"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.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
An important enzyme in the glyoxylic acid cycle which reversibly catalyzes the synthesis of L-malate from acetyl-CoA and glyoxylate. This enzyme was formerly listed as EC 4.1.3.2.
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.
A dicarboxylic acid ketone that is an important metabolic intermediate of the CITRIC ACID CYCLE. It can be converted to ASPARTIC ACID by ASPARTATE TRANSAMINASE.
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.
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.
"Citrates, in a medical context, are compounds containing citric acid, often used in medical solutions for their chelating properties and as a part of certain types of nutritional support."
Compounds based on fumaric acid.
A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)
Derivatives of SUCCINIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,4-carboxy terminated aliphatic structure.
A key enzyme in the glyoxylate cycle. It catalyzes the conversion of isocitrate to succinate and glyoxylate. EC 4.1.3.1.
Dicarboxylic acids are organic compounds containing two carboxyl (-COOH) groups in their structure, making them capable of forming salts and esters by losing two hydrogen ions.
An enzyme that catalyzes the reversible hydration of fumaric acid to yield L-malic acid. It is one of the citric acid cycle enzymes. EC 4.2.1.2.
A key intermediate in metabolism. It is an acid compound found in citrus fruits. The salts of citric acid (citrates) can be used as anticoagulants due to their calcium chelating ability.
An enzyme with high affinity for carbon dioxide. It catalyzes irreversibly the formation of oxaloacetate from phosphoenolpyruvate and carbon dioxide. This fixation of carbon dioxide in several bacteria and some plants is the first step in the biosynthesis of glucose. EC 4.1.1.31.
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)
Enzymes that catalyze the cleavage of a carbon-carbon bond of a 3-hydroxy acid. (Dorland, 28th ed) EC 4.1.3.
Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.
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 ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.
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)
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.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
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.
A metallic element that has the atomic number 13, atomic symbol Al, and atomic weight 26.98.
The rate dynamics in chemical or physical systems.
Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)
The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
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.
Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.
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).
The mitochondria of the myocardium.
A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.
The Ketoglutarate Dehydrogenase Complex is a multi-enzyme complex involved in the citric acid cycle, catalyzing the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA and CO2, thereby connecting the catabolism of amino acids, carbohydrates, and fats to the generation of energy in the form of ATP.
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.
Derivatives of ACETIC ACID which contain an hydroxy group attached to the methyl carbon.
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 organic anion transporters that specifically transport DICARBOXYLIC ACIDS such as alpha-ketoglutaric acid across cellular membranes.
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 class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.
Proteins involved in the transport of organic anions. They play an important role in the elimination of a variety of endogenous substances, xenobiotics and their metabolites from the body.
Salts or esters of LACTIC ACID containing the general formula CH3CHOHCOOR.
Mitochondria of skeletal and smooth muscle. It does not include myocardial mitochondria for which MITOCHONDRIA, HEART is available.
A botanical insecticide that is an inhibitor of mitochondrial electron transport.
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
An aspartate aminotransferase found in MITOCHONDRIA.
A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.
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.
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.
Organic compounds that are acyclic and contain three acid groups. A member of this class is citric acid which is the first product formed by reaction of pyruvate and oxaloacetate. (From Lehninger, Principles of Biochemistry, 1982, p443)
Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.
A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.
A nonmetallic element with atomic symbol C, atomic number 6, and atomic weight [12.0096; 12.0116]. It may occur as several different allotropes including DIAMOND; CHARCOAL; and GRAPHITE; and as SOOT from incompletely burned fuel.
An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.
Biosynthesis of GLUCOSE from nonhexose or non-carbohydrate precursors, such as LACTATE; PYRUVATE; ALANINE; and GLYCEROL.
Tartrates are salts or esters of tartaric acid, primarily used in pharmaceutical industry as buffering agents, and in medical laboratories for the precipitation of proteins.
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.
Gram-negative aerobic rods found in warm water (40-79 degrees C) such as hot springs, hot water tanks, and thermally polluted rivers.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
A compound that inhibits aminobutyrate aminotransferase activity in vivo, thereby raising the level of gamma-aminobutyric acid in tissues.
A plant genus of the family BROMELIACEAE known for the edible fruit that is the source of BROMELAINS.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Electron transfer through the cytochrome system liberating free energy which is transformed into high-energy phosphate bonds.

Control of ketogenesis from amino acids. IV. Tissue specificity in oxidation of leucine, tyrosine, and lysine. (1/967)

In vitro and in vivo studies were made on the tissue specificity of oxidation of the ketogenic amino acids, leucine, tyrosine, and lysine. In in vitro studies the abilities of slices of various tissues of rats to form 14CO2 from 14C-amino acids were examined. With liver, but not kidney slices, addition of alpha-ketoglutarate was required for the maximum activities with these amino acids. Among the various tissues tested, kidney had the highest activity for lysine oxidation, followed by liver; other tissues showed very low activity. Kidney also had the highest activity for leucine oxidation, followed by diaphragm; liver and adipose tissue had lower activities. Liver had the highest activity for tyrosine oxidation, but kidney also showed considerable activity; other tissues had negligible activity. In in vivo studies the blood flow through the liver or kidney was stopped by ligation of the blood vessels. Then labeled amino acids were injected and recovery of radioactivity in respiratory 14CO2 was measured. In contrast to results with slices, no difference was found in the respiratory 14CO2 when the renal blood vessels were or were not ligated. On the contrary ligation of the hepatic vessels suppressed the oxidations of lysine and tyrosine completely and that of leucine partially. Thus in vivo, lysine and tyrosine seem to be metabolized mainly in the liver, whereas leucine is metabolized mostly in extrahepatic tissues and partly in liver. Use of tissue slices seems to be of only limited value in elucidating the metabolisms of these amino acids.  (+info)

Microbial oxidation and assimilation of propylene. (2/967)

Hydrocarbon-utilizing microorganisms in our culture collection oxidized propylene but could not utilize it as the sole source of carbon and energy. When propane-grown cells of Mycobacterium convulutum were placed on propylene, acrylate, the terminally oxidized, three-carbon unsaturated acid, accumulated. A mixed culture and an axenic culture (strain PL-1) that utilized propylene as the sole source of carbon and energy were isolated from soil. Respiration rates, enzyme assays, fatty acid profiles, and 14CO2 incorporation experiments suggest that both the mixed culture and strain PL-1 oxidize propylene via attack at the double bond, resulting in a C2+C1 cleavage of the molecule.  (+info)

Replenishment and depletion of citric acid cycle intermediates in skeletal muscle. Indication of pyruvate carboxylation. (3/967)

The effects of various substrates on the concentrations of free amino acids, citric acid cycle intermediates and acylcarnitines were studies in perfused hindquarter of rat in presence of glucose and insulin in order to assess regulatory mechanisms of the level of citric acid cycle intermediates in skeletal muscle. 1. Acetate and acetoacetate effected a significant increase in the level of citrate cycle intermediates and accumulation of acetylcarnitine. These changes were accompanied by a reduction in the level of alanine. The concentration of AMP was significantly elevated. 2. Muscle mitochondria fixed 14CO2 in the presence of pyruvate. The products were identified as malate or citrate when whole and disintegrated mitochondria were used respectively. The fixation was greatly stimulated by acetylcarnitine. 3. Acetylcarnitine inhibited the production of pyruvate from malate by muscle mitochondria. 4. Perfusion with 2-oxoisocaproate and 2-oxoisovalerate promoted increases in the level of citric cycle intermediates, a drop in both alanine and glutamate, and accumulation of branched-chain acylcarnitines. 2-Oxoisocaproate also caused a reduction of alanine released from the muscle. 5. Perfusion with leucine and valine did not change the concentration of citric acid cycle intermediates, but elevated glutamate and still more the concentration of alanine. 6. It is concluded that citric cycle intermediate level in the perfused resting muscle is modified by a) conditions which change the concentration of acetyl-CoA and thereby modify the rate of pyruvate carboxylation and decarboxylation of malate via malic enzyme b) conditions which change the concentration of pyruvate cause changes in alanine and cycle intermediates in the same direction via transamination reactions c) conditions which change the concentrations of 2-oxoacids which are converted to cycle intermediates via oxidation.  (+info)

Metabolism of threo-beta-methylmalate by a soil bacterium. (4/967)

Studies on threo-beta-methylmalate metabolism in a soil bacterium of the genus Bacillus which can utilize threo-beta-methylmalate as a sole carbon source were carried out. When DL-threo-beta-methylmalate was incubated with a cell-free extract of the bacterium, citramalate was found to be formed. Similarly, formation of threo-beta-methylmalate from DL-citramalate was confirmed. These dicarbosylic acids were identified by gas chromatography-mass spectrometry. Examination of inducibility, substrate specificity, and cofactor requirement of the enzymes involved in the reactions showed the existence of two interconversion reactions between the threo-beta-methylmalate and citramalate. One was an interconversion reaction between L-threo-beta-methylmalate and L-citramalate via mesaconate and the other was an interconversion reaction between D-threo-beta-methylmalate and D-citramalate via citraconate. These reactions were both reversible and were catalyzed by distinct and inducible enzymes. It is suggested that the two reactions participate in the catabolism of threo-beta-methylmalate.  (+info)

Metabolism and the triggering of germination of Bacillus megaterium. Concentrations of amino acids, organic acids, adenine nucleotides and nicotinamide nucleotides during germination. (5/967)

A considerable amount of evidence suggests that metabolism of germinants or metabolism stimulated by them is involved in triggering bacterial-spore germination. On the assumption that such a metabolic trigger might lead to relatively small biochemical changes in the first few minutes of germination, sensitive analytical techniques were used to detect any changes in spore components during the L-alanine-triggered germination of Bacillus megaterium KM spores. These experiments showed that no changes in spore free amino acids or ATP occurred until 2-3 min after L-alanine addition. Spores contained almost no oxo acids (pyruvate, alpha-oxoglutarate, oxaloacetate), malate or reduced NAD. These compounds were again not detectable until 2-3 min after addition of germinants. It is suggested, therefore, that metabolism associated with these intermediates is not involved in the triggering of germination of this organism.  (+info)

Influence of malic acid supplementation on ruminal pH, lactic acid utilization, and digestive function in steers fed high-concentrate finishing diets. (6/967)

