An NAD+ dependent enzyme that catalyzes the oxidation of betain aldehyde to BETAINE.
A naturally occurring compound that has been of interest for its role in osmoregulation. As a drug, betaine hydrochloride has been used as a source of hydrochloric acid in the treatment of hypochlorhydria. Betaine has also been used in the treatment of liver disorders, for hyperkalemia, for homocystinuria, and for gastrointestinal disturbances. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1341)
Oxidoreductases that are specific for ALDEHYDES.
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.
An enzyme bound to the inner mitochondrial membrane that catalyzes the oxidation of CHOLINE to BETAINE.
A plant genus in the CHENOPODIACEAE family.
A basic constituent of lecithin that is found in many plants and animal organs. It is important as a precursor of acetylcholine, as a methyl donor in various metabolic processes, and in lipid metabolism.
Organic compounds containing a carbonyl group in the form -CHO.
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 carbamate derivative used as an alcohol deterrent. It is a relatively nontoxic substance when administered alone, but markedly alters the intermediary metabolism of alcohol. When alcohol is ingested after administration of disulfiram, blood acetaldehyde concentrations are increased, followed by flushing, systemic vasodilation, respiratory difficulties, nausea, hypotension, and other symptoms (acetaldehyde syndrome). It acts by inhibiting aldehyde dehydrogenase.
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 colorless, flammable liquid used in the manufacture of acetic acid, perfumes, and flavors. It is also an intermediate in the metabolism of alcohol. It has a general narcotic action and also causes irritation of mucous membranes. Large doses may cause death from respiratory paralysis.
A metalloflavoprotein enzyme involved the metabolism of VITAMIN A, this enzyme catalyzes the oxidation of RETINAL to RETINOIC ACID, using both NAD+ and FAD coenzymes. It also acts on both the 11-trans- and 13-cis-forms of RETINAL.
A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
A widely cultivated plant, native to Asia, having succulent, edible leaves eaten as a vegetable. (From American Heritage Dictionary, 1982)
A cyanide compound which has been used as a fertilizer, defoliant and in many manufacturing processes. It often occurs as the calcium salt, sometimes also referred to as cyanamide. The citrated calcium salt is used in the treatment of alcoholism.

The choline-converting pathway in Staphylococcus xylosus C2A: genetic and physiological characterization. (1/30)

A Staphylococcus xylosus C2A gene cluster, which encodes enzymes in the pathway for choline uptake and dehydrogenation (cud), to form the osmoprotectant glycine betaine, was identified. The cud locus comprises four genes, three of which encode proteins with significant similarities to those known to be involved in choline transport and conversion in other organisms. The physiological role of the gene products was confirmed by analysis of cud deletion mutants. The fourth gene possibly codes for a regulator protein. Part of the gene cluster was shown to be transcriptionally regulated by choline and elevated NaCl concentrations as inducers.  (+info)

Genes for the synthesis of the osmoprotectant glycine betaine from choline in the moderately halophilic bacterium Halomonas elongata DSM 3043, USA. (2/30)

The genes involved in the oxidative pathway of choline to glycine betaine in the moderate halophile Halomonas elongata DSM 3043 were isolated by functional complementation of an Escherichia coli strain defective in glycine betaine synthesis. The cloned region was able to mediate the oxidation of choline to glycine betaine in E. coli, but not the transport of choline, indicating that the gene(s) involved in choline transport are not clustered with the glycine betaine synthesis genes. Nucleotide sequence analysis of a 4.6 kb segment from the cloned DNA revealed the occurrence of three ORFs (betIBA) apparently arranged in an operon. The deduced betI gene product exhibited features typical for DNA-binding regulatory proteins. The deduced BetB and BetA proteins showed significant similarity to soluble glycine betaine aldehyde dehydrogenases and membrane-bound choline dehydrogenases, respectively, from a variety of organisms. Evidence is presented that BetA is able to oxidize both choline and glycine betaine aldehyde and therefore can mediate both steps in the synthesis of glycine betaine.  (+info)

