves dietary restrictions and supplementation with nucleotides or nucleosides to help support normal pyrimidine metabolism.

The Proton-Motive Force (PMF) is not a medical term per se, but it is a fundamental concept in the field of biochemistry and cellular physiology. It is primarily used to describe a key mechanism in bacterial cells and mitochondria that drives the synthesis of ATP (adenosine triphosphate), an essential energy currency for many cellular processes.

PMF is the electrochemical gradient of protons (H+ ions) across a biological membrane, such as the inner mitochondrial membrane or the bacterial cytoplasmic membrane. This gradient consists of two components:

1. A chemical component, which arises from the difference in proton concentration [H+] between the two sides of the membrane. Protons tend to move from an area of higher concentration (more acidic) to an area of lower concentration (less acidic).
2. An electrical component, which is due to the separation of charges across the membrane. The movement of protons generates a charge difference, creating an electric field that drives the flow of charged particles, such as ions.

The PMF stores energy in the form of this electrochemical gradient, and it can be harnessed by special enzymes called ATP synthases to produce ATP through a process called chemiosmosis. When protons flow back across the membrane through these enzymes, they release their stored energy, which is then used to convert ADP (adenosine diphosphate) and inorganic phosphate into ATP.

While PMF is not a medical term per se, understanding its role in cellular energy production is crucial for grasping various aspects of cell biology, bioenergetics, and related medical fields such as molecular biology, microbiology, and mitochondrial disorders.

The Citric Acid Cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, is a crucial metabolic pathway in the cell's powerhouse, the mitochondria. It plays a central role in the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins, into carbon dioxide and high-energy electrons. This process generates energy in the form of ATP (adenosine triphosphate), reducing equivalents (NADH and FADH2), and water.

The cycle begins with the condensation of acetyl-CoA with oxaloacetate, forming citrate. Through a series of enzyme-catalyzed reactions, citrate is converted back to oxaloacetate, releasing two molecules of carbon dioxide, one GTP (guanosine triphosphate), three NADH, one FADH2, and regenerating oxaloacetate to continue the cycle. The reduced coenzymes (NADH and FADH2) then donate their electrons to the electron transport chain, driving ATP synthesis through chemiosmosis. Overall, the Citric Acid Cycle is a vital part of cellular respiration, connecting various catabolic pathways and generating energy for the cell's metabolic needs.

Biotin is a water-soluble vitamin, also known as Vitamin B7 or Vitamin H. It is a cofactor for several enzymes involved in metabolism, particularly in the synthesis and breakdown of fatty acids, amino acids, and carbohydrates. Biotin plays a crucial role in maintaining healthy skin, hair, nails, nerves, and liver function. It is found in various foods such as nuts, seeds, whole grains, milk, and vegetables. Biotin deficiency is rare but can occur in people with malnutrition, alcoholism, pregnancy, or certain genetic disorders.

Phosphatidylethanolamines (PE) are a type of phospholipid that are abundantly found in the cell membranes of living organisms. They play a crucial role in maintaining the structural integrity and functionality of the cell membrane. PE contains a hydrophilic head, which consists of an ethanolamine group linked to a phosphate group, and two hydrophobic fatty acid chains. This unique structure allows PE to form a lipid bilayer, where the hydrophilic heads face outwards and interact with the aqueous environment, while the hydrophobic tails face inwards and interact with each other.

PE is also involved in various cellular processes, such as membrane trafficking, autophagy, and signal transduction. Additionally, PE can be modified by the addition of various functional groups or molecules, which can further regulate its functions and interactions within the cell. Overall, phosphatidylethanolamines are essential components of cellular membranes and play a critical role in maintaining cellular homeostasis.

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.

Oxalic acid is not a medical term, but it is a chemical compound with the formula HOOC-COOH. It is a white crystalline solid that is soluble in water and polar organic solvents. Medically, oxalic acid is relevant due to its presence in certain foods and its potential to form calcium oxalate stones in the kidneys when excreted in urine.

Hyperoxaluria is a medical condition characterized by increased levels of oxalate in the urine, which can lead to the formation of kidney stones. This condition can be caused by genetic factors or excessive intake of oxalate-rich foods such as spinach, rhubarb, and certain nuts and beans. In severe cases, it may require medical treatment to reduce oxalate levels in the body.

Oxalates, also known as oxalic acid or oxalate salts, are organic compounds that contain the functional group called oxalate. Oxalates are naturally occurring substances found in various foods such as spinach, rhubarb, nuts, and seeds. They can also be produced by the body as a result of metabolism.

In the body, oxalates can bind with calcium and other minerals to form crystals, which can accumulate in various tissues and organs, including the kidneys. This can lead to the formation of kidney stones, which are a common health problem associated with high oxalate intake or increased oxalate production in the body.

It is important for individuals with a history of kidney stones or other kidney problems to monitor their oxalate intake and limit consumption of high-oxalate foods. Additionally, certain medical conditions such as hyperoxaluria, a rare genetic disorder that causes increased oxalate production in the body, may require medical treatment to reduce oxalate levels and prevent complications.

Carbon radioisotopes are radioactive isotopes of carbon, which is an naturally occurring chemical element with the atomic number 6. The most common and stable isotope of carbon is carbon-12 (^12C), but there are also several radioactive isotopes, including carbon-11 (^11C), carbon-14 (^14C), and carbon-13 (^13C). These radioisotopes have different numbers of neutrons in their nuclei, which makes them unstable and causes them to emit radiation.

Carbon-11 has a half-life of about 20 minutes and is used in medical imaging techniques such as positron emission tomography (PET) scans. It is produced by bombarding nitrogen-14 with protons in a cyclotron.

Carbon-14, also known as radiocarbon, has a half-life of about 5730 years and is used in archaeology and geology to date organic materials. It is produced naturally in the atmosphere by cosmic rays.

Carbon-13 is stable and has a natural abundance of about 1.1% in carbon. It is not radioactive, but it can be used as a tracer in medical research and in the study of metabolic processes.

"Zymomonas" is a genus of Gram-negative, facultatively anaerobic bacteria that are commonly found in sugar-rich environments such as fruit and flower nectar. The most well-known species in this genus is Zymomonas mobilis, which has attracted significant interest in the field of biofuels research due to its ability to efficiently ferment sugars into ethanol.