Two trials were conducted to evaluate the influence of malic acid supplementation on ruminal fermentation. In Trial 1, six Holstein steers (300 kg) with ruminal cannulas were used in a crossover design experiment to study the influence of malic acid (MA) on ruminal metabolism during glucose-induced lactic acidosis. Treatments consisted of a 77% steam-flaked barley-based finishing diet supplemented to provide 0 or 80 g/d of MA. After a 13-d dietary adjustment period, 1 kg of glucose was infused into the rumen 1 h after the morning feeding. Ruminal pH was closely associated (R2 = .70) with ruminal DL-lactate concentration. Malic acid supplementation increased (P < .01) ruminal pH 3 h after the glucose infusion. However, there were no treatment effects (P > .10) on ruminal VFA molar proportions or ruminal and plasma DL-lactate concentrations. In Trial 2, four Holstein steers (150 kg) with cannulas in the rumen and proximal duodenum were used in a crossover design experiment to evaluate the influence of MA supplementation on characteristics of digestion. Treatments consisted of an 81% steam-flaked barley-based finishing diet supplemented to provide 0 or 80 g/d of MA. There were no treatment effects (P > .10) on ruminal and total tract digestion of OM, ADF, starch, and feed N or on ruminal microbial efficiency. Malic acid supplementation increased (P < .05) ruminal pH 2 h after feeding. As with Trial 1, there were no treatment effects (P > .10) on ruminal VFA and DL-lactate concentrations. We conclude that supplementation of high-grain finishing diets with MA may be beneficial in promoting a higher ruminal pH during periods of peak acid production without detrimental effects on ruminal microbial efficiency or starch, fiber, and protein digestion. There were no detectable beneficial effects of MA supplementation on ruminal and plasma lactic acid concentrations in cattle fed high-grain diets.  (+info)

Comparative absorption of calcium sources and calcium citrate malate for the prevention of osteoporosis. (7/967)

Anthropologically speaking, humans were high consumers of calcium until the onset of the Agricultural Age, 10,000 years ago. Current calcium intake is one-quarter to one-third that of our evolutionary diet and, if we are genetically identical to the Late Paleolithic Homo sapiens, we may be consuming a calcium-deficient diet our bodies cannot adjust to by physiologic mechanisms. Meta-analyses of calcium and bone mass studies demonstrate supplementation of 500 to 1500 mg calcium daily improves bone mass in adolescents, young adults, older men, and postmenopausal women. Calcium citrate malate has high bioavailability and thus has been the subject of calcium studies in these populations. Positive effects have been seen in prepubertal girls, adolescents, and postmenopausal women. The addition of trace minerals and vitamin D in separate trials has improved the effect of calcium citrate malate on bone density and shown a reduction of fracture risk.  (+info)

Effects of DL-malate on ruminal metabolism and performance of cattle fed a high-concentrate diet. (8/967)

To determine the effects of DL-malate on ruminal metabolism, four steers equipped with ruminal cannulas were fed an 80% rolled grain (75% corn:25% wheat) diet twice daily with a DMI equal to 2.0% of BW (485+/-24.8 kg). DL-Malate was infused into the rumen on two consecutive days in 500 mL of phosphate buffer to provide 0, 27, 54, or 80 g of DL-malate/d. Ruminal pH linearly increased (P < .01) with DL-malate concentration and was greater (P < .01) for DL-malate than for the control steers (6.07 vs 5.77). DL-Malate treatment linearly decreased (P < .10) total VFA and tended to linearly increase (P = .10) acetate concentration. Propionate, butyrate, and L-lactate concentrations and acetate:propionate ratio were not affected (P > .10) by DL-malate. Three finishing studies were conducted to determine the effects of feeding DL-malate on growth rate and feed efficiency. In a 98-d experiment, 33 crossbred steers were randomly allotted in a Calan gate feeding system to three DL-malate levels (0, 40, and 80 g/d). Steers (initial weight = 367+/-4.5 kg) were fed a rolled corn-based diet twice daily. After 84 d on feed, gain efficiency (gain:feed) tended to improve with more DL-malate (linear, P < .10) and was 8.1% greater (P < .05) for DL-malate than for the control. The ADG linearly increased (P < .05) with more DL-malate and was 8.6% greater (P = .10) for DL-malate than for the control. After 98-d on feed, ADG was linearly increased (P = .09) by DL--malate, and the greatest increase occurred with 80 g of DL-malate. In the second performance study, 27 Angus steers were randomly allotted in a Calan gate feeding system to three DL-malate concentrations (0, 60, and 120 g/d). Steers (initial weight = 432+/-4.6 kg) were fed diets used in the first finishing study twice daily, but DL-malate was included during the 10-d step-up period. During the 10-d step-up period, feed efficiency and ADG linearly increased (P = .01) with more DL-malate. DL-Malate had little effect on steer and heifer performance or plasma constituents in a 113-d finishing study. Collectively, these results suggest that feeding DL-malate to cattle consuming high-grain diets alleviates subclinical acidosis, and it improved animal performance in two finishing studies.  (+info)

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.

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.

Malate Synthase is a key enzyme in the gluconeogenesis pathway and the glyoxylate cycle, which are present in many organisms including plants, bacteria, and parasites. The glyoxylate cycle is a variation of the citric acid cycle (Krebs cycle) that allows these organisms to convert two-carbon molecules into four-carbon molecules, bypassing steps that require oxygen.

Malate Synthase catalyzes the reaction between glyoxylate and acetyl-CoA to produce malate, a four-carbon compound. This enzyme plays a crucial role in enabling these organisms to utilize fatty acids as a carbon source for growth and energy production, particularly under conditions where oxygen is limited or absent. In humans, Malate Synthase is not typically found, but its presence can indicate certain parasitic infections or metabolic disorders.

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.

Oxaloacetic acid is a chemical compound that plays a significant role in the Krebs cycle, also known as the citric acid cycle. It is a key metabolic intermediate in both glucose and fatty acid catabolism. Oxaloacetic acid is a four-carbon carboxylic acid that has two carboxyl groups and one ketone group.

In the Krebs cycle, oxaloacetic acid reacts with acetyl-CoA (an activated form of acetic acid) to form citric acid, releasing CoA and initiating the cycle. Throughout the cycle, oxaloacetic acid is continuously regenerated from malate, another intermediate in the cycle.

Additionally, oxaloacetic acid plays a role in amino acid metabolism as it can accept an amino group (NH3) to form aspartic acid, which is an essential component of several biochemical processes, including protein synthesis and the urea cycle.

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.

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.

Citrates are the salts or esters of citric acid, a weak organic acid that is naturally found in many fruits and vegetables. In a medical context, citrates are often used as a buffering agent in intravenous fluids to help maintain the pH balance of blood and other bodily fluids. They are also used in various medical tests and treatments, such as in urine alkalinization and as an anticoagulant in kidney dialysis solutions. Additionally, citrate is a component of some dietary supplements and medications.

Fumarates are the salts or esters of fumaric acid, a naturally occurring organic compound with the formula HO2C-CH=CH-CO2H. In the context of medical therapy, fumarates are used as medications for the treatment of psoriasis and multiple sclerosis.

One such medication is dimethyl fumarate (DMF), which is a stable salt of fumaric acid. DMF has anti-inflammatory and immunomodulatory properties, and it's used to treat relapsing forms of multiple sclerosis (MS) and moderate-to-severe plaque psoriasis.

The exact mechanism of action of fumarates in these conditions is not fully understood, but they are thought to modulate the immune system and have antioxidant effects. Common side effects of fumarate therapy include gastrointestinal symptoms such as diarrhea, nausea, and abdominal pain, as well as flushing and skin reactions.

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.

Succinates, in a medical context, most commonly refer to the salts or esters of succinic acid. Succinic acid is a dicarboxylic acid that is involved in the Krebs cycle, which is a key metabolic pathway in cells that generates energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins.

Succinates can also be used as a buffer in medical solutions and as a pharmaceutical intermediate in the synthesis of various drugs. In some cases, succinate may be used as a nutritional supplement or as a component of parenteral nutrition formulations to provide energy and help maintain acid-base balance in patients who are unable to eat normally.

It's worth noting that there is also a condition called "succinic semialdehyde dehydrogenase deficiency" which is a genetic disorder that affects the metabolism of the amino acid gamma-aminobutyric acid (GABA). This condition can lead to an accumulation of succinic semialdehyde and other metabolic byproducts, which can cause neurological symptoms such as developmental delay, hypotonia, and seizures.

Isocitrate lyase is an enzyme that plays a crucial role in the glyoxylate cycle, a metabolic pathway found in plants, bacteria, fungi, and parasites. This cycle bypasses two steps of the citric acid cycle (TCA cycle) and allows these organisms to grow on two-carbon compounds as their sole carbon source.

Isocitrate lyase specifically catalyzes the conversion of isocitrate into succinate and glyoxylate, which are further processed in the glyoxylate cycle to generate oxaloacetate and other metabolic intermediates. In humans, isocitrate lyase is not typically found in healthy tissues but has been observed in certain pathological conditions such as tumor growth and during periods of nutrient deprivation. It is also involved in the biosynthesis of fatty acids and steroids in some organisms.

Dicarboxylic acids are organic compounds containing two carboxyl groups (-COOH) in their molecular structure. The general formula for dicarboxylic acids is HOOC-R-COOH, where R represents a hydrocarbon chain or a functional group.

The presence of two carboxyl groups makes dicarboxylic acids stronger acids than monocarboxylic acids (compounds containing only one -COOH group). This is because the second carboxyl group contributes to the acidity of the molecule, allowing it to donate two protons in solution.

Examples of dicarboxylic acids include oxalic acid (HOOC-COOH), malonic acid (CH2(COOH)2), succinic acid (HOOC-CH2-CH2-COOH), glutaric acid (HOOC-(CH2)3-COOH), and adipic acid (HOOC-(CH2)4-COOH). These acids have various industrial applications, such as in the production of polymers, dyes, and pharmaceuticals.

Fumarate hydratase (FH) is an enzyme that plays a crucial role in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle. The citric acid cycle 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), carbon dioxide, and water.

Fumarate hydratase is specifically responsible for catalyzing the conversion of fumarate to malate in this cycle. A deficiency or dysfunction of this enzyme can lead to various metabolic disorders and hereditary diseases, such as fumarate hydratase deficiency, which may manifest as neurological issues, hemolytic anemia, and an increased risk of developing renal cell carcinoma.

Citric acid is a weak organic acid that is widely found in nature, particularly in citrus fruits such as lemons and oranges. Its chemical formula is C6H8O7, and it exists in a form known as a tribasic acid, which means it can donate three protons in chemical reactions.