Steady-state kinetic mechanism of the NADP+- and NAD+-dependent reactions catalysed by betaine aldehyde dehydrogenase from Pseudomonas aeruginosa. (3/30)

Betaine aldehyde dehydrogenase (BADH) catalyses the irreversible oxidation of betaine aldehyde to glycine betaine with the concomitant reduction of NAD(P)(+) to NADP(H). In Pseudomonas aeruginosa this reaction is a compulsory step in the assimilation of carbon and nitrogen when bacteria are growing in choline or choline precursors. The kinetic mechanisms of the NAD(+)- and NADP(+)-dependent reactions were examined by steady-state kinetic methods and by dinucleotide binding experiments. The double-reciprocal patterns obtained for initial velocity with NAD(P)(+) and for product and dead-end inhibition establish that both mechanisms are steady-state random. However, quantitative analysis of the inhibitions, and comparison with binding data, suggest a preferred route of addition of substrates and release of products in which NAD(P)(+) binds first and NAD(P)H leaves last, particularly in the NADP(+)-dependent reaction. Abortive binding of the dinucleotides, or their analogue ADP, in the betaine aldehyde site was inferred from total substrate inhibition by the dinucleotides, and parabolic inhibition by NADH and ADP. A weak partial uncompetitive substrate inhibition by the aldehyde was observed only in the NADP(+)-dependent reaction. The kinetics of P. aeruginosa BADH is very similar to that of glucose-6-phosphate dehydrogenase, suggesting that both enzymes fulfil a similar amphibolic metabolic role when the bacteria grow in choline and when they grow in glucose.  (+info)

Overproduction of spinach betaine aldehyde dehydrogenase in Escherichia coli. Structural and functional properties of wild-type, mutants and E. coli enzymes. (4/30)

Betaine aldehyde dehydrogenase (BADH) catalyzes the last step in the synthesis of the osmoprotectant glycine betaine from choline. Although betaine aldehyde has been thought to be a specific substrate for BADH, recent studies have shown that human and sugar beet BADHs also catalyze the oxidation of omega-aminoaldehydes. To characterize the kinetic and stability properties of spinach BADH, five kinds of expression vectors encoding full length, mature, E103Q, E103K, and chimera BADHs were constructed. These enzymes together with Escherichia coli BADH were expressed in E. coli and purified. The affinities for betaine aldehyde were similar in the spinach and E. coli BADHs, whereas those for omega-aminoaldehydes were higher in spinach BADH than in E. coli BADH. A chimera BADH in which part of the Rossmann type fold in the spinach BADH was replaced with that of E. coli BADH, showed properties which resembled spinach BADH more than E. coli BADH. The spinach E103K mutant was almost inactive, whereas the E103Q mutant showed a similar activity for the oxidation of betaine aldehyde to that of wild type BADH, but a lower affinity for omega-aminoaldehydes. All spinach BADHs were dimers whereas E. coli BADH was a tetramer. E. coli BADH was more stable at high temperature than spinach BADHs. The E103Q mutant was most labile to high temperature. These properties are discussed in relation to the structure of spinach BADH.  (+info)

Isolation of a choline monooxygenase cDNA clone from Amaranthus tricolor and its expressions under stress conditions. (5/30)

Plants synthesize the osmoprotectant glycine betaine (GB) via choline-->betaine aldehyde-->glycine betaine[1]. Two enzymes are involved in the pathway, choline monooxygenase (CMO) and betaine aldehyde dehydrogenase (BADH). A full length CMO cDNA (1,643bp) was cloned from Amaranthus tricolor. The open reading frame encoded a 442-amino acid polypeptide, which showed 69% identity with CMOs in Spinacia oleracea L. and Beta vulgaris L. DNA gel blot analysis indicated the presence of one copy of CMO gene in the A. tricolor genome. The expressions of CMO and BADH proteins in A.tricolor leaves significantly increased under salinization, drought and heat stress (42 degrees C), as determined by immunoblot analysis, but did not respond to cold stress (4 degrees C), or exogenous ABA application. The increase of GB content in leaves was parallel to CMO and BADH contents.  (+info)