Zymomonas bacteria are unique in their metabolism and possess a number of unusual features, including a highly streamlined genome, a single polar flagellum for motility, and the ability to survive and grow at relatively high temperatures and ethanol concentrations. These characteristics make Zymomonas an attractive candidate for industrial applications, particularly in the production of biofuels and other bioproducts.

In addition to their potential industrial uses, Zymomonas bacteria have also been implicated in certain human diseases, particularly in individuals with weakened immune systems or underlying medical conditions. However, such cases are relatively rare, and the overall impact of Zymomonas on human health is still not well understood.

Isocitrate Dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate to α-ketoglutarate in the presence of NAD+ or NADP+, producing NADH or NADPH respectively. This reaction occurs in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, which is a crucial metabolic pathway in the cell's energy production and biosynthesis of various molecules. There are three isoforms of IDH found in humans: IDH1 located in the cytosol, IDH2 in the mitochondrial matrix, and IDH3 within the mitochondria. Mutations in IDH1 and IDH2 have been associated with several types of cancer, such as gliomas and acute myeloid leukemia (AML), leading to abnormal accumulation of 2-hydroxyglutarate, which can contribute to tumorigenesis.

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.

Pyrogallol is not typically considered a medical term, but it does have relevance to the field of pathology as a chemical reagent. Pyrogallol is an organic compound with the formula C6H3(OH)3. It is a type of phenol and can be used in histological stains to demonstrate the presence of certain enzymes or structures within tissue samples.

In a medical context, pyrogallol may be mentioned in pathology reports related to the use of this chemical in laboratory tests. However, it is not a condition or disease entity itself.

Thiamine, also known as vitamin B1, is a water-soluble vitamin that plays a crucial role in certain metabolic reactions, particularly in the conversion of carbohydrates into energy in the body. It is essential for the proper functioning of the heart, nerves, and digestive system. Thiamine acts as a cofactor for enzymes involved in the synthesis of neurotransmitters and the metabolism of carbohydrates, lipids, and proteins. Deficiency in thiamine can lead to serious health complications, such as beriberi (a disease characterized by peripheral neuropathy, muscle wasting, and heart failure) and Wernicke-Korsakoff syndrome (a neurological disorder often seen in alcoholics due to chronic thiamine deficiency). Thiamine is found in various foods, including whole grains, legumes, pork, beef, and fortified foods.

Uroporphyrins are porphyrin derivatives that contain four carboxylic acid groups. They are intermediates in the biosynthesis of heme, which is a component of hemoglobin and other hemoproteins. Uroporphyrinogen I and III are precursors to uroporphyrin I and III, respectively, through the action of uroporphyrinogen decarboxylase.

Uroporphyrin I and III differ in the position of acetate and propionate side chains on the porphyrin ring. Uroporphyrins are usually elevated in the urine of patients with certain inherited metabolic disorders, such as acute intermittent porphyria, variegate porphyria, and hereditary coproporphyria, due to enzyme deficiencies in the heme biosynthetic pathway.

The measurement of uroporphyrins in urine or other body fluids can be helpful in diagnosing and monitoring these disorders.

Hereditary coproporphyria (HCP) is a rare inherited disorder of the heme biosynthesis pathway, which is the process by which your body produces heme. Heme is a crucial component of various proteins, including hemoglobin, which carries oxygen in red blood cells.

In HCP, there is a deficiency of an enzyme called coproporphyrinogen oxidase. This enzyme is essential for converting coproporphyrinogen III to protoporphyrin IX in the heme biosynthesis pathway. As a result, coproporphyrinogen III accumulates and gets converted to coproporphyrin, which is excreted in urine and stool in abnormally high amounts.

The symptoms of HCP can be diverse and may include both neurological and gastrointestinal manifestations. Neurological symptoms might include abdominal pain, muscle weakness, numbness, tingling, seizures, and psychiatric disturbances. Gastrointestinal symptoms could encompass nausea, vomiting, constipation, or diarrhea. These symptoms are typically triggered by certain factors such as infections, drugs, hormonal changes, or alcohol consumption.

HCP is usually inherited in an autosomal dominant manner, meaning that a child has a 50% chance of inheriting the disease-causing gene from a parent with the disorder. However, some cases may result from de novo mutations, which means the mutation occurs spontaneously without a family history of the condition.

Diagnosis of HCP is usually made through measuring porphyrin levels and their precursors in urine, stool, and blood during an acute attack or between attacks. Genetic testing can confirm the diagnosis by identifying mutations in the CPOX gene, which encodes coproporphyrinogen oxidase.

Treatment for HCP typically involves avoiding triggers, providing supportive care during acute attacks, and using medications to manage symptoms. In some cases, heme arginate or hemine may be given to help decrease porphyrin precursor production. Preventive measures such as avoidance of potential triggers, adequate hydration, and a balanced diet are essential in managing HCP.

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.

Glutaryl-CoA Dehydrogenase (GCDH) is an enzyme that plays a crucial role in the catabolism of the amino acids lysine and hydroxylysine. It is located in the inner mitochondrial membrane and functions as a homotetramer, with each subunit containing one molecule of FAD as a cofactor.

GCDH catalyzes the oxidative decarboxylation of glutaryl-CoA to form succinyl-CoA, which is then further metabolized in the citric acid cycle. This reaction also involves the reduction of FAD to FADH2, which can subsequently be used in the electron transport chain to generate ATP.

Deficiency in GCDH function can lead to a rare inherited disorder called glutaric acidemia type I (GA-I), which is characterized by an accumulation of glutaryl-CoA and its metabolites, including glutaric acid and 3-hydroxyglutaric acid. These metabolites can cause neurological damage and intellectual disability if left untreated.

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.

Tyramine is not a medical condition but a naturally occurring compound called a biogenic amine, which is formed from the amino acid tyrosine during the fermentation or decay of certain foods. Medically, tyramine is significant because it can interact with certain medications, particularly monoamine oxidase inhibitors (MAOIs), used to treat depression and other conditions.

The interaction between tyramine and MAOIs can lead to a hypertensive crisis, a rapid and severe increase in blood pressure, which can be life-threatening if not treated promptly. Therefore, individuals taking MAOIs are often advised to follow a low-tyramine diet, avoiding foods high in tyramine, such as aged cheeses, cured meats, fermented foods, and some types of beer and wine.

The Glycine Decarboxylase Complex (GDC) is a multienzyme complex that plays a crucial role in the metabolism of glycine, an amino acid. This complex is composed of four main proteins: P-, H-, T- and L-protein. The H-protein, also known as the H protein of the glycine decarboxylase complex or GLDC, is a pyridoxal phosphate (PLP)-dependent enzyme that catalyzes the first step in the glycine cleavage system (GCS).