In the context of medical definitions, citric acid may be mentioned in relation to various physiological processes, such as its role in the Krebs cycle (also known as the citric acid cycle), which is a key metabolic pathway involved in energy production within cells. Additionally, citric acid may be used in certain medical treatments or therapies, such as in the form of citrate salts to help prevent the formation of kidney stones. It may also be used as a flavoring agent or preservative in various pharmaceutical preparations.

Phosphoenolpyruvate carboxylase (PEP-carboxylase or PEPC) is a biotin-dependent enzyme that plays a crucial role in the carbon fixation process of photosynthesis, specifically in the C4 and CAM (Crassulacean Acid Metabolism) plant pathways. It is also found in some bacteria and archaea.

PEP-carboxylase catalyzes the irreversible reaction between phosphoenolpyruvate (PEP) and bicarbonate (HCO3-) to form oxaloacetate and inorganic phosphate (Pi). This reaction helps to initiate the carbon fixation process by incorporating atmospheric carbon dioxide into an organic molecule, which can then be used for various metabolic processes.

In C4 plants, PEP-carboxylase is primarily located in the mesophyll cells where it facilitates the initial fixation of CO2 onto PEP, forming oxaloacetate. This oxaloacetate is then reduced to malate, which is subsequently transported to bundle sheath cells for further metabolism and additional carbon fixation by another enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO).

In CAM plants, PEP-carboxylase operates at night to fix CO2 into malate, which is stored in vacuoles. During the day, malate is decarboxylated, releasing CO2 for RuBisCO-mediated carbon fixation while conserving water through reduced stomatal opening.

PEP-carboxylase is also found in some non-photosynthetic bacteria and archaea, where it contributes to various metabolic pathways such as gluconeogenesis, anaplerotic reactions, and the glyoxylate cycle.

NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.

Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.

Succinic acid, also known as butanedioic acid, is an organic compound with the chemical formula HOOC(CH2)2COOH. It is a white crystalline powder that is soluble in water and has a slightly acerbic taste. In medicine, succinic acid is not used as a treatment for any specific condition. However, it is a naturally occurring substance found in the body and plays a role in the citric acid cycle, which is a key process in energy production within cells. It can also be found in some foods and is used in the manufacturing of various products such as pharmaceuticals, resins, and perfumes.

Oxo-acid lyases are a class of enzymes that catalyze the cleavage of a carbon-carbon bond in an oxo-acid to give a molecule with a carbonyl group and a carbanion, which then reacts non-enzymatically with a proton to form a new double bond. The reaction is reversible, and the enzyme can also catalyze the reverse reaction.

Oxo-acid lyases play important roles in various metabolic pathways, such as the citric acid cycle, glyoxylate cycle, and the degradation of certain amino acids. These enzymes are characterized by the presence of a conserved catalytic mechanism involving a nucleophilic attack on the carbonyl carbon atom of the oxo-acid substrate.

The International Union of Biochemistry and Molecular Biology (IUBMB) has classified oxo-acid lyases under EC 4.1.3, which includes enzymes that catalyze the formation of a carbon-carbon bond by means other than carbon-carbon bond formation to an enolate or carbonion, a carbanionic fragment, or a Michael acceptor.

"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.

Acetates, in a medical context, most commonly refer to compounds that contain the acetate group, which is an functional group consisting of a carbon atom bonded to two hydrogen atoms and an oxygen atom (-COO-). An example of an acetate is sodium acetate (CH3COONa), which is a salt formed from acetic acid (CH3COOH) and is often used as a buffering agent in medical solutions.

Acetates can also refer to a group of medications that contain acetate as an active ingredient, such as magnesium acetate, which is used as a laxative, or calcium acetate, which is used to treat high levels of phosphate in the blood.

In addition, acetates can also refer to a process called acetylation, which is the addition of an acetyl group (-COCH3) to a molecule. This process can be important in the metabolism and regulation of various substances within the body.

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.

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.

Mitochondria are specialized structures located inside cells that convert the energy from food into ATP (adenosine triphosphate), which is the primary form of energy used by cells. They are often referred to as the "powerhouses" of the cell because they generate most of the cell's supply of chemical energy. Mitochondria are also involved in various other cellular processes, such as signaling, differentiation, and apoptosis (programmed cell death).

Mitochondria have their own DNA, known as mitochondrial DNA (mtDNA), which is inherited maternally. This means that mtDNA is passed down from the mother to her offspring through the egg cells. Mitochondrial dysfunction has been linked to a variety of diseases and conditions, including neurodegenerative disorders, diabetes, and aging.

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.

The chemical element aluminum (or aluminium in British English) is a silvery-white, soft, non-magnetic, ductile metal. The atomic number of aluminum is 13 and its symbol on the periodic table is Al. It is the most abundant metallic element in the Earth's crust and is found in a variety of minerals such as bauxite.

Aluminum is resistant to corrosion due to the formation of a thin layer of aluminum oxide on its surface that protects it from further oxidation. It is lightweight, has good thermal and electrical conductivity, and can be easily formed and machined. These properties make aluminum a widely used metal in various industries such as construction, packaging, transportation, and electronics.

In the medical field, aluminum is used in some medications and medical devices. For example, aluminum hydroxide is commonly used as an antacid to neutralize stomach acid and treat heartburn, while aluminum salts are used as adjuvants in vaccines to enhance the immune response. However, excessive exposure to aluminum can be harmful and has been linked to neurological disorders such as Alzheimer's disease, although the exact relationship between aluminum and these conditions is not fully understood.

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'd be happy to help! However, I believe there might be a slight misunderstanding in your question. Mitochondria are organelles found in the cells of all complex living organisms, including humans, while the liver is a large, solid organ located in the upper right portion of the abdomen. They don't have a medical definition together. I can certainly provide you with separate definitions for each:

1. Mitochondria: These are double-membrane-bound cellular organelles that generate most of the chemical energy needed to power the cell's biochemical reactions. Commonly known as the "powerhouse of the cell," mitochondria convert organic substrates, such as glucose, fatty acids, and amino acids, into adenosine triphosphate (ATP) through a process called oxidative phosphorylation. Mitochondria are dynamic structures that can change their shape, size, and number through fission (division) and fusion (merging) processes. They play essential roles in various cellular functions, including calcium signaling, apoptosis (programmed cell death), and the regulation of cellular metabolism.

2. Liver: The liver is a large, lobulated organ that lies mainly in the upper right portion of the abdominal cavity, just below the diaphragm. It plays a crucial role in various physiological functions, such as detoxification, protein synthesis, metabolism, and nutrient storage. The liver is responsible for removing toxins from the bloodstream, producing bile to aid in digestion, regulating glucose levels, synthesizing plasma proteins, and storing glycogen, vitamins, and minerals. It also contributes to the metabolism of carbohydrates, lipids, and amino acids, helping maintain energy homeostasis in the body.

I hope this clarifies any confusion! If you have any further questions or need more information, please don't hesitate to ask.

Oxygen consumption, also known as oxygen uptake, is the amount of oxygen that is consumed or utilized by the body during a specific period of time, usually measured in liters per minute (L/min). It is a common measurement used in exercise physiology and critical care medicine to assess an individual's aerobic metabolism and overall health status.

In clinical settings, oxygen consumption is often measured during cardiopulmonary exercise testing (CPET) to evaluate cardiovascular function, pulmonary function, and exercise capacity in patients with various medical conditions such as heart failure, chronic obstructive pulmonary disease (COPD), and other respiratory or cardiac disorders.

During exercise, oxygen is consumed by the muscles to generate energy through a process called oxidative phosphorylation. The amount of oxygen consumed during exercise can provide important information about an individual's fitness level, exercise capacity, and overall health status. Additionally, measuring oxygen consumption can help healthcare providers assess the effectiveness of treatments and rehabilitation programs in patients with various medical conditions.

Aspartic acid is an α-amino acid with the chemical formula HO2CCH(NH2)CO2H. It is one of the twenty standard amino acids, and it is a polar, negatively charged, and hydrophilic amino acid. In proteins, aspartic acid usually occurs in its ionized form, aspartate, which has a single negative charge.

Aspartic acid plays important roles in various biological processes, including metabolism, neurotransmitter synthesis, and energy production. It is also a key component of many enzymes and proteins, where it often contributes to the formation of ionic bonds and helps stabilize protein structure.

In addition to its role as a building block of proteins, aspartic acid is also used in the synthesis of other important biological molecules, such as nucleotides, which are the building blocks of DNA and RNA. It is also a component of the dipeptide aspartame, an artificial sweetener that is widely used in food and beverages.

Like other amino acids, aspartic acid is essential for human health, but it cannot be synthesized by the body and must be obtained through the diet. Foods that are rich in aspartic acid include meat, poultry, fish, dairy products, eggs, legumes, and some fruits and vegetables.

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.

Glutamates are the salt or ester forms of glutamic acid, which is a naturally occurring amino acid and the most abundant excitatory neurotransmitter in the central nervous system. Glutamate plays a crucial role in various brain functions, such as learning, memory, and cognition. However, excessive levels of glutamate can lead to neuronal damage or death, contributing to several neurological disorders, including stroke, epilepsy, and neurodegenerative diseases like Alzheimer's and Parkinson's.

Glutamates are also commonly found in food as a natural flavor enhancer, often listed under the name monosodium glutamate (MSG). While MSG has been extensively studied, its safety remains a topic of debate, with some individuals reporting adverse reactions after consuming foods containing this additive.

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.

I'm happy to help! However, it seems like there are two terms combined into one request: "Mitochondria" and "Heart." I will provide separate definitions for each.

Mitochondrion (singular) or Mitochondria (plural): These are specialized structures found in the cytoplasm of most eukaryotic cells (cells with a true nucleus), including human cells. They are often referred to as the "powerhouse" of the cell because they generate energy in the form of ATP (adenosine triphosphate) through a process called oxidative phosphorylation. Mitochondria contain their own DNA, which is distinct from the nuclear DNA, and are believed to have originated from ancient bacteria that established a symbiotic relationship with primitive eukaryotic cells.

Heart: In human anatomy, the heart is a muscular organ responsible for pumping blood throughout the body. It is located in the thoracic cavity, slightly left of the center, and is enclosed by the pericardium, a double-walled sac that provides protection and lubrication for the heart's movement. The human heart is divided into four chambers: two atria on the top and two ventricles on the bottom. The right side of the heart receives deoxygenated blood from the body and pumps it to the lungs, while the left side receives oxygenated blood from the lungs and pumps it to the rest of the body. The heart's pumping action is regulated by electrical signals that originate in a group of specialized cardiac muscle cells called the sinoatrial node (SA node).