Modulation of the reactivity of the essential cysteine residue of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa. (6/30)

Betaine aldehyde dehydrogenase (BADH) catalyses the irreversible NAD(P)(+)-dependent oxidation of betaine aldehyde to glycine betaine. In the human opportunistic pathogen Pseudomonas aeruginosa this reaction is an obligatory step in the assimilation of carbon and nitrogen when bacteria are growing in choline or choline precursors. As with every aldehyde dehydrogenase studied so far, BADH possesses an essential cysteine residue involved in the formation of the intermediate thiohemiacetal with the aldehyde substrate. We report here that the chemical modification of this residue is conveniently measured by the loss in enzyme activity, which allowed us to explore its reactivity in a pH range around neutrality. The pH dependence of the observed second-order rate constant of BADH inactivation by methyl methanethiosulphonate (MMTS) suggests that at low pH values the essential cysteine residue exists as thiolate by the formation of an ion pair with a positively charged residue. The estimated macroscopic pK values are 8.6 and 4.0 for the free and ion-pair-forming thiolate respectively. The reactivity towards MMTS of both thiolate forms is notably lower than that of model compounds of similar pK, suggesting a considerable steric inhibition by the structure of the protein. Binding of the dinucleotides rapidly induced a significant and transitory increment of thiolate reactivity, followed by a relatively slow change to an almost unreactive form. Thus it seems that to gain protection against oxidation without compromising catalytic efficiency, BADH from P. aeruginosa has evolved a complex and previously undescribed mechanism, involving several conformational rearrangements of the active site, to suit the reactivity of the essential thiol to the availability of coenzyme and substrate.  (+info)

Isolating the promoter of a stress-induced gene encoding betaine aldehyde dehydrogenase from the halophyte Atriplex centralasiatica Iljin. (7/30)

The betaine aldehyde dehydrogenase (AcBADH) gene of the halophyte Atriplex centralasiatica Iljin is induced by drought, salinity, cold stress and abscisic acid, in parallel with an increase in betaine level. In order to study the molecular basis of its expression and to obtain an effective stress-induced promoter, the 5' flanking region of betaine aldehyde dehydrogenase gene (about 1.2 kb) was isolated from the halophyte A. centralasiatica Iljin by screening the genomic library. The transcription start site, which localized at 84 bases upstream of the start ATG, was determined by primer extension and 5'-RACE method. To investigate the molecular mechanism of the stress-induced gene regulation, the AcBADH promoter-beta-glucuronidase chimeric gene constructs containing six deletions were introduced into tobacco by Agrobacterium-mediated transformation. The AcBADH 5'-flanking region, a promoter strongly induced by salt stress, contains two salt-responsive enhancer regions localized between -1115 and -890, -462 and -230 and one silencer region between -890 and -641.  (+info)

The Sinorhizobium meliloti glycine betaine biosynthetic genes (betlCBA) are induced by choline and highly expressed in bacteroids. (8/30)

The symbiotic soil bacterium Sinorhizobium meliloti has the capacity to synthesize the osmoprotectant glycine betaine from choline-O-sulfate and choline. This pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). Here, we report that betICBA genes constitute a single operon, despite the existence of intergenic regions containing mosaic elements between betI and betC, and betB and betA. The regulation of the bet operon was investigated by using transcriptional lacZ (beta-galactosidase) fusions and has revealed a strong induction by choline at concentrations as low as 25 microM and to a lesser extent by choline-O-sulfate and acetylcholine but not by osmotic stress or oxygen. BetI is a repressor of the bet transcription in the absence of choline, and a nucleotide sequence of dyad symmetry upstream of betI was identified as a putative betI box. Measurements of intracellular pools of choline, well correlated with beta-galactosidase activities, strongly suggested that BetI senses the endogenous choline pool that modulates the intensity of BetI repression. In contrast to Escherichia coli, BetI did not repress choline transport. During symbiosis with Medicago sativa, S. meliloti bet gene expression was observed within the infection threads, in young and in mature nodules. The existence of free choline in nodule cytosol, peribacteroid space, and bacteroids was demonstrated, and the data suggest that bet regulation in planta is mediated by BetI repression, as in free-living cells. Neither Nod nor Fix phenotypes were significantly impaired in a betI::omega mutant, indicating that glycine betaine biosynthesis from choline is not crucial for nodulation and nitrogen fixation.  (+info)