The GCS is responsible for the oxidative cleavage of glycine to form ammonia, carbon dioxide, and a methyl group, which is then transferred to tetrahydrofolate. The H-protein functions as a dehydrogenase in this process, facilitating the conversion of glycine to aminoacetic acid (also known as β-alanine) and liberating a molecule of CO2.

In summary, Glycine Decarboxylase Complex H-Protein is a key enzyme in the Glycine Decarboxylase Complex that facilitates the oxidative cleavage of glycine, an essential amino acid metabolism pathway.

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.

Droxidopa is a medication that is used to treat neurogenic orthostatic hypotension, which is a condition characterized by a drop in blood pressure when standing up from a seated or lying down position. Droxidopa works by helping the body to maintain normal levels of norepinephrine, a hormone and neurotransmitter that helps to regulate blood pressure.

Droxidopa is a synthetic precursor of norepinephrine, which means that it is converted into norepinephrine in the body. By increasing the availability of norepinephrine, droxidopa helps to constrict blood vessels and increase blood pressure, reducing symptoms of orthostatic hypotension such as dizziness, lightheadedness, and fainting.

Droxidopa is available in capsule form and is typically taken three times a day with food. It may take several weeks of treatment before the full benefits of droxidopa are seen. Common side effects of droxidopa include headache, dizziness, and fatigue.

Glyoxylates are organic compounds that are intermediates in various metabolic pathways, including the glyoxylate cycle. The glyoxylate cycle is a modified version of the Krebs cycle (also known as the citric acid cycle) and is found in plants, bacteria, and some fungi.

Glyoxylates are formed from the breakdown of certain amino acids or from the oxidation of one-carbon units. They can be converted into glycine, an important amino acid involved in various metabolic processes. In the glyoxylate cycle, glyoxylates are combined with acetyl-CoA to form malate and succinate, which can then be used to synthesize glucose or other organic compounds.

Abnormal accumulation of glyoxylates in the body can lead to the formation of calcium oxalate crystals, which can cause kidney stones and other health problems. Certain genetic disorders, such as primary hyperoxaluria, can result in overproduction of glyoxylates and increased risk of kidney stone formation.

'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.

Ornithine decarboxylase (ODC) is a medical/biochemical term that refers to an enzyme (EC 4.1.1.17) involved in the metabolism of amino acids, particularly ornithine. This enzyme catalyzes the decarboxylation of ornithine to form putrescine, which is a precursor for the synthesis of polyamines, such as spermidine and spermine. Polyamines play crucial roles in various cellular processes, including cell growth, differentiation, and gene expression.

Ornithine decarboxylase is a rate-limiting enzyme in polyamine biosynthesis, meaning that its activity regulates the overall production of these molecules. The regulation of ODC activity is tightly controlled at multiple levels, including transcription, translation, and post-translational modifications. Dysregulation of ODC activity has been implicated in several pathological conditions, such as cancer, neurodegenerative disorders, and inflammatory diseases.

Inhibitors of ornithine decarboxylase have been explored as potential therapeutic agents for various diseases, including cancer, due to their ability to suppress polyamine synthesis and cell proliferation. However, the use of ODC inhibitors in clinical settings has faced challenges related to toxicity and limited efficacy.

I believe there may be a slight spelling error in your question. If you are referring to "isocitrate," I can provide a medical definition for that. Isocitrate is a chemical compound that is naturally found in the body and plays a crucial role in energy production within cells. It is a key intermediate in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, which is a series of chemical reactions used by all living cells to generate energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins into adenosine triphosphate (ATP).

Isocitrate is an important molecule in this cycle as it undergoes oxidative decarboxylation, catalyzed by the enzyme isocitrate dehydrogenase, to form alpha-ketoglutarate. This reaction also produces nicotinamide adenine dinucleotide (NADH), which serves as an essential electron carrier in the generation of ATP during oxidative phosphorylation.

If you meant something else or need more information, please let me know, and I will be happy to help.