L-Lactate Dehydrogenase (LDH) is an enzyme found in various tissues within the body, including the heart, liver, kidneys, muscles, and brain. It plays a crucial role in the process of energy production, particularly during anaerobic conditions when oxygen levels are low.

In the presence of the coenzyme NADH, LDH catalyzes the conversion of pyruvate to lactate, generating NAD+ as a byproduct. Conversely, in the presence of NAD+, LDH can convert lactate back to pyruvate using NADH. This reversible reaction is essential for maintaining the balance between lactate and pyruvate levels within cells.

Elevated blood levels of LDH may indicate tissue damage or injury, as this enzyme can be released into the circulation following cellular breakdown. As a result, LDH is often used as a nonspecific biomarker for various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and certain types of cancer. However, it's important to note that an isolated increase in LDH does not necessarily pinpoint the exact location or cause of tissue damage, and further diagnostic tests are usually required for confirmation.

Succinate dehydrogenase (SDH) is an enzyme complex that plays a crucial role in the process of cellular respiration, specifically in the citric acid cycle (also known as the Krebs cycle) and the electron transport chain. It is located in the inner mitochondrial membrane of eukaryotic cells.

SDH catalyzes the oxidation of succinate to fumarate, converting it into a molecule of fadaquate in the process. During this reaction, two electrons are transferred from succinate to the FAD cofactor within the SDH enzyme complex, reducing it to FADH2. These electrons are then passed on to ubiquinone (CoQ), which is a mobile electron carrier in the electron transport chain, leading to the generation of ATP, the main energy currency of the cell.

SDH is also known as mitochondrial complex II because it is the second complex in the electron transport chain. Mutations in the genes encoding SDH subunits or associated proteins have been linked to various human diseases, including hereditary paragangliomas, pheochromocytomas, gastrointestinal stromal tumors (GISTs), and some forms of neurodegenerative disorders.

The Ketoglutarate Dehydrogenase Complex (KGDC or α-KGDH) is a multi-enzyme complex that plays a crucial role in the Krebs cycle, also known as the citric acid cycle. It is located within the mitochondrial matrix of eukaryotic cells and functions to catalyze the oxidative decarboxylation of α-ketoglutarate into succinyl-CoA, thereby connecting the Krebs cycle to the electron transport chain for energy production.

The KGDC is composed of three distinct enzymes:

1. α-Ketoglutarate dehydrogenase (E1): This enzyme catalyzes the decarboxylation and oxidation of α-ketoglutarate to form a thioester intermediate with lipoamide, which is bound to the E2 component.
2. Dihydrolipoyl succinyltransferase (E2): This enzyme facilitates the transfer of the acetyl group from the lipoamide cofactor to CoA, forming succinyl-CoA and regenerating oxidized lipoamide.
3. Dihydrolipoyl dehydrogenase (E3): The final enzyme in the complex catalyzes the reoxidation of reduced lipoamide back to its disulfide form, using FAD as a cofactor and transferring electrons to NAD+, forming NADH.

The KGDC is subject to regulation by several mechanisms, including phosphorylation-dephosphorylation reactions that can inhibit or activate the complex, respectively. Dysfunction of this enzyme complex has been implicated in various diseases, such as neurodegenerative disorders and cancer.

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.

Glycolates are a type of chemical compound that contain the group COOCH2, which is derived from glycolic acid. In a medical context, glycolates are often used in dental and medical materials as they can be biodegradable and biocompatible. For example, they may be used in controlled-release drug delivery systems or in bone cement. However, it's important to note that some glycolate compounds can also be toxic if ingested or otherwise introduced into the body in large amounts.

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.

Dicarboxylic acid transporters are a type of membrane transport protein that are responsible for the transportation of dicarboxylic acids across biological membranes. Dicarboxylic acids are organic compounds that contain two carboxyl groups, and they play important roles in various metabolic processes within the body.

The sodium-dependent dicarboxylic acid transporters (NaDCs) are a subfamily of these transporters that are widely expressed in many tissues, including the kidney, intestine, and brain. NaDCs mediate the uptake of dicarboxylates, such as succinate and glutarate, into cells in an energy-dependent manner, using the gradient of sodium ions across the membrane to drive the transport process.

The other subfamily of dicarboxylic acid transporters are the proton-coupled dicarboxylate transporters (PCDTs), which use a proton gradient to transport dicarboxylates. These transporters play important roles in the absorption and metabolism of dietary fibers, as well as in the regulation of intracellular pH.

Defects in dicarboxylic acid transporters have been implicated in several human diseases, including renal tubular acidosis, a condition characterized by impaired ability to excrete hydrogen ions and reabsorb bicarbonate ions in the kidney.

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.

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

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

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

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

Organic anion transporters (OATs) are membrane transport proteins that are responsible for the cellular uptake and excretion of various organic anions, such as drugs, toxins, and endogenous metabolites. They are found in various tissues, including the kidney, liver, and brain, where they play important roles in the elimination and detoxification of xenobiotics and endogenous compounds.

In the kidney, OATs are located in the basolateral membrane of renal tubular epithelial cells and mediate the uptake of organic anions from the blood into the cells. From there, the anions can be further transported into the urine by other transporters located in the apical membrane. In the liver, OATs are expressed in the sinusoidal membrane of hepatocytes and facilitate the uptake of organic anions from the blood into the liver cells for metabolism and excretion.

There are several isoforms of OATs that have been identified, each with distinct substrate specificities and tissue distributions. Mutations in OAT genes can lead to various diseases, including renal tubular acidosis, hypercalciuria, and drug toxicity. Therefore, understanding the function and regulation of OATs is important for developing strategies to improve drug delivery and reduce adverse drug reactions.

Lactates, also known as lactic acid, are compounds that are produced by muscles during intense exercise or other conditions of low oxygen supply. They are formed from the breakdown of glucose in the absence of adequate oxygen to complete the full process of cellular respiration. This results in the production of lactate and a hydrogen ion, which can lead to a decrease in pH and muscle fatigue.

In a medical context, lactates may be measured in the blood as an indicator of tissue oxygenation and metabolic status. Elevated levels of lactate in the blood, known as lactic acidosis, can indicate poor tissue perfusion or hypoxia, and may be seen in conditions such as sepsis, cardiac arrest, and severe shock. It is important to note that lactates are not the primary cause of acidemia (low pH) in lactic acidosis, but rather a marker of the underlying process.

Mitochondria in muscle, also known as the "powerhouses" of the cell, are organelles that play a crucial role in generating energy for muscle cells through a process called cellular respiration. They convert the chemical energy found in glucose and oxygen into ATP (adenosine triphosphate), which is the main source of energy used by cells.

Muscle cells contain a high number of mitochondria due to their high energy demands for muscle contraction and relaxation. The number and size of mitochondria in muscle fibers can vary depending on the type of muscle fiber, with slow-twitch, aerobic fibers having more numerous and larger mitochondria than fast-twitch, anaerobic fibers.

Mitochondrial dysfunction has been linked to various muscle disorders, including mitochondrial myopathies, which are characterized by muscle weakness, exercise intolerance, and other symptoms related to impaired energy production in the muscle cells.

Rotenone is not strictly a medical term, but it is a pesticide that is used in some medical situations. According to the National Pesticide Information Center, rotenone is a pesticide derived from the roots and stems of several plants, including Derris Eliptica, Lonchocarpus utilis, and Tephrosia vogelii. It is used as a pesticide to control insects, mites, and fish in both agricultural and residential settings.

In medical contexts, rotenone has been studied for its potential effects on human health, particularly in relation to Parkinson's disease. Some research suggests that exposure to rotenone may increase the risk of developing Parkinson's disease, although more studies are needed to confirm this link. Rotenone works by inhibiting the mitochondria in cells, which can lead to cell death and neurodegeneration.

It is important to note that rotenone is highly toxic and should be handled with care. It can cause skin and eye irritation, respiratory problems, and gastrointestinal symptoms if ingested or inhaled. Therefore, it is recommended to use personal protective equipment when handling rotenone and to follow all label instructions carefully.

NADP (Nicotinamide Adenine Dinucleotide Phosphate) is a coenzyme that plays a crucial role as an electron carrier in various redox reactions in the human body. It exists in two forms: NADP+, which functions as an oxidizing agent and accepts electrons, and NADPH, which serves as a reducing agent and donates electrons.

NADPH is particularly important in anabolic processes, such as lipid and nucleotide synthesis, where it provides the necessary reducing equivalents to drive these reactions forward. It also plays a critical role in maintaining the cellular redox balance by participating in antioxidant defense mechanisms that neutralize harmful reactive oxygen species (ROS).

In addition, NADP is involved in various metabolic pathways, including the pentose phosphate pathway and the Calvin cycle in photosynthesis. Overall, NADP and its reduced form, NADPH, are essential molecules for maintaining proper cellular function and energy homeostasis.

Aspartate aminotransferase (AST), mitochondrial isoform, is an enzyme found primarily in the mitochondria of cells. It is involved in the transfer of an amino group from aspartic acid to alpha-ketoglutarate, resulting in the formation of oxaloacetate and glutamate. This enzyme plays a crucial role in the cellular energy production process, particularly within the mitochondria.

Elevated levels of AST, mitochondrial isoform, can be found in various medical conditions, including liver disease, muscle damage, and heart injury. However, it's important to note that most clinical laboratories measure a combined level of both cytosolic and mitochondrial AST isoforms when testing for this enzyme. Therefore, the specific contribution of the mitochondrial isoform may not be easily discernible in routine medical tests.

Glucose is a simple monosaccharide (or single sugar) that serves as the primary source of energy for living organisms. It's a fundamental molecule in biology, often referred to as "dextrose" or "grape sugar." Glucose has the molecular formula C6H12O6 and is vital to the functioning of cells, especially those in the brain and nervous system.

In the body, glucose is derived from the digestion of carbohydrates in food, and it's transported around the body via the bloodstream to cells where it can be used for energy. Cells convert glucose into a usable form through a process called cellular respiration, which involves a series of metabolic reactions that generate adenosine triphosphate (ATP)—the main currency of energy in cells.

Glucose is also stored in the liver and muscles as glycogen, a polysaccharide (multiple sugar) that can be broken down back into glucose when needed for energy between meals or during physical activity. Maintaining appropriate blood glucose levels is crucial for overall health, and imbalances can lead to conditions such as diabetes mellitus.

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.

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.

Tricarboxylic acids, also known as TCA cycle or citric acid cycle, 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 carbon dioxide and water in the form of ATP. This process is an important part of cellular respiration and occurs in the mitochondria. The cycle involves eight steps that result in the production of two molecules of ATP, reduced coenzymes NADH and FADH2, and the release of three molecules of carbon dioxide.