Betaine-aldehyde dehydrogenase (BADH) is an enzyme involved in the metabolic pathway of betaine, a compound that helps protect cells from environmental stress and is important for maintaining cell volume and osmotic balance. The enzyme catalyzes the conversion of betaine aldehyde to betaine, using NAD+ as a cofactor.

Deficiency in BADH has been associated with certain genetic disorders, such as hyperbetalipoproteinemia type I, which is characterized by elevated levels of lipids and lipoproteins in the blood. Additionally, mutations in the BADH gene have been linked to an increased risk of alcoholism and alcohol-related disorders.

Betaine, also known as trimethylglycine, is a naturally occurring compound that can be found in various foods such as beets, spinach, and whole grains. In the body, betaine functions as an osmolyte, helping to regulate water balance in cells, and as a methyl donor, contributing to various metabolic processes including the conversion of homocysteine to methionine.

In medical terms, betaine is also used as a dietary supplement and medication. Betaine hydrochloride is a form of betaine that is sometimes used as a supplement to help with digestion by providing additional stomach acid. Betaine anhydrous, on the other hand, is often used as a supplement for improving athletic performance and promoting liver health.

Betaine has also been studied for its potential role in protecting against various diseases, including cardiovascular disease, diabetes, and neurological disorders. However, more research is needed to fully understand its mechanisms of action and therapeutic potential.

Aldehyde oxidoreductases are a class of enzymes that catalyze the oxidation of aldehydes to carboxylic acids using NAD+ or FAD as cofactors. They play a crucial role in the detoxification of aldehydes generated from various metabolic processes, such as lipid peroxidation and alcohol metabolism. These enzymes are widely distributed in nature and have been identified in bacteria, yeast, plants, and animals.

The oxidation reaction catalyzed by aldehyde oxidoreductases involves the transfer of electrons from the aldehyde substrate to the cofactor, resulting in the formation of a carboxylic acid and reduced NAD+ or FAD. The enzymes are classified into several families based on their sequence similarity and cofactor specificity.

One of the most well-known members of this family is alcohol dehydrogenase (ADH), which catalyzes the oxidation of alcohols to aldehydes or ketones as part of the alcohol metabolism pathway. Another important member is aldehyde dehydrogenase (ALDH), which further oxidizes the aldehydes generated by ADH to carboxylic acids, thereby preventing the accumulation of toxic aldehydes in the body.

Deficiencies in ALDH enzymes have been linked to several human diseases, including alcoholism and certain types of cancer. Therefore, understanding the structure and function of aldehyde oxidoreductases is essential for developing new therapeutic strategies to treat these conditions.

Aldehyde dehydrogenase (ALDH) is a class of enzymes that play a crucial role in the metabolism of alcohol and other aldehydes in the body. These enzymes catalyze the oxidation of aldehydes to carboxylic acids, using nicotinamide adenine dinucleotide (NAD+) as a cofactor.

There are several isoforms of ALDH found in different tissues throughout the body, with varying substrate specificities and kinetic properties. The most well-known function of ALDH is its role in alcohol metabolism, where it converts the toxic aldehyde intermediate acetaldehyde to acetate, which can then be further metabolized or excreted.