The Krapcho decarboxylation is a related decarboxylation of an ester. The Tsuji-Trost reaction involves the intermediacy of an ... Decarboxylations are the bases of many named reactions. These include Barton decarboxylation, Kolbe electrolysis, Kochi ... The decarboxylation can be depicted as such: RC ( O ) CO 2 Fe II + O 2 ⟶ RCO 2 Fe IV = O + CO 2 {\displaystyle {\ce {RC(O)CO2Fe ... However, modelling of decarboxylation of salicylic acid with a water molecule had suggested an activation barrier of 150 kJ/mol ...
... at organic-chemistry.org [1] Barton decarboxylation at themerckindex.cambridgesoft.com [2][permanent ... The Barton decarboxylation is a radical reaction in which a carboxylic acid is converted to a thiohydroxamate ester (commonly ... This is an example of a reductive decarboxylation. Using this reaction it is possible to remove carboxylic acid moieties from ... The N-O bond of the thiohydroxamate ester undergoes homolysis to form a carboxyl radical which then undergoes decarboxylation ...
The Krapcho decarboxylation is a useful way to manipulate malonic esters because it cleaves only one of the two ester groups. ... The Krapcho decarboxylation is the chemical reaction of esters with halide anions. The ester must contain an electron- ... The apparent alternative, base hydrolysis followed by decarboxylation, requires a subsequent step to regenerate the ester. ...
The Adams decarboxylation is a chemical reaction that involved the decarboxylation of coumarins which have carboxylic acid ... The decarboxylation is achieved by aqueous solution of sodium bisulfite, heat and a concentrated solution of sodium hydroxide. ...
... or pyruvate oxidation, also known as the link reaction, Swanson Conversion, or oxidative ... The pyruvate dehydrogenase complex (PDC) catalyzes the decarboxylation of pyruvate, resulting in the synthesis of acetyl-CoA, ... cite web}}: Check ,url= value (help) "Oxidative decarboxylation of Pyruvate". Bioscience Notes. 2018-07-29. Retrieved 2021-07- ... decarboxylation of pyruvate, is the conversion of pyruvate into acetyl-CoA by the enzyme complex pyruvate dehydrogenase complex ...
... namely oxidative decarboxylation, which is different from the common decarboxylation reaction, namely common decarboxylation. ... Decarboxylation in metabolism can be either non-oxidative or oxidative. In contrast to the relatively facile decarboxylation of ... Oxidative decarboxylation is a decarboxylation reaction caused by oxidation. Most are accompanied by α- Ketoglutarate α- ... To sum up, in the oxidative decarboxylation reaction, there is both an oxidation reaction and a decarboxylation. For simple ...
... of propanoic acid over a manganese(II) oxide catalyst in a tube furnace affords 3-pentanone. Of ... The initial formation of an intermediate carbanion via decarboxylation of one of the acid groups prior to the nucleophilic ... In organic chemistry, ketonic decarboxylation (also known as decarboxylative ketonization) is a type of organic reaction and a ... This reaction is different from oxidative decarboxylation, which proceeds through a radical mechanism and is characterised by a ...
Decarboxylation gives skatole. The perceived bad odor of feces has been hypothesized to be a deterrent for humans, as consuming ...
Decarboxylation gives indole. Baeyer-Drewson indigo synthesis Bayer, A.; Emmerling, A. (1869). "Synthese des indoles" [ ...
This decarboxylation gives putrescine. Thereafter the enzyme spermidine synthase effects two N-alkylation by decarboxy-S- ... Another pathway in plants starts with decarboxylation of L-arginine to produce agmatine. The imine functional group in agmatine ... Spermine biosynthesis in animals starts with decarboxylation of ornithine by the enzyme Ornithine decarboxylase in the presence ...
Decarboxylation of Salicylic Acids". The Journal of Organic Chemistry. 29 (9): 2556-2559. doi:10.1021/jo01032a016. Dioscorides ...
Decarboxylation gives the methylindole. Chemically, it can be synthesized by the reaction of indole with glycolic acid in the ...
Decarboxylation of Salicylic Acids". The Journal of Organic Chemistry. 29 (9): 2556-2559. doi:10.1021/jo01032a016. "Phenol ...
"BRENDA - Information on EC 4.1.1.9 - malonyl-CoA decarboxylase". Hayaishi O (Jul 1955). "Enzymatic decarboxylation of malonic ...
McCullough WG, Piligian JT, Daniel IJ (1957). "Enzymatic decarboxylation of three aminobenzoates". J. Am. Chem. Soc. 79 (3): ...
Krampitz, Lester Orville; Werkman, Chester Hamlin (1941). "The enzymic decarboxylation of oxaloacetate". Biochemical Journal. ...
Decarboxylation of glycin gives metol. Glycin has a milder reduction potential than metol. The two developers have markedly ...
The mechanism of decarboxylation. Part II. The production of cyanide-like ions from α-picolinic, quinaldinic, and ... The Hammick reaction, named after Dalziel Hammick, is a chemical reaction in which the thermal decarboxylation of α-picolinic ( ... Experiments on the mechanism of decarboxylation. Part I. Decomposition of quinaldinic and isoquinaldinic acids in the presence ...
Decarboxylation "Carboxylation: The introduction of a carboxyl group into a molecule or compound to form a carboxylic acid or a ... The opposite reaction is decarboxylation. In chemistry, the term carbonation is sometimes used synonymously with carboxylation ...
In ketonic decarboxylation carboxylic acids are converted to ketones. Organolithium reagents (>2 equiv) react with carboxylic ... Many acids undergo oxidative decarboxylation. Enzymes that catalyze these reactions are known as carboxylases (EC 6.4.1) and ...
Hayaishi O (July 1955). "Enzymatic decarboxylation of malonic acid". The Journal of Biological Chemistry. 215 (1): 125-36. PMID ...
"A novel decarboxylation of .ALPHA.-amino acids. A facile method of decarboxylation by the use of 2-cyclohexen-1-one as a ... Researchers in Japan were attempting to use t-butyl peroxide as a catalyst for decarboxylation using a solvent choice of ... Laval, G; Golding, B (2003). "One-pot Sequence for the Decarboxylation of α-Amino Acids". Synlett (4): 542-546. doi:10.1055/s- ... Cyclohexenone is an in-vitro catalyst for a relatively mild decarboxylation of alpha amino acids. cyclopropenone cyclobutenone ...
In ketonic decarboxylation symmetrical ketones are prepared from carboxylic acids. Oxidation of amines with iron(III) chloride ... By decarboxylation of carboxylic anhydride. Ketones can be prepared from haloketones in reductive dehalogenation of halo ...
HAYAISHI O, JAKOBY WB, OHMURA E (1956). "Enzymatic decarboxylation of oxalic acid". J. Biol. Chem. 222 (1): 435-46. PMID ...
Janssen, Peter H.; Liesack, Werner (1995). "Succinate decarboxylation by Propionigenium maris sp. nov., a new anaerobic ... Hilpert, Wilhelm; Schink, Bernhard; Dimroth, Peter (1984). "Life by a new decarboxylation-dependent energy conservation ...
Decarboxylation leads to tropane alkaloid formation. The reduction of tropinone is mediated by NADPH-dependent reductase ... Ornithine then undergoes a pyridoxal phosphate-dependent decarboxylation to form putrescine. In some animals, the urea cycle ...