The tricarboxylic acids involved in this cycle are:

1. Citric acid (also known as citrate)
2. Cis-aconitic acid
3. Isocitric acid
4. Oxalosuccinic acid (an intermediate that is not regenerated)
5. α-Ketoglutaric acid (also known as alpha-ketoglutarate)
6. Succinyl-CoA
7. Succinic acid (also known as succinate)
8. Fumaric acid
9. Malic acid
10. Oxaloacetic acid (also known as oxalacetate)

These acids play a crucial role in the energy production and metabolism of living organisms.

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

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

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

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.

In the context of medical definitions, 'carbon' is not typically used as a standalone term. Carbon is an element with the symbol C and atomic number 6, which is naturally abundant in the human body and the environment. It is a crucial component of all living organisms, forming the basis of organic compounds, such as proteins, carbohydrates, lipids, and nucleic acids (DNA and RNA).

Carbon forms strong covalent bonds with various elements, allowing for the creation of complex molecules that are essential to life. In this sense, carbon is a fundamental building block of life on Earth. However, it does not have a specific medical definition as an isolated term.

Glutamate Dehydrogenase (GLDH or GDH) is a mitochondrial enzyme that plays a crucial role in the metabolism of amino acids, particularly within liver and kidney tissues. It catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate, which links amino acid metabolism with the citric acid cycle and energy production. This enzyme is significant in clinical settings as its levels in blood serum can be used as a diagnostic marker for diseases that damage liver or kidney cells, since these cells release GLDH into the bloodstream upon damage.

Gluconeogenesis is a metabolic pathway that occurs in the liver, kidneys, and to a lesser extent in the small intestine. It involves the synthesis of glucose from non-carbohydrate precursors such as lactate, pyruvate, glycerol, and certain amino acids. This process becomes particularly important during periods of fasting or starvation when glucose levels in the body begin to drop, and there is limited carbohydrate intake to replenish them.

Gluconeogenesis helps maintain blood glucose homeostasis by providing an alternative source of glucose for use by various tissues, especially the brain, which relies heavily on glucose as its primary energy source. It is a complex process that involves several enzymatic steps, many of which are regulated to ensure an adequate supply of glucose while preventing excessive production, which could lead to hyperglycemia.

Tartrates are salts or esters of tartaric acid, a naturally occurring organic acid found in many fruits, particularly grapes. In a medical context, potassium bitartrate (also known as cream of tartar) is sometimes used as a mild laxative or to treat acidosis by helping to restore the body's normal pH balance. Additionally, sodium tartrate has been historically used as an antidote for lead poisoning. However, these uses are not common in modern medicine.

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.

"Thermus" is not a medical term, but rather a genus of bacteria that are capable of growing in extreme temperatures. These bacteria are named after the Greek word "therme," which means heat. They are commonly found in hot springs and deep-sea hydrothermal vents, where the temperature can reach up to 70°C (158°F).

Some species of Thermus have been found to produce enzymes that remain active at high temperatures, making them useful in various industrial applications such as molecular biology and DNA amplification techniques like polymerase chain reaction (PCR). However, Thermus itself is not a medical term or concept.

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

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

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

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

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

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

"Ananas" is the common name for a tropical fruit that is also known as a pineapple. The term "ananas" comes from the Tupi language, which was spoken by indigenous people in what is now Brazil. When European explorers first encountered this fruit in South America, they adopted the Tupi word "nana," meaning "excellent fruit," and added the Greek prefix "an-" to mean "producing."

The medical or scientific definition of Ananas refers to the genus Ananas, which is a member of the Bromeliaceae family. The most common species in this genus is Ananas comosus, which is the pineapple that we are familiar with today.

Pineapples have several health benefits and are rich in vitamins, minerals, and antioxidants. They contain bromelain, a mixture of enzymes that has anti-inflammatory properties and can help with digestion. Pineapple is also an excellent source of vitamin C, manganese, and dietary fiber.

In summary, the medical definition of "Ananas" refers to the pineapple fruit and its genus Ananas, which belongs to the Bromeliaceae family. It has several health benefits due to its rich nutritional content, including bromelain, vitamin C, manganese, and dietary fiber.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Oxidative phosphorylation is the metabolic process by which cells use enzymes to generate energy in the form of adenosine triphosphate (ATP) from the oxidation of nutrients, such as glucose or fatty acids. This process occurs in the inner mitochondrial membrane of eukaryotic cells and is facilitated by the electron transport chain, which consists of a series of protein complexes that transfer electrons from donor molecules to acceptor molecules. As the electrons are passed along the chain, they release energy that is used to pump protons across the membrane, creating a gradient. The ATP synthase enzyme then uses the flow of protons back across the membrane to generate ATP, which serves as the main energy currency for cellular processes.