Deficiencies in ALDH activity have been linked to a number of clinical conditions, including alcohol flush reaction, alcohol-induced liver disease, and certain types of cancer. Additionally, increased ALDH activity has been associated with chemotherapy resistance in some cancer cells.

Choline dehydrogenase is an enzyme that plays a role in the metabolism of choline, a nutrient that is essential for the normal functioning of cells. Specifically, choline dehydrogenase helps to catalyze the oxidation of choline to betaine aldehyde, which is then further metabolized to betaine. This reaction is an important step in the conversion of choline to a molecule called glycine betaine, which helps to regulate cell volume and protect cells from osmotic stress. Choline dehydrogenase is found in various tissues throughout the body, including the liver, kidneys, and brain. Deficiencies in choline or dysfunction of choline dehydrogenase can lead to a variety of health problems, including fatty liver disease, muscle damage, and neurological disorders.

"Atriplex" is a genus of plants that belongs to the family Chenopodiaceae. It includes several species commonly known as saltbushes or orache. These plants are native to various parts of the world, including North America, Europe, and Asia. They are often found in salty or alkaline soils and have a tolerance for drought conditions. Some species of Atriplex are used for food, medicine, or as ornamental plants. However, I am not aware of any specific medical definition associated with the term "Atriplex." If you have more context or information about how this term is being used in a medical sense, I would be happy to help further!

Choline is an essential nutrient that is vital for the normal functioning of all cells, particularly those in the brain and liver. It is a water-soluble compound that is neither a vitamin nor a mineral, but is often grouped with vitamins because it has many similar functions. Choline is a precursor to the neurotransmitter acetylcholine, which plays an important role in memory, mood, and other cognitive processes. It also helps to maintain the structural integrity of cell membranes and is involved in the transport and metabolism of fats.

Choline can be synthesized by the body in small amounts, but it is also found in a variety of foods such as eggs, meat, fish, nuts, and cruciferous vegetables. Some people may require additional choline through supplementation, particularly if they follow a vegetarian or vegan diet, are pregnant or breastfeeding, or have certain medical conditions that affect choline metabolism.

Deficiency in choline can lead to a variety of health problems, including liver disease, muscle damage, and neurological disorders. On the other hand, excessive intake of choline can cause fishy body odor, sweating, and gastrointestinal symptoms such as diarrhea and vomiting. It is important to maintain adequate levels of choline through a balanced diet and, if necessary, supplementation under the guidance of a healthcare professional.

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

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

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

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.

Disulfiram is a medication used to treat chronic alcoholism. It works by inhibiting the enzyme acetaldehyde dehydrogenase, which is responsible for breaking down acetaldehyde, a toxic metabolite produced when alcohol is consumed. When a person taking disulfiram consumes alcohol, the buildup of acetaldehyde causes unpleasant symptoms such as flushing, nausea, palpitations, and shortness of breath, which can help discourage further alcohol use.

The medical definition of Disulfiram is:

A medication used in the treatment of chronic alcoholism, which works by inhibiting the enzyme acetaldehyde dehydrogenase, leading to an accumulation of acetaldehyde when alcohol is consumed, causing unpleasant symptoms that discourage further alcohol use. Disulfiram is available as a tablet for oral administration and is typically prescribed under medical supervision due to its potential for serious interactions with alcohol and other substances.

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.

Acetaldehyde is a colorless, volatile, and flammable liquid with a pungent odor. It is the simplest aldehyde, with the formula CH3CHO. Acetaldehyde is an important intermediate in the metabolism of alcohol and is produced by the oxidation of ethanol by alcohol dehydrogenase. It is also a naturally occurring compound that is found in small amounts in various foods and beverages, such as fruits, vegetables, and coffee.

Acetaldehyde is a toxic substance that can cause a range of adverse health effects, including irritation of the eyes, nose, and throat, nausea, vomiting, and headaches. It has been classified as a probable human carcinogen by the International Agency for Research on Cancer (IARC). Long-term exposure to acetaldehyde has been linked to an increased risk of certain types of cancer, including cancers of the oral cavity, esophagus, and liver.