Origins and catalytic nature of the solvent rate acceleration for the decarboxylation of 3-carboxybenzisoxazoles". Journal of ... Kemp, Daniel S. (April 1970). "Decarboxylation of benzisoxazole-3-carboxylic acids. Catalysis by extraction of possible ...
The follow-up is a decarboxylation. With palladium(0) as a catalyst, the reaction (Tsuji, 1980) is much milder (path B) with an ... Decarboxylation precedes allylation as evidenced by this reaction catalyzed by tetrakis(triphenylphosphine)palladium(0): By ... This organic reaction is accompanied by decarboxylation and the final product is a γ,δ-allylketone. The Carroll rearrangement ...
The lactone undergoes decarboxylation to acetylacetone. It is also a precursor to sorbic acid, dienoic acid, and hexenoic acid ...
Unique features of the glycine decarboxylation". Mol. Cell. Biochem. 45 (3): 137-49. doi:10.1007/bf00230082. PMID 6750353. ... which catalyzes the decarboxylation of glycine and attaches the intermediate molecule to the H-protein to be shuttled to the T- ... with the three other proteins and acts as a shuttle for some of the intermediate products in glycine decarboxylation. In both ...
The Krapcho decarboxylation is a related decarboxylation of an ester. The Tsuji-Trost reaction involves the intermediacy of an ... Decarboxylations are the bases of many named reactions. These include Barton decarboxylation, Kolbe electrolysis, Kochi ... The decarboxylation can be depicted as such: RC ( O ) CO 2 Fe II + O 2 ⟶ RCO 2 Fe IV = O + CO 2 {\displaystyle {\ce {RC(O)CO2Fe ... However, modelling of decarboxylation of salicylic acid with a water molecule had suggested an activation barrier of 150 kJ/mol ...
The decarboxylation can be depicted as such: RC. (. O. ). CO. 2. Fe. II. +. O. 2. ⟶. RCO. 2. Fe. IV. =. O. +. CO. 2. {\ ... Decarboxylation of amino acids Edit Common biosynthetic oxidative decarboxylations of amino acids to amines are: *tryptophan to ... Decarboxylation, Dr. Ian A. Hunt, Department of Chemistry, University of Calgary *^ Jim Clark (2004). "The Decarboxylation of ... Named decarboxylation reactions Edit Decarboxylations are the bases of many named reactions. These include Barton ...
In a Cu-catalyzed degree-controlled deacylative deuteration of diverse alkyl groups, the methylketone (acetyl) moiety acts as a traceless activating group. The use of N-methylpicolino-hydrazonamide (MPHA) promotes efficient aromatization-driven C-C cleavage. Mono-, di-, and trideuteration at specific sites can be selectively achieved ...
... of the Chinese Academy of Sciences have reported that photocatalytic decarboxylation is an efficient alternate pathway for ... Chinese team uses light to convert fatty acids into alkanes with up to 95% yield; photocatalytic decarboxylation 24 February ... Huang, Z., Zhao, Z., Zhang, C. et al. (2020) "Enhanced photocatalytic alkane production from fatty acid decarboxylation via ... The researchers found that under illumination, the decarboxylation of fatty acids could be easily induced by photo-generated ...
Kinetic isotope effects in the decarboxylation of oxaloacetic acid were studied at 25° in aqueous solution for the acid alone, ... Wood, Alexander (1961) Carbon Isotope Effects in the Decarboxylation of Oxaloacetic Acid. PhD thesis, University of Glasgow. ...
Ketonic decarboxylation has gained significant attention in recent years as a pathway to reduce the oxygen content within ... Heterogeneous ketonic decarboxylation of dodecanoic acid: studying reaction parameters Perera-Solis, Diego D.; Zholobenko, ... Here we use MgO to catalyse the ketonic decarboxylation of dodecanoic acid to form 12-tricosanone at moderate temperatures (250 ... Perera-Solis, D. D., Zholobenko, V. L., Whiting, A., & Greenwell, H. C. (2021). Heterogeneous ketonic decarboxylation of ...
Decarboxylation is the removal or loss of a carboxyl group from an organic compound. During the reaction carbon dioxide (CO2) ...
The word decarboxylation may sound like a highly scientific one, and you may even be intimidated by the process. Learn How to ... Decarboxylation Guide. Posted on January 06 2023. The word decarboxylation may sound like a highly scientific one, and you may ... What Does Decarboxylation Achieve?. Before consuming any type of herbs, they will need to undergo the process of ... Now that you are ready to begin the process of decarboxylation, follow the steps below to get started:. *Preheat your oven to ...
What is decarboxylation? What needs to be considered and what are the advantages of the process? ▷ This is how cannabis has the ... 2 What is decarboxylation?. 2.1 What is involved in decarboxylation?. 2.2 Advantages of decarboxylation. 3 Decarboxylation of ... What is decarboxylation?. Decarboxylation (or oxidative decarboxylation) is a chemical process that occurs naturally when the ... Decarboxylation of cannabidiol (CBD). In connection with cannabinoids from the cannabis plant, the term decarboxylation or ...
... Catalog No: PI00020002 Product Name: Ceftizoxime Open-ring decarboxylation ...
Decarboxylation Factors. There are several factors that can influence the rate of decarboxylation, including temperature, ... WEED HEAT: THCa & Decarboxylation Recap. In conclusion, heat plays a crucial role in the conversion of THCA to THC in cannabis. ... Decarboxylation occurs when THCa is heated, and it is what allows THC to interact with the bodys endocannabinoid system and ... Decarboxylation is an important process for those who consume cannabis in order to experience the psychoactive effects of THC. ...
What is decarboxylation?. Ive heard about decarboxylation when it comes to preparing cannabis for consumption. What exactly ... Decarboxylation is a chemical reaction that removes a carboxyl group and releases carbon dioxide (CO2). It is an essential step ... To summarize, decarboxylation is an essential step when preparing cannabis for consumption. Heat is applied to raw cannabis to ...
Step 1: Decarboxylation. Its important to bake cannabis before making cannabutter. In its raw form, it contains ... By heating these compounds, they undergo decarboxylation - also known as decarbing - and become the active compounds THC and ...
Decarboxylation of cannabis in a jar is one of the best decarboxylation methods because it helps preserve the cannabis terpenes ... How to decarboxylation cannabis ?. Decarboxylation is a process that actives the psychoactive compounds in the cannabis plant ... How to decarboxylation cannabis. *What is decarboxylation and why is it needed? ... The final explanation of decarboxylation. Although the decarboxylation process may seem daunting at first, it is actually very ...
The external digital display lets you monitor the temperature inside your DecarBox™ during decarboxylation without opening the ...
... and how of cannabis decarboxylation to make delicious edibles and more at home. ... Decarboxylation can easily be done in your kitchen at home by baking the dried cannabis in the oven at a low temperature for a ... Decarboxylation is the first step you need to take before infusing cannabis into oil, butter, tinctures, edibles, topicals, and ... Yes - the decarboxylation process can cause your house to smell like weed. This is because, when we bake cannabis, we activate ...