... s catalyzes the interconversion of malate to oxaloacetate. In the citric acid cycle, malate dehydrogenase ... L-malate binding to malate dehydrogenase is promoted at alkaline conditions. Consequently, the non-protonated form malate ... The ΔG'° of malate dehydrogenase is +29.7 kJ/mol and the ΔG (in the cell) is 0 kJ/mol. Malate dehydrogenase is also involved in ... Malate dehydrogenase (EC 1.1.1.37) (MDH) is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate using ...
The Our Lady of Remedies Parish, also known as Malate Church (Spanish: Iglesia Parroquial de Malate), is a parish church in the ... Except for a short time, Malate was always administered by the Augustinians. The priest of Malate also administered the town of ... Wikimedia Commons has media related to Malate Church. Website of Malate Church Coordinates (Use dmy dates from July 2019, ... Pasay separated from Malate under the name of Pineda on 17 May 1863. Malate was also a place of recreation for the residents of ...
... is discussed as being a more bioavailable form of magnesium, along with other forms such as citrate and ... Magnesium malate, the magnesium salt of malic acid, is a mineral supplement often used for nutritional concerns. It is ... "Magnesium Malate". Isotrope, Inc. 7 July 2017. Retrieved 8 September 2017. v t e (Articles needing additional references from ... Malates, Dietary supplements, All stub articles, Gastrointestinal system drug stubs). ...
... refers to organic compounds containing malate and ammonium. Two stoichiometries are discussed: NH4H(C2H3OH(CO2) ... As a food additive, diammonium malate has been used as flavoring agent and as an acidity regulator. It has the E number E349. ... 2) with one ammonium ion per formula unit, and (NH4)2(C2H3OH(CO2)2). Malate, the conjugate base of malic acid, is chiral. ... Ammonium malate". Journal of Crystal Growth. 310 (6): 1228-1238. Bibcode:2008JCrGr.310.1228A. doi:10.1016/j.jcrysgro.2007.12. ...
Media related to Malate, Manila at Wikimedia Commons Malate travel guide from Wikivoyage (Articles with short description, ... Prominent secondary schools in Malate are the Jesus Reigns Christian Academy, Jose Abad Santos Memorial School and the Malate ... In the 1990s, Malate and the nearby district of Ermita had been "cleaned-up" and big businesses and resort hotels have sprouted ... The name Malate is derived from a corruption of the Tagalog word maalat ("salty"). The name likely referred to the brackish ...
... is a compound with formula Ca(C2H4O(COO)2). It is the calcium salt of malic acid. As a food additive, it has the ... It is related to, but different from, calcium citrate malate. Commission directive 2000/63/EC of 5 October 2000 Official ... Malates, Calcium compounds, E-number additives, All stub articles, Organic compound stubs). ...
In enzymology, a malate oxidase (EC 1.1.3.3) is an enzyme that catalyzes the chemical reaction (S)-malate + O2 ⇌ {\displaystyle ... Malate oxidase belongs to the family of malate dehydrogenases (EC 1.1.1.37) (MDH) that reversibly catalyze the oxidation of ... In this case, malate oxidase is qualified as malate dehydrogenase (quinone). In mutant strains of Escherichia coli lacking the ... Malate oxidase is induced only in cells, which completely lack the activity of NAD-specific malate dehydrogenase. Irradiation ...
... malate condensing enzyme, malate synthetase, malic synthetase, and malic-condensing enzyme. Malate synthases fall into two ... Traditionally, malate synthases are described in bacteria as part of the glyoxylate cycle, and malate synthase activity had not ... The structure and kinetics of Mycobacterium tuberculosis malate synthase have been well categorized. Malate synthase is ... malate + CoA The 3 substrates of this enzyme are acetyl-CoA, H2O, and glyoxylate, whereas its two products are (S)-malate and ...
... is a compound with formula Na2(C2H4O(COO)2). It is the sodium salt of malic acid. As a food additive, it has the ... Sodium malate is an odorless white crystalline powder. It is freely soluble in water. It is used as an acidity regulator and ... Malates, Organic sodium salts, E-number additives, All stub articles, Organic compound stubs). ...
... is the salt that transports from the leaves to the root. At the root, the potassium malate oxidizes to ... Potassium malate is a compound with formula K2(C2H4O(COO)2). It is the potassium salt of malic acid. As a food additive, it has ... Malates, Potassium compounds, Food additives, E-number additives). ...
... malate and NAD+, whereas its three products are pyruvate, CO2, and NADH. Malate is oxidized to pyruvate and CO2, and NAD+ is ... Malate dehydrogenase (decarboxylating) (EC 1.1.1.39) or NAD-malic enzyme (NAD-ME) is an enzyme that catalyzes the chemical ... Saz HJ, Hubbard JA (1957). "The oxidative decarboxylation of malate by Ascaris lumbricoides". J. Biol. Chem. 225 (2): 921-933. ... The systematic name of this enzyme class is (S)-malate:NAD+ oxidoreductase (decarboxylating). This enzyme participates in ...
... (Paaralang Katoliko ng Malate or MCS) is a private catholic gender-isolated K to 12 school in Malate ... "There's a school by the Church of Malate That we honor with heart sincere; It's our own school and none could be better, To our ... 1992 Gabriel Reyes, then the Auxiliary Bishop of Manila launched the Madre Ignacia Movement, Malate chapter on March 1. On the ... 1588 The Augustinians from Spain established a mission in Malate under the advocacy of Our Lady of Remedies. 1596 The ...
Citrate also inhibits malate oxidation, but only at low malate or NAD concentrations. When both malate and NAD concentrations ... Malate dehydrogenase, mitochondrial also known as malate dehydrogenase 2 is an enzyme that in humans is encoded by the MDH2 ... Malate dehydrogenase catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in ... In addition, association of malate dehydrogenase with these other two enzymes enhances malate dehydrogenase activity due to a ...
Allen SH, Patil JR (1972). "Studies on the structure and mechanism of action of the malate-lactate transhydrogenase". J. Biol. ... In enzymology, a lactate-malate transhydrogenase (EC 1.1.99.7) is an enzyme that catalyzes the chemical reaction (S)-lactate + ... This enzyme is also called malate-lactate transhydrogenase. This enzyme participates in pyruvate metabolism. It employs one ... Allen SH (1966). "The isolation and characterization of malate-lactate transhydrogenase from Micrococcus lactilyticus". J. Biol ...
... at Jost Chemical "Calcium citrate malate as source for calcium for use in foods for Particular ... Calcium citrate malate is similar to calcium malate and other calcium salts. The European Food Safety Authority has concluded ... Calcium citrate malate is a water-soluble calcium supplement. It is the calcium salt of citric acid and malic acid with ... Calcium citrate malate's bioavailability stems from its water-solubility and its method of dissolution. When dissolved, it ...
Once malate is formed, the first antiporter (malate-alpha-ketoglutarate) imports the malate from the cytosol into the ... Malate dehydrogenase is present in two forms in the shuttle system: mitochondrial malate dehydrogenase and cytosolic malate ... The malate-aspartate shuttle (sometimes simply the malate shuttle) is a biochemical system for translocating electrons produced ... After malate reaches the mitochondrial matrix, it is converted by mitochondrial malate dehydrogenase into oxaloacetate, during ...
In enzymology, a malate-CoA ligase (EC 6.2.1.9) is an enzyme that catalyzes the chemical reaction ATP + malate + CoA ⇌ {\ ... The systematic name of this enzyme class is malate:CoA ligase (ADP-forming). Other names in common use include malyl-CoA ... displaystyle \rightleftharpoons } ADP + phosphate + malyl-CoA The 3 substrates of this enzyme are ATP, malate, and CoA, whereas ... synthetase, malyl coenzyme A synthetase, and malate thiokinase. This enzyme participates in glyoxylate and dicarboxylate ...
... malate NADP+ dehydrogenase, NADP+ malate dehydrogenase, NADP+-linked malate dehydrogenase, and malate dehydrogenase (NADP+). ... In enzymology, a malate dehydrogenase (NADP+) (EC 1.1.1.82) is an enzyme that catalyzes the chemical reaction (S)-malate + ... The systematic name of this enzyme class is (S)-malate:NADP+ oxidoreductase. Other names in common use include NADP+-malic ... Johnson HS (1971). "NADP-malate dehydrogenase: photoactivation in leaves of plants with Calvin cycle photosynthesis". Biochem. ...
Other names in common use include FAD-dependent malate-vitamin K reductase, malate-vitamin K reductase, and (S)-malate:(quinone ... In enzymology, a malate dehydrogenase (quinone) (EC 1.1.5.4), formerly malate dehydrogenase (acceptor) (EC 1.1.99.16), is an ... Imai D; Brodie AF (1973). "A phospholipid-requiring enzyme, malate-vitamin K reductase". J. Biol. Chem. 248: 7487-7494. Imai T ... Prasada Reddy TL, Suryanarayana Murthy P, Venkitasubramanian TA (1975). "Variations in the pathways of malate oxidation and ...
Malate dehydrogenase (decarboxylating) or NAD-malic enzyme Malate dehydrogenase (NADP+) Malate dehydrogenase (NAD(P)+) Malate ... or NADP-malic enzyme Malate dehydrogenase (quinone) D-malate dehydrogenase (decarboxylating) Malate dehydrogenase 2 This ... Malate dehydrogenase is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate using the reduction of NAD+ ... disambiguation page lists articles associated with the title Malate dehydrogenase. If an internal link led you here, you may ...
Malate would be transported by the malate shuttle, moving from cytosol to matrix. It is a highly efficient transport system. At ... The citrate-malate shuttle system consists of citrate shuttle and malate shuttle, which are carrier proteins. Carrier proteins ... Both citrate and malate involved in the citrate-malate shuttle are necessary intermediates of the Krebs cycle. Usually ... "MDH - malate dehydrogenase (thale cress)". pubchem.ncbi.nlm.nih.gov. Retrieved 2022-03-28. PubChem. "mMDH1 - Lactate/malate ...
In enzymology, a malate dehydrogenase (oxaloacetate-decarboxylating) (EC 1.1.1.38) is an enzyme that catalyzes the chemical ... The systematic name of this enzyme class is (S)-malate:NAD+ oxidoreductase (oxaloacetate-decarboxylating). Other names in ... malate and NAD+, whereas its 3 products are pyruvate, CO2, and NADH. This enzyme belongs to the family of oxidoreductases, ... reaction below (S)-malate + NAD+ ⇌ {\displaystyle \rightleftharpoons } pyruvate + CO2 + NADH Thus, the two substrates of this ...
Other names in common use include D-malate dehydrogenase, D-malic enzyme, bifunctional L(+)-tartrate dehydrogenase-D(+)-malate ... In enzymology, a D-malate dehydrogenase (decarboxylating) (EC 1.1.1.83) is an enzyme that catalyzes the chemical reaction (R)- ... The systematic name of this enzyme class is (R)-malate:NAD+ oxidoreductase (decarboxylating). ... malate and NAD+, whereas its 3 products are pyruvate, CO2, and NADH. This enzyme belongs to the family of oxidoreductases, ...
Other names in common use include 1-sinapoylglucose-L-malate sinapoyltransferase, and sinapoylglucose:malate ... malate Thus, the two substrates of this enzyme are 1-O-sinapoyl-beta-D-glucose and (S)-malate, whereas its two products are D- ... Strack D (June 1982). "Development of 1-O-sinapoyl-β-D-glucose: L-malate sinapoyltransferase activity in cotyledons of red ... In enzymology, a sinapoylglucose---malate O-sinapoyltransferase (EC 2.3.1.92) is an enzyme that catalyzes the chemical reaction ...
... (EC 1.1.1.299, MdH II, NAD(P)+-dependent malate dehyrogenase) is an enzyme with systematic name ... It is different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.5.4 ( ... S)-malate:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction (S)-malate + NAD(P)+ ⇌ {\displaystyle \ ... malate dehydrogenase (quinone)). Thompson H, Tersteegen A, Thauer RK, Hedderich R (July 1998). "Two malate dehydrogenases in ...
... malate and NADP+, whereas its 3 products are pyruvate, CO2, and NADPH. Malate is oxidized to pyruvate and CO2, and NADP+ is ... Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) (EC 1.1.1.40) or NADP-malic enzyme (NADP-ME) is an enzyme that ... C4 NADP-ME has been shown to be partially inhibited by its substrate, malate, suggesting two independent binding sites: one at ... 1. Conversion of malate into pyruvate". The Biochemical Journal. 73 (4): 646-54. doi:10.1042/bj0730646. PMC 1197115. PMID ...
"Almotriptan malate". Drug Information Portal. U.S. National Library of Medicine. Portal: Medicine (Articles with short ... "Axert- almotriptan malate tablet, coated". DailyMed. Retrieved 17 February 2021. "Active substance: almotriptan" (PDF). List of ...