Retinal dehydrogenase, also known as Aldehyde Dehydrogenase 2 (ALDH2), is an enzyme involved in the metabolism of alcohol and other aldehydes in the body. In the eye, retinal dehydrogenase plays a specific role in the conversion of retinaldehyde to retinoic acid, which is an important molecule for the maintenance and regulation of the visual cycle and overall eye health.

Retinoic acid is involved in various physiological processes such as cell differentiation, growth, and survival, and has been shown to have a protective effect against oxidative stress in the retina. Therefore, retinal dehydrogenase deficiency or dysfunction may lead to impaired visual function and increased susceptibility to eye diseases such as age-related macular degeneration and diabetic retinopathy.

Alcohol dehydrogenase (ADH) is a group of enzymes responsible for catalyzing the oxidation of alcohols to aldehydes or ketones, and reducing equivalents such as NAD+ to NADH. In humans, ADH plays a crucial role in the metabolism of ethanol, converting it into acetaldehyde, which is then further metabolized by aldehyde dehydrogenase (ALDH) into acetate. This process helps to detoxify and eliminate ethanol from the body. Additionally, ADH enzymes are also involved in the metabolism of other alcohols, such as methanol and ethylene glycol, which can be toxic if allowed to accumulate in the body.

"Spinacia oleracea" is the scientific name for a plant species, not a medical term. It is commonly known as spinach, a leafy green vegetable. While spinach has many health benefits and is often recommended as part of a balanced diet, it does not have a specific medical definition.

Spinach is rich in various nutrients such as iron, calcium, vitamin A, vitamin C, and folic acid. It can contribute to overall health, support immune function, and provide antioxidant benefits. However, it is important to note that 'Spinacia oleracea' itself does not have a medical definition.

Cyanamide is a chemical compound with the formula NH2CN. It is a colorless, crystalline solid that is highly soluble in water and has an ammonia-like odor. Cyanamide is used as a reagent in organic synthesis and as a fertilizer.

In a medical context, cyanamide may be used as a drug to treat certain conditions. For example, it has been used as a muscle relaxant and to reduce muscle spasms in people with multiple sclerosis. It is also being studied as a potential treatment for alcohol dependence, as it may help to reduce cravings and withdrawal symptoms.

It is important to note that cyanamide can be toxic in high doses, and it should only be used under the supervision of a healthcare professional.