They simply add their solventless Rosin to the Rosin POT and enclose the POT in the Decarboxylation Capsule, then add to your ... Nug Smashers answer to easy and fast decarboxylation! Meant to be used with all of the NugSmasher® line of Machines. ... Decrease quantity for NugSmasher Decarboxylation Capsules (Mini & Large) Increase quantity for NugSmasher Decarboxylation ... The Decarboxylation Capsule is made to seal under pressure in your NugSmasher and needs to cool down completely prior to ...
Here we will explain all about decarboxylation and how you can perform decarboxylation in your own kitchen in as little as 30 ... Conditions Necessary for Decarboxylation. The two major components which are required in order for decarboxylation to take ... The process of decarboxylation is one which confuses many who are new to the cannabis industry, or may not have put a whole lot ... The Basics of Decarboxylation. In its raw plant form, all of the cannabinoids which are present in the cannabis plant possess ...
This is a list of changes made recently to pages linked from a specified page (or to members of a specified category). Pages on your watchlist are bold. ...
By understanding and implementing the basics of decarboxylation, we can maximize the quality and efficacy of the distillation ... The Basics of Crude Cannabis Decarboxylation for Distillation. Introduction:. Decarboxylation is a crucial step to obtaining ... Understanding Decarboxylation:. The decarboxylation process removes carboxyl groups from cannabinoids and terpenes, converting ... Once the desired decarboxylation level is reached, remove the heat source and let the container cool naturally. Cooling down ...
The Global Hemp Biomass Decarboxylation System Market is anticipated to grow at a modest rate over the forecast period on ... 8.1 Hemp Biomass Decarboxylation System Segmentation Market Forecast (Region Level). 8.2 Hemp Biomass Decarboxylation System ... 8.3 Hemp Biomass Decarboxylation System Segmentation Market Forecast (Industry Level). 8.4 Hemp Biomass Decarboxylation System ... What are the major applications for Global Hemp Biomass Decarboxylation System? Global Hemp Biomass Decarboxylation System has ...
Decarboxylation ... What Is It Exactly? Why Is It Important? How to Tell If A CBD Product I Bought Has Been Decarbed? See the ... "Most hemp CBD products offered on the market have undergone decarboxylation." "Decarboxylation can be both a natural, slow ... Decarboxylation in Biochemistry. Aside from cannabis, this process has a range of applications in biochemistry. Decarboxylation ... Decarboxylation. de-kärb-ˈbäk-sə-ˌlāSH(ə)n , Noun. A chemical reaction that uses heat to activate the compounds in cannabis, ...
Decarboxylation chart. As with any other chemical process, there are certain things that need to happen in order for chemical ... This is called a decarboxylation chart and it allows you to see how you can reach the desired THC by baking the buds on a ... Through decarboxylation, were essentially applying heat to plant material so that the THCA gets converted to THC, enabling us ... Decarboxylation temperature chart. Use this chart to decarboxylate kief, hash, oil and high THC/CBD flowers. ...
pH Dependent Kinetics of the Decarboxylation of Pyruvate for pH Mapping Experiments. Nicholas Drachman1, Stephen J. Kadlecek1, ...
Influence of decarboxylation on Cannabis sativas antioxidant activity and flavonoid profile: A preliminary study Authors. * ... Our aim was to determine the effect of the decarboxylation on C. sativa´s resin (CSR) antioxidant effect and its relationship ... The decarboxylation process modified the HPLC flavonoids profile and increased the resins antioxidant activities. The EC50 of ... Saint Martin, M. ., Marrassini, C., Peralta, I., Cogoi, L., Alonso, M. R., & Anesini, C. . (2023). Influence of decarboxylation ...
Study of the mechanism of oxidative decarboxylation of [alpha]-hydroxy acids by bromine water Pink, Judith Margaret Osyany ... A kinetic study of the mechanism of oxidative decarboxylation of α-hydroxy acids by bromine water throughout the pH range ... A kinetic study of the mechanism of oxidative decarboxylation of α-hydroxy acids by bromine water throughout the pH range ... Results are also presented of: 1) A preliminary investigation of oxidative decarboxylation of α-amino acids by bromine water. 2 ...
What the Ding-Dong Is Decarboxylation? By TY Staff 4 years ago ... by Old Hippie BeyondChronic.com Decarboxylation: Why you never ...
Enantioselective decarboxylation of 2-methyl-2-aminomalonate catalyzed by (S)-2-hydroxy-2′-(3-phenyluryl-benzyl)-1,1′- ... Enantioselective decarboxylation of 2-methyl-2-aminomalonate catalyzed by (S)-2-hydroxy-2′-(3-phenyluryl-benzyl)-1,1′- ...
Dive into the research topics of Pd(II)-Catalyzed Direct ortho-C-H Acylation of Aromatic Ketones by Oxidative Decarboxylation ... Pd(II)-Catalyzed Direct ortho-C-H Acylation of Aromatic Ketones by Oxidative Decarboxylation of α-Oxocarboxylic Acids. ...
  • In connection with cannabinoids from the cannabis plant, the term decarboxylation or oxidative decarboxylation is often mentioned. (alpinols.com)
  • Prior to the process of decarboxylation, THCA is what we see present in the highest form as far as cannabinoids are concerned. (grasschief.cc)
  • This process is effectively what decides there level of potency in terms of THC, although all cannabinoids within the plant have an extra carboxyl element which can be altered by decarboxylation. (grasschief.cc)
  • By activating the cannabinoids and terpenes in crude cannabis extracts, decarboxylation allows for their efficient separation and concentration during the distillation process. (timelessvapes.com)
  • The decarboxylation process removes carboxyl groups from cannabinoids and terpenes, converting them from their inactive acidic forms (e.g. (timelessvapes.com)
  • Decarboxylation is essential before distillation because it allows us to unlock the therapeutic and psychoactive properties of cannabinoids, making them readily available for use. (timelessvapes.com)
  • It is known that decarboxylation transforms acid cannabinoids into their neutral, usually more active, forms. (ms-editions.cl)
  • Our aim was to determine the effect of the decarboxylation on C. sativa ´s resin (CSR) antioxidant effect and its relationship with cannabinoids and polyphenolic compounds. (ms-editions.cl)
  • Decarboxylation (or oxidative decarboxylation) is a chemical process that occurs naturally when the plant material is exposed to the sun and air without protection. (alpinols.com)
  • Study of the mechanism of oxidative decarboxylation. (ubc.ca)
  • A kinetic study of the mechanism of oxidative decarboxylation of α-hydroxy acids by bromine water throughout the pH range revealed two distinct reactions paths. (ubc.ca)
  • Results are also presented of: 1) A preliminary investigation of oxidative decarboxylation of α-amino acids by bromine water. (ubc.ca)
  • When cannabis is heated in vacuum, the decarboxylation of tetrahydrocannabinolic acid (THCA) appears to follow first order kinetics. (wikipedia.org)