11 p. Malate (2003). "ACID STIMULATION OF INJECTION WELLS IN THE LEYTE GEOTHERMAL POWER PROJECT, PHILIPPINES". Twenty-Second ... Malate, Ramonchito Cedric M. (2000). "SK-2D: A CASE HISTORY ON GEOTHERMAL WELLBORE ENHANCEMENT, MINDANAO GEOTHERMAL PRODUCTION ...
Malate. Orosa-Nakpil, Malate became a National Book Store Best Seller in April 2007.[citation needed] It has been featured in ... He is the author of the novel Orosa-Nakpil, Malate and is working as Assistant Professor of Medicine for the Hawaii Center for ... "Malate by night , Sunday Life, Lifestyle Features, The Philippine Star". philstar.com. 2009-04-19. Retrieved 2015-04-05. "TOP ... The English version of Orosa-Nakpil, Malate was released in September 2009 and the second edition of Gee My Grades Are Terrific ...
"Cabozantinib s-malate". NCI Drug Dictionary. National Cancer Institute. "Cabozantinib-S-Malate". National Cancer Institute. 19 ... Clinical trial number NCT01835158 for "Cabozantinib-s-malate or Sunitinib Malate in Treating Patients With Previously Untreated ... "Cabometyx cabozantinib (as (S)-malate) 20 mg film-coated tablet bottle (283800)". Therapeutic Goods Administration (TGA). 27 ...
Malate dehydrogenases catalyzes the interconversion of malate to oxaloacetate. In the citric acid cycle, malate dehydrogenase ... L-malate binding to malate dehydrogenase is promoted at alkaline conditions. Consequently, the non-protonated form malate ... The ΔG° of malate dehydrogenase is +29.7 kJ/mol and the ΔG (in the cell) is 0 kJ/mol. Malate dehydrogenase is also involved in ... Malate dehydrogenase (EC 1.1.1.37) (MDH) is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate using ...
S)-malate(2−) (CHEBI:15589) is a malate(2−) (CHEBI:15595) (S)-malate(2−) (CHEBI:15589) is conjugate base of (S)-malic acid ( ... sinapic acid (S)-malate ester (CHEBI:15596) has functional parent (S)-malate(2−) (CHEBI:15589). disodium (S)-malate (CHEBI: ... S)-malate(2−) (CHEBI:15589) has role Saccharomyces cerevisiae metabolite (CHEBI:75772) (S)-malate(2−) (CHEBI:15589) has role ... S)-malic acid (CHEBI:30797) is conjugate acid of (S)-malate(2−) (CHEBI:15589). (R)-malate(2−) (CHEBI:15588) is enantiomer of (S ...
This page contains brief information about sunitinib malate and a collection of links to more information about the use of this ... Sunitinib malate is approved to treat adults with:. *Gastrointestinal stromal tumor (a type of stomach cancer). It is used in ... More About Sunitinib Malate. Definition from the NCI Drug Dictionary - Detailed scientific definition and other names for this ... This page contains brief information about sunitinib malate and a collection of links to more information about the use of this ...
Find treatment reviews for Magnesium Malate from other patients. Learn from their experiences about effectiveness, side effects ... How do members experience Magnesium Malate?. Top 5 reported purposes & perceived effectiveness. Purpose. Patients. Evaluations ...
... Eur J Appl Physiol. 2010 Sep;110(2): ... Our aim was to evaluate the effects of diet supplementation with L-citrulline-malate prior to intense exercise on the metabolic ... Citrulline-malate ingestion significantly increased the plasma concentration of citrulline, arginine, ornithine, urea, ... Growth hormone increased after exercise in both groups, although the increase was higher in the citrulline-malate supplemented ...
The Torre Lorenzo Malate (TLM) development will host The Suites and lyf which will cater to the evolving needs of students, ... Since TLM is located in the heart of Malate, Ascott expects The Suites and lyf to cater to a healthy mix of students, ... On the other hand, lyf Malate Manila is a co-living property with 202 rooms. Ascott developed the lyf brand, which stands for " ... "Yes, there are hotels and condominiums there (in Malate), but no melting pot of short-stay and long-stay with both corporate ...
Natures Life Renewing Magnesium Malate -- 200 mg - 250 Tablets * Shop all Natures Life ...
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CanMED: NDC. The Cancer Medications Enquiry Database (CanMED) is a two-part resource for cancer drug treatment related studies.
Cells were treated with cisplatin (3, 6, 13, and 18 ,i,μ,/i,M) and sunitinib malate (1, 2, 4, 6, and 20 ,i ... In isolation, cisplatin and sunitinib malate statistically (). Autophagy and apoptosis studies showed a greater incidence when ... The aim of this paper is to analyse sunitinib malate ,i,in vitro,/i, ability to enhance cisplatin cytotoxicity in T24, 5637, ... μM of sunitinib malate. For flow cytometry assay, 3 μM cisplatin was combined with 1, 2, and 4 μM of sunitinib malate. ...
Timeline for Protein Malate oxidoreductase (malic enzyme) from c.2.1.7: Aminoacid dehydrogenase-like, C-terminal domain: * ... Lineage for Protein: Malate oxidoreductase (malic enzyme). *Root: SCOPe 2.08 *. Class c: Alpha and beta proteins (a/b) [51349 ... Protein Malate oxidoreductase (malic enzyme) from c.2.1.7: Aminoacid dehydrogenase-like, C-terminal domain first appeared in ... Protein Malate oxidoreductase (malic enzyme) from c.2.1.7: Aminoacid dehydrogenase-like, C-terminal domain appears in SCOPe ...
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... citrate/malate) is a highly bioavailable magnesium chelate. Featuring 240 mg of magnesium in each serving of two vegetarian ... citrate/malate) 90 19.99 //www.planetorganic.com/cdn/shop/products/Pure-Encapsulations-Magnesium-citrate-malate-90-29553_ ... Magnesium (citrate/malate) is a highly bioavailable magnesium chelate. Featuring 240 mg of magnesium in each serving of two ... Magnesium (citrate/malate) is a highly bioavailable magnesium chelate. Featuring 240 mg of magnesium in each serving of two ...
Crystal structure of human D-2-hydroxyglutarate dehydrogenase in complex with D-malate (D-MAL) ... This work reports the crystal structures of human D-2-HGDH in apo form and in complexes with D-2-HG, D-malate, D-lactate, L-2- ... D-MALATE. C4 H6 O5. BJEPYKJPYRNKOW-UWTATZPHSA-N. Ligand Interaction. ... Crystal structure of human D-2-hydroxyglutarate dehydrogenase in complex with D-malate (D-MAL). *PDB DOI: https://doi.org/ ...
Approach to Monitor Cardiac Metabolic Pathway Remodeling in Response to Sunitinib Malate PLoS One. 2017 Jan 27;12(1):e0169964. ...
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1.36 Angstrom Resolution Crystal Structure of Malate Synthase G from Pseudomonas aeruginosa in Complex with Glycolic Acid. ... 1.36 Angstrom Resolution Crystal Structure of Malate Synthase G from Pseudomonas aeruginosa in Complex with Glycolic Acid.. * ... 1.36 Angstrom Resolution Crystal Structure of Malate Synthase G from Pseudomonas aeruginosa in Complex with Glycolic Acid.. ...
Mag Malate RenewTM is a 100% pure combination of magnesium and malic acid. Malic acid is ionized in the body to form malate, ... AOR Mag Malate Renew, Magnesium is a mineral that is involved in over 300 biochemical processes in the body. One of its most ... Magnesium malate dihydrate - 793mg. Elemental magnesium - 100mg. Non-Medicinal Ingredients: microcrystalline cellulose, sodium ... This has been confirmed in several studies which have found that magnesium malate reduces the symptoms of fibromyalgia and ...
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Cabozantinib-s-malate and sunitinib malate may stop the growth of tumor cells by blocking some of the enzymes needed for cell ... Cabozantinib-s-malate or Sunitinib Malate in Treating Patients With Previously Untreated Locally Advanced or Metastatic Kidney ... It is not yet known whether cabozantinib-s-malate is more effective than sunitinib malate in treating patients with kidney ... This randomized phase II trial studies how well cabozantinib-s-malate works compared to sunitinib malate in treating patients ...
Abundance of Malate dehydrogenase [Mdh] on acetate medium & Pyridoxal phosphate phosphatase [YbhA] 3 d into stationary phase. ...
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A targeted proteomic multiplex CSF assay identifies increased malate dehydrogenase and other neurodegenerative biomarkers in ... malate dehydrogenase; total APOE; chitinase-3-like protein 1 (YKL-40); osteopontin and cystatin C. In an independent ... malate dehydrogenase; total APOE; chitinase-3-like protein 1 (YKL-40); osteopontin and cystatin C. In an independent ... A targeted proteomic multiplex CSF assay identifies increased malate dehydrogenase and other neurodegenerative biomarkers in ...
Guex, N.; Henry, H.; Flach, J.; Richter, H.; Widmer, F. 1995: Glyoxysomal malate dehydrogenase and malate synthase from soybean ... Using a cDNA clone for glyoxysomal malate synthase from cucumber cotyledons as a probe, it was shown that malate synthase gene ... Temporal changes in translatable mRNAs for isocitrate lyase and malate synthase European Journal of Biochemistry 112(3): 469- ... Henry, H.; Guex, N.; Widmer, F. 1992: Glyoxysomal malate dehydrogenase from soybean enzyme cluster and sequence of cdna clones ...
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  • Malate dehydrogenase (EC 1.1.1.37) (MDH) is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate using the reduction of NAD+ to NADH. (wikipedia.org)
  • Other malate dehydrogenases, which have other EC numbers and catalyze other reactions oxidizing malate, have qualified names like malate dehydrogenase (NADP+). (wikipedia.org)
  • Several isozymes of malate dehydrogenase exist. (wikipedia.org)
  • Humans and most other mammals express the following two malate dehydrogenases: The malate dehydrogenase family contains L-lactate dehydrogenase and L-2-hydroxyisocaproate dehydrogenases. (wikipedia.org)
  • In most organisms, malate dehydrogenase (MDH) exists as a homodimeric molecule and is closely related to lactate dehydrogenase (LDH) in structure. (wikipedia.org)
  • Because the sequence identity of malate dehydrogenase in the mitochondria is more closely related to its prokaryotic ancestors in comparison to the cytoplasmic isozyme, the theory that mitochondria and chloroplasts were developed through endosymbiosis is plausible. (wikipedia.org)
  • This indicates that there is a possible evolutionary linkage between lactate dehydrogenase and malate dehydrogenase. (wikipedia.org)
  • Each subunit of the malate dehydrogenase dimer has two distinct domains that vary in structure and functionality. (wikipedia.org)
  • Malate dehydrogenase has also been shown to have a mobile loop region that plays a crucial role in the enzyme's catalytic activity. (wikipedia.org)
  • Studies have also indicated that this loop region is highly conserved in malate dehydrogenase. (wikipedia.org)
  • The active site of malate dehydrogenase is a hydrophobic cavity within the protein complex that has specific binding sites for the substrate and its coenzyme, NAD+. (wikipedia.org)
  • Mechanistically, malate dehydrogenase catalyzes the oxidation of the hydroxyl group of malate by utilizing NAD+ as an electron acceptor. (wikipedia.org)
  • Studies have also identified a mobile loop in malate dehydrogenase that participates in the catalytic activity of the enzyme. (wikipedia.org)
  • The loop undergoes a conformational change to shield the substrate and catalytic amino acids from the solvent in response to the binding of the malate dehydrogenase:coenzyme complex to substrate. (wikipedia.org)
  • Light activation: Chloroplastic glyceraldehyde-3-phosphate dehydrogenase and malate dehydrogenase. (uic.edu)
  • Changes in activity of malate dehydrogenase and glucosephosphate isomerase in serum of rats exposed chronically to inorganic mercury and its aryl and alkyl compounds. (cdc.gov)
  • The Calcium Citrate Malate Market size is expected to reach US$ 484.3 million by 2030, from US$ 290 million in 2023, at a CAGR of 7.6% during the forecast period. (coherentmarketinsights.com)
  • Calcium citrate malate is a calcium supplement often derived from limestone or eggshells. (coherentmarketinsights.com)
  • The key drivers of the calcium citrate malate market include rising health consciousness, growing geriatric population, and increasing prevalence of bone disorders like osteoporosis. (coherentmarketinsights.com)
  • The Calcium Citrate Malate Market is segmented by product type, application, end-user, and region. (coherentmarketinsights.com)
  • North America is expected to be the largest market for Calcium Citrate Malate Market during the forecast period, accounting for over 41.2% of the market share in 2023. (coherentmarketinsights.com)