  • In general, higher temperatures and longer heating times will lead to a more complete decarboxylation of THCa. (avldispensary.com)
  • However, decarboxylation is also important for those interested in the potential therapeutic effects of THCa, as it has a number of potential health benefits on its own. (avldispensary.com)
  • Without decarboxylation, the high we achieve will be minimal at best, although there are still many benefits to be obtained from the likes of THCA. (grasschief.cc)
  • Through decarboxylation, we're essentially applying heat to plant material so that the THCA gets converted to THC, enabling us to get high. (vancityherbs.ca)
  • THC results from the decarboxylation of THCA when exposed to light and heat. (cfah.org)
  • Researchers led by Prof. WANG Feng at the Dalian Institute of Chemical Physics (DICP) of the Chinese Academy of Sciences have reported that photocatalytic decarboxylation is an efficient alternate pathway for converting biomass-derived fatty acids into alkanes under mild conditions of ambient temperature and pressure. (greencarcongress.com)
  • Regardless of which method of decarboxylation you opt for, keep in mind that you should avoid baking it for too long or at too high a temperature. (ongrok.com)
  • There are several factors that can influence the rate of decarboxylation, including temperature, humidity, and duration of heating. (avldispensary.com)
  • The ideal temperature for decarboxylation starts at 250 °F (121.1 °C), and your flowers need about 30 to 45 minutes for the decarboxylation to work. (nukaseeds.com)
  • The external digital display lets you monitor the temperature inside your DecarBox™ during decarboxylation without opening the oven, keeping temperatures from fluctuating. (magicalbutter.eu)
  • Decarboxylation can easily be done in your kitchen at home by baking the dried cannabis in the oven at a low temperature for a certain period of time. (emilykylenutrition.com)
  • The entire process may seem somewhat scientific and intimidating, in reality though, decarboxylation, dialed down to the basics beyond its name, is simply heating your flower to a certain temperature, over a period of time, which allows its full potential to be utilized in different ways. (grasschief.cc)
  • Control the heating process by setting the temperature within the desired range, typically around 220-240°F (105-115°C). This temperature range is optimal for decarboxylation without risking excessive degradation of the compounds. (timelessvapes.com)
  • Regularly monitor the temperature during decarboxylation to ensure it stays within the desired range. (timelessvapes.com)
  • Also, the lower the temperature, the longer the decarboxylation process will take. (mrhempflower.com)
  • This is called a decarboxylation chart and it allows you to see how you can reach the desired THC by baking the buds on a specific temperature for a set period of time. (vancityherbs.ca)
  • Decarboxylation temperature is probably the most important factor when decarbing different types of material. (vancityherbs.ca)
  • In ketonic decarboxylation a carboxylic acid is converted to a ketone. (wikipedia.org)
  • Ketonic decarboxylation has gained significant attention in recent years as a pathway to reduce the oxygen content within biomass-derived oils, and to produce sustainable ketones. (worktribe.com)
  • Here we use MgO to catalyse the ketonic decarboxylation of dodecanoic acid to form 12-tricosanone at moderate temperatures (250 °C, 280 °C and 300 °C) with low catalyst loads of 1% (w/w), 3% (w/w) and 5% (w/w) with respect to the dodecanoic acid, with a reaction time of 1 hour under batch conditions. (worktribe.com)
  • Decarboxylation is a chemical reaction that removes a carboxyl group and releases carbon dioxide (CO2). (wikipedia.org)
  • This is conceptually the same as the more general term "decarboxylation" as defined above except that it specifically requires that the carboxyl group is, as expected, replaced by a hydrogen. (wikipedia.org)
  • Decarboxylation is the removal or loss of a carboxyl group from an organic compound. (buchler-gmbh.com)
  • This extra carboxyl group gets removed in the process of decarboxylation due to the effect heat has on their chemical structure. (vancityherbs.ca)
  • Depending on how much cannabis you decarboxylate at once, the full decarboxylation process may take longer. (nukaseeds.com)
  • 2020) "Enhanced photocatalytic alkane production from fatty acid decarboxylation via inhibition of radical oligomerization. (greencarcongress.com)
  • Kinetic isotope effects in the decarboxylation of oxaloacetic acid were studied at 25° in aqueous solution for the acid alone, and then in turn in the presence of the cations of the rare earth metals: yttrium, dysprosium and gadolinium, which act as catalysts through complex formation. (gla.ac.uk)
  • Based on our results, we predict the following scenario: decarboxylation preferentially removes 12 C α -carbon (i.e., carbonyl-carbon) from pyruvic acid in glycolysis, and from α -ketoglutaric acid in the tricarboxylic acid cycle, leaving behind the 13 C-enriched both pyruvic and α -ketoglutaric acids. (springeropen.com)
  • Carbidopa, an inhibitor of aromatic amino acid decarboxylation, is a white, crystalline compound, slightly soluble in water, with a molecular weight of 244.3. (nih.gov)
  • is a non-psychoactive component that can only be activated to THC after raw hemp has undergone decarboxylation. (nukaseeds.com)
  • With tables and figures helping analyze worldwide Global Hemp Biomass Decarboxylation System market, this research provides key statistics on the state of the industry and is a valuable source of guidance and direction for companies and individuals interested in the market. (amplemarketreports.com)
  • Enzymes that catalyze decarboxylations are called decarboxylases or, the more formal term, carboxy-lyases (EC number 4.1.1). (wikipedia.org)
  • By heating these compounds, they undergo decarboxylation - also known as decarbing - and become the active compounds THC and CBD ( 2 , 8 ). (healthline.com)
  • Decarboxylation is a process that actives the psychoactive compounds in the cannabis plant so that you feel high when you consume it. (nukaseeds.com)
  • Decarboxylation is a crucial step to obtaining highly refined compounds through distillation. (timelessvapes.com)
  • RC(O)CH(OH)R'}}} Pyridoxal phosphate promotes decarboxylation of amino acids. (wikipedia.org)
  • Pyridoxal phosphate promotes decarboxylation of amino acids. (wikipedia.org)
  • Decarboxylation of aryl carboxylates can generate the equivalent of the corresponding aryl anion, which in turn can undergo cross coupling reactions. (wikipedia.org)
  • Before consuming any type of herbs, they will need to undergo the process of decarboxylation to make them edible. (ongrok.com)
  • HIV-1 protease), pyridoxal phosphate-catalyzed alpha decarboxylation, and acetolactate synthase. (umass.edu)
  • The word decarboxylation may sound like a highly scientific one, and you may even be intimidated by the process. (ongrok.com)