  • The Asia Pacific market is expected to be the second-largest market for Calcium Citrate Malate Market, accounting for over 28.7% of the market share in 2023. (coherentmarketinsights.com)
  • The Europe market is expected to be the fastest-growing market for Calcium Citrate Malate Market, with a CAGR of over 16.5% during the forecast period. (coherentmarketinsights.com)
  • The growth of the market in Europe is attributed to the growing adoption of preventive healthcare practices and increasing launches of calcium citrate malate products. (coherentmarketinsights.com)
  • The growing prevalence of bone health issues such as osteoporosis and osteopenia is a major factor driving growth of the calcium citrate malate market. (coherentmarketinsights.com)
  • Calcium citrate malate supplements can help improve bone mineral density and reduce the risk of fractures. (coherentmarketinsights.com)
  • The rising cases of bone health problems globally is creating significant demand for calcium supplements including calcium citrate malate. (coherentmarketinsights.com)
  • Calcium citrate malate is more soluble and bioavailable compared to other forms of calcium, making it an ideal choice. (coherentmarketinsights.com)
  • The shift towards preventive health is driving supplements sales, fueling growth of the calcium citrate malate market. (coherentmarketinsights.com)
  • The rapid growth of dietary supplements industry across the globe is creating significant opportunities for calcium supplement manufacturers including calcium citrate malate products. (coherentmarketinsights.com)
  • Calcium citrate malate is increasingly being used as a food additive in functional food and beverages to boost their calcium content. (coherentmarketinsights.com)
  • The rising demand for clean-label and organic ingredients is also favoring adoption of plant-derived calcium citrate malate in food & beverages, supporting market growth. (coherentmarketinsights.com)
  • Mag Malate RenewTM is a 100% pure combination of magnesium and malic acid. (purepharmacy.com)
  • Malic acid is ionized in the body to form malate, which is a key intermediate in the energy production cycle that makes ATP, the fuel that allows cells to function. (purepharmacy.com)
  • Source Naturals Magnesium Malate is a compound of magnesium and malic acid. (fullscript.com)
  • This type has been bound with malic acid , which is perhaps best known of as a beneficial component of apples and apple cider vinegar, to form Magnesium Malate. (avivahealth.com)
  • Pro Magnesium Malate contains magnesium and malic acid. (fullscript.com)
  • Mag-Malate tablets provide magnesium and malic acid, two key nutrients involved in energy production and muscular function. (atlantafunctionalmedicine.com)
  • The synergistic combination of L-citrulline amino acid and malic acid is L-citrulline malate. (ironbody.de)
  • Malic acid (malate) is an organic acid, which can be found in nature (for example in apple). (ironbody.de)
  • This randomized phase II trial studies how well cabozantinib-s-malate works compared to sunitinib malate in treating patients with previously untreated kidney cancer that has spread from where it started to nearby tissue or lymph nodes or to other places in the body. (mayo.edu)
  • It is not yet known whether cabozantinib-s-malate is more effective than sunitinib malate in treating patients with kidney cancer. (mayo.edu)
  • Cabozantinib-s-malate and sunitinib malate may stop the growth of tumor cells by blocking some of the enzymes needed for cell growth. (mayo.edu)
  • This randomized phase II trial studies how well cabozantinib s-malate and nivolumab work in treating patients with endometrial cancer that has come back (recurrent) or spread to other places in the body (advanced or metastatic). (ucsd.edu)
  • To evaluate the clinical anti-tumor activity of cabozantinib s-malate (XL184 ([cabozantinib]) and nivolumab based on progression free survival (PFS) in patients with advanced, recurrent or metastatic endometrial cancer previously treated with at least one line of platinum-based chemotherapy compared to patients receiving nivolumab alone. (ucsd.edu)
  • ARM A: Patients receive cabozantinib s-malate orally (PO) once daily (QD) on days 1-28 and nivolumab intravenously (IV) over 30 minutes on days 1 and 15, then on day 1 beginning cycle 5. (ucsd.edu)
  • Our aim was to evaluate the effects of diet supplementation with L-citrulline-malate prior to intense exercise on the metabolic handle of plasma amino acids and on the products of metabolism of arginine as creatinine, urea and nitrite and the possible effects on the hormonal levels. (nih.gov)
  • L-citrulline-malate supplementation can enhance the use of amino acids, especially the branched chain amino acids during exercise and also enhance the production of arginine-derived metabolites such as nitrite, creatinine, ornithine and urea. (nih.gov)
  • Citrulline malate supplementation has been shown to reduce post-workout muscle soreness for up to 48 hours in trained athletes, while also reducing the sensation and onset of muscle fatigue. (pharmafreak.com)
  • 793 mg Magnesium Malate Dihydrate , providing 100 mg of Elemental Magnesium. (avivahealth.com)
  • Seventeen voluntary male pre-professional cyclists were randomly assigned to one of two groups: control or supplemented (6 g L-citrulline-malate 2 h prior exercise) and participated in a 137-km cycling stage. (nih.gov)
  • Mix One Serving Of Citrulline Malate In 8-12 Ounces Of Your Favorite Beverages, Pre-Workout Or Post-Workout. (nutritionwholesalers.com)
  • For Optimal Results, Consume Citrulline Malate Daily Before Exercise And Combined With Condense, Stimpact And/Or Noxygen. (nutritionwholesalers.com)
  • Like all BioTech USA products, Citrulline Malate powder consists of safe and carefully selected ingredients. (ironbody.de)
  • AOR Mag Malate Renew, Magnesium is a mineral that is involved in over 300 biochemical processes in the body. (purepharmacy.com)
  • There's also a whole other demographic that might be interested in giving Mag Malate Renew a try: athletes! (avivahealth.com)
  • On the other hand, lyf Malate Manila is a co-living property with 202 rooms. (bworldonline.com)
  • Sunitinib malate is an orally bioavailable molecule with the ability to block the intracellular tyrosine kinase domain of tyrosine kinase receptors. (hindawi.com)
  • Magnesium (citrate/malate) is a highly bioavailable magnesium chelate. (planetorganic.com)
  • Magnesium Malate, Threonate, AA Chelate is an oral powder drug that contains 200 mg/scoop. (imedix.com)
  • This work reports the crystal structures of human D-2-HGDH in apo form and in complexes with D-2-HG, D-malate, D-lactate, L-2-HG, and 2-oxoglutarate, respectively. (rcsb.org)
  • therefore ultimately yield formate, glycine, malate, C2H6O2 inhalation of ambient air, ingestion of carbon dioxide and oxalic acid. (cdc.gov)
  • Purification and functional characterization of the vacuolar malate transporter tDT from Arabidopsis . (bvsalud.org)
  • This investigation aims to analyse the in vitro effects of cisplatin and sunitinib malate in isolation and in combination, on one human nonmuscle invasive urinary bladder-cancer cell line (5637) and on two human muscle-invasive urinary bladder-cancer cell lines (T24 and HT1376). (hindawi.com)
  • This has been confirmed in several studies which have found that magnesium malate reduces the symptoms of fibromyalgia and chronic fatigue such as muscle pain and brain fog. (purepharmacy.com)
  • Low levels of ATP have been associated with both fibromyalgia and chronic fatigue, and there is some evidence of mitochondrial dysfunction in those with ME/CFS (Myalgic Encephalomyelitis/Chronic Fatigue Syndrome), and these may be underlying factors in the low energy levels, persistent fatigue, brain fog, and muscle pains associated with those conditions, which magnesium malate may be able to help with. (avivahealth.com)
  • Calcium malate is a compound with formula Ca(C2H4O(COO)2). (mubychem.in)
  • Find Clinical Trials for Sunitinib Malate - Check for trials from NCI's list of cancer clinical trials now accepting patients. (cancer.gov)
  • BARCELONA, Spain--(HSMN NewsFeed)--Pfizer announced today the initiation of a Phase III clinical trial to evaluate the safety and efficacy of sunitinib malate, in combination with a standard chemotherapy regimen, in patients with metastatic colorectal cancer (mCRC) - cancer originating in the colon that has spread to other parts of the body. (salesandmarketingnetwork.com)
  • In addition, new data from a Phase I study being presented this week at the World Congress on Gastrointestinal Cancer (WCGC) in Barcelona showed that sunitinib malate is active and generally well-tolerated in combination with a standard chemotherapy regimen, FOLFIRI, in previously untreated patients with mCRC. (salesandmarketingnetwork.com)
  • A multi-national Phase III study is currently open and enrolling in Europe, Canada, Asia and South America and will include more than 700 patients to evaluate the safety and efficacy of sunitinib malate combined with FOLFIRI, a standard chemotherapy regimen used in mCRC comprised of fluorouracil (5-FU), folinic acid ( Leucovorin ), and irinotecan, compared with FOLFIRI plus placebo, in the first-line treatment of patients with mCRC. (salesandmarketingnetwork.com)
  • New data presented this week from an ongoing, open-label Phase I trial of 16 previously untreated mCRC patients randomized to three distinct dosing regimens, determined the maximum tolerated dose (MTD) for sunitinib malate of four weeks on treatment followed by two weeks off (4/2) in combination with FOLFIRI was 37.5 mg/day. (salesandmarketingnetwork.com)
  • Treatment emergent grade greater than or equal to 3 adverse events for patients on the sunitinib malate 37.5 mg/day 4/2 regimen were one case of respiratory tract infection and two cases of neutropenia without fever. (salesandmarketingnetwork.com)
  • These data support further research of sunitinib malate in metastatic colorectal cancer, in an effort to potentially expand the range of therapies available to physicians and patients. (salesandmarketingnetwork.com)
  • Although the classic boot-shaped heart ( coeur en sabot ) is the hallmark of the disorder in infants, this shape of the heart may not be seen in adult patients. (medscape.com)
  • Direct assays of enzyme activity and immunological tests indicated that the regulation of malate synthase was brought about by changes in the number of gene transcripts for the enzyme rather than through a control of translation. (eurekamag.com)
  • One is found in the mitochondrial matrix, participating as a key enzyme in the citric acid cycle that catalyzes the oxidation of malate. (wikipedia.org)
  • The researchers focused on three drugs used to treat kidney cancer: sorafenib (Nexavar), sunitinib malate (Sutent), and pazopanib hydrochloride (Votrient). (medscape.com)
  • All complexes were found to adopt supramolecular stratified structures made of alternating layers of poly(β,L-malate) and surfactant with a periodicity on the length scale of 3-5 nm, which increased proportionally to the length of the polymethylene chain. (uni-regensburg.de)
  • 2) the malate-aspartate shuttle, which involves taking apart NADH molecules so they can be reassembled in the mitochondria of cells in the heart and liver to produce more energy. (avivahealth.com)
  • The other is found in the cytoplasm, assisting the malate-aspartate shuttle with exchanging reducing equivalents so that malate can pass through the mitochondrial membrane to be transformed into oxaloacetate for further cellular processes. (wikipedia.org)
  • This page contains brief information about sunitinib malate and a collection of links to more information about the use of this drug, research results, and ongoing clinical trials. (cancer.gov)
  • For more information about sunitinib malate trials currently open and enrolling, please visit www.ClinicalTrials.gov or www.suntrials.com or call Pfizer Oncology's toll-free number at 001-646-277-4066. (salesandmarketingnetwork.com)
  • An optically active form of malate having ( S )-configuration. (ebi.ac.uk)
  • 5VFB: 1.36 Angstrom Resolution Crystal Structure of Malate Synthase G from Pseudomonas aeruginosa in Complex with Glycolic Acid. (rcsb.org)
  • We are encouraged by these data, which add to a growing body of research demonstrating the activity and tolerability of sunitinib malate in numerous cancers," said Charles Baum, MD PhD, head of oncology development at Pfizer. (salesandmarketingnetwork.com)