  • In this guide, we share with you more about the process of decarboxylation. (ongrok.com)
  • While it is up to you to take the additional step of grinding your herbs, it is not necessary to do so before the decarboxylation process - at the end of the day, it all boils down to personal preferences. (ongrok.com)
  • This process is known as decarboxylation, and it is what allows THC to interact with the body's endocannabinoid system and produce the psychoactive effects that are associated with consuming cannabis. (avldispensary.com)
  • Decarboxylation is an important process for those who consume cannabis in order to experience the psychoactive effects of THC. (avldispensary.com)
  • Decarboxylation is the process that must take place for the psychoactive components of cannabis to become active and produce effects. (nukaseeds.com)
  • The process of decarboxylation is one which confuses many who are new to the cannabis industry, or may not have put a whole lot of thought into how their edibles became infused with psychoactive properties. (grasschief.cc)
  • Here we will explain more about the process, how it is not as intimidating as it seems, and how you can perform decarboxylation in your own kitchen in as little as 30 minutes. (grasschief.cc)
  • Where we see the notable need for, and difference from pre to post decarboxylation is when we consume edibles, or during the process of making concentrates. (grasschief.cc)
  • Following decarboxylation, the crude extract is now ready for the distillation process. (timelessvapes.com)
  • By understanding and implementing the basics of decarboxylation, we can maximize the quality and efficacy of the distillation process, ultimately providing us with highly refined cannabis extracts that offer a multitude of benefits. (timelessvapes.com)
  • Tetrahydrocannabinol (THC) present in weed speeds up the decarboxylation process. (mrhempflower.com)
  • The decarboxylation process modified the HPLC flavonoids profile and increased the resin's antioxidant activities. (ms-editions.cl)
  • It converts to THC when you expose the plant to heat and light - the process is known as decarboxylation. (cfah.org)
  • We recommended local exhaust ventilation for the grinding operations, moving the decarboxylation process to a seldom occupied area in the facility, developing a cleaning schedule to remove cannabis components from work and tool surfaces, and encouraging employees to report new or ongoing symptoms to their personal healthcare provider. (cdc.gov)
  • Decarboxylation can occur naturally over time, even without the application of heat. (avldispensary.com)
  • Decarboxylation, or the prolonged exposure of cannabis to heat, occurs immediately after smoking marihuana, when marihuana reacts to high temperatures. (nukaseeds.com)
  • The two major components which are required in order for decarboxylation to take place are simply time and heat. (grasschief.cc)
  • Heat being the major component means that when we smoke or vaporize our cannabis, decarboxylation can occur naturally. (grasschief.cc)
  • Considering heat, we know that decarboxylation begins to occur at around 220F. (grasschief.cc)
  • Once the desired decarboxylation level is reached, remove the heat source and let the container cool naturally. (timelessvapes.com)
  • Schematic representation of photocatalytic decarboxylation strategy for alkane production from biomass-derived fatty acids. (greencarcongress.com)
  • The researchers found that under illumination, the decarboxylation of fatty acids could be easily induced by photo-generated holes on the semiconductor TiO 2 , subsequently generating alkyl radical intermediates. (greencarcongress.com)
  • In simpler tests, as decarboxylation simply means removing carboxyl from the molecules in your herbs, allowing you to cook and consume it. (ongrok.com)
  • Decarboxylation of cannabis in a jar is one of the best decarboxylation methods because it helps preserve the cannabis terpenes , which have their own benefits and help preserve the flavour and aroma of the marihuana. (nukaseeds.com)
  • RH + CO2}}} Decarboxylation is one of the oldest known organic reactions. (wikipedia.org)
  • Decarboxylations are the bases of many named reactions. (wikipedia.org)
  • In addition to decarboxylation, OMPD is able to catalyze other reactions. (rcsb.org)
  • Usually, decarboxylation refers to a reaction of carboxylic acids, removing a carbon atom from a carbon chain. (wikipedia.org)
  • Decarboxylation of alkanoic acids is often slow. (wikipedia.org)
  • Overall, the facility of decarboxylation depends upon stability of the carbanion intermediate R− . Important exceptions are the decarboxylation of beta-keto acids, β,γ-unsaturated acids, and α-phenyl, α-nitro, and α-cyanoacids. (wikipedia.org)
  • [3] [4] Important exceptions are the decarboxylation of beta- keto acids , β,γ-unsaturated acids, and α-phenyl, α-nitro, and α-cyanoacids. (wikipedia.org)
  • Biotin-coupled processes effect the decarboxylation of malonyl-CoA to acetyl-CoA. (wikipedia.org)
  • I've heard about decarboxylation when it comes to preparing cannabis for consumption. (mjanswers.com)
  • To summarize, decarboxylation is an essential step when preparing cannabis for consumption. (mjanswers.com)
  • For users of marijuana flower, decarboxylation is essential because it allows them to get high. (mrhempflower.com)
  • Naturally, many are striving to achieve a complete decarboxylation. (grasschief.cc)
  • Decarboxylation draws the moisture out of the cannabis flowers. (alpinols.com)
  • In this blog post, we'll explore the basics of decarboxylation and its role in preparing crude cannabis extracts for distillation. (timelessvapes.com)
  • However, it is important to note that decarboxylation can also occur at lower temperatures and shorter heating times, especially if the cannabis is heated in a humid environment. (avldispensary.com)
  • Decarboxylation is an important step in preparing crude cannabis extracts for distillation. (timelessvapes.com)
  • What is decarboxylation and why is it important? (vancityherbs.ca)
  • Decarboxylation is the first step you need to take before infusing cannabis into oil , butter , tinctures , edibles , topicals , and more. (emilykylenutrition.com)
  • Decarboxylation is a vital step in the creation of CBD and THC isolates . (grasschief.cc)
  • However, the rate of decarboxylation is much slower under these conditions, and it is generally not enough to produce significant psychoactive effects. (avldispensary.com)
  • Time will produce some levels of decarboxylation, although the changes noted here will be quite minimal. (grasschief.cc)
  • LC−MS analysis of heating trials, deuterium labeling experiments, and kinetic studies demonstrated that a carboxylated AZA analogue, AZA17, undergoes rapid decarboxylation when heated to produce AZA3. (canada.ca)
  • Nug Smasher's answer to easy and fast decarboxylation! (urban-grow.ca)
  • They simply add their solventless Rosin to the Rosin POT and enclose the POT in the Decarboxylation Capsule, then add to your machine according to the times below. (urban-grow.ca)