In enzymology, a betaine-aldehyde dehydrogenase (EC 1.2.1.8) is an enzyme that catalyzes the chemical reaction betaine aldehyde ... Other names in common use include betaine aldehyde oxidase, BADH, betaine aldehyde dehydrogenase, and BetB. This enzyme ... ROTHSCHILD HA, BARRON ES (1954). "The oxidation of betaine aldehyde by betaine aldehyde dehydrogenase". J. Biol. Chem. 209 (2 ... Eklund H; El-Ahmad, M; Ramaswamy, S; Hjelmqvist, L; Jörnvall, H; Eklund, H (1998). "Structure of betaine aldehyde dehydrogenase ...
The human aldehyde dehydrogenase (EC 1.2.1.3) stimulates the transformation of betaine aldehyde to glycine betaine. Betaine ... aldehyde is a substrate for choline dehydrogenase (mitochondrial). Glycine betaine aldehyde is a short chain aldehyde and ... Glycine betaine aldehyde, often simply called betaine aldehyde, is an intermediate in the metabolism of glycine, serine and ... stress tolerance in Escherichia coli and Nicotiana tabacum expressing a betaine aldehyde dehydrogenase/choline dehydrogenase ...
This is oxidized by mitochondrial or cytosolic betaine-aldehyde dehydrogenases to trimethylglycine. Trimethylglycine is a ... In humans, choline is oxidized irreversibly in liver mitochondria to glycine betaine aldehyde by choline oxidases. ... April 2019). "Dietary choline and betaine intakes and risk of total and lethal prostate cancer in the Atherosclerosis Risk in ... Zeisel SH, Mar MH, Howe JC, Holden JM (May 2003). "Concentrations of choline-containing compounds and betaine in common foods ...
Betaine aldehyde is further oxidised in the mitochondria in mice to betaine by the enzyme betaine-aldehyde dehydrogenase (EC ... In humans betaine aldehyde activity is performed by a nonspecific cystosolic aldehyde dehydrogenase enzyme (EC 1.2.1.3) ... "BRENDA - Information on EC 1.2.1.8 - betaine-aldehyde dehydrogenase". Brenda-enzymes.org. Archived from the original on 29 June ... Chern, M. K.; Pietruszko, R. (1999). "Evidence for mitochondrial localization of betaine aldehyde dehydrogenase in rat liver: ...
... rice domesticate that suffered a deletion in exon 7 and as a result sequence coding for betaine aldehyde dehydrogenase (BADH2) ...
... betaine aldehyde + reduced acceptor Thus, the two substrates of this enzyme are choline and acceptor, whereas its two products ... are betaine aldehyde and reduced acceptor. This enzyme belongs to the family of oxidoreductases, specifically those acting on ... In enzymology, a choline dehydrogenase (EC 1.1.99.1) is an enzyme that catalyzes the chemical reaction choline + acceptor ⇌ {\ ... Gadda G, McAllister-Wilkins EE (2003). "Cloning, Expression, and Purification of Choline Dehydrogenase from the Moderate ...
... benzaldehyde dehydrogenase (NADP+) MeSH D08.811.682.657.163.515 - betaine-aldehyde dehydrogenase MeSH D08.811.682.657.163.562 ... aldehyde dehydrogenase MeSH D08.811.682.657.163.249.750 - omega-crystallins MeSH D08.811.682.657.163.311 - aldehyde oxidase ... malate dehydrogenase MeSH D08.811.682.047.748 - malate dehydrogenase (nadp+) MeSH D08.811.682.047.892 - xanthine dehydrogenase ... acetoin dehydrogenase MeSH D08.811.682.047.070 - alcohol dehydrogenase MeSH D08.811.682.047.150 - carbohydrate dehydrogenases ...
Brocker C, Cantore M, Failli P, Vasiliou V (May 2011). "Aldehyde dehydrogenase 7A1 (ALDH7A1) attenuates reactive aldehyde and ... In particular, antiquitin localizes to the mitochondria in kidney and liver to contribute to the synthesis of betaine, a ... Aldehyde dehydrogenase 7 family, member A1, also known as ALDH7A1 or antiquitin, is an enzyme that in humans is encoded by the ... The protein encoded by this gene is a member of subfamily 7 in the aldehyde dehydrogenase gene family. These enzymes are ...
... was benzaldehyde dehydrogenase) EC 1.2.1.7: benzaldehyde dehydrogenase (NADP+) EC 1.2.1.8: betaine-aldehyde dehydrogenase EC ... aldehyde dehydrogenase (NAD+) EC 1.2.1.4: aldehyde dehydrogenase (NADP+) EC 1.2.1.5: aldehyde dehydrogenase (NAD(P)+) EC 1.2. ... D-glucuronolactone dehydrogenase. Now included with EC 1.2.1.3 aldehyde dehydrogenase (NAD+) EC 1.1.1.71: alcohol dehydrogenase ... mycothiol dehydrogenase]] EC 1.2.1.67: vanillin dehydrogenase EC 1.2.1.68: coniferyl-aldehyde dehydrogenase EC 1.2.1.69: ...
PheA uses a simple dehydrogenase to convert prephenate to phenylpyruvate, while TyrA uses a NAD-dependent dehydrogenase to make ... His4 catalyzes the oxidation of L-histidinol to form L-histidinal, an amino aldehyde. In the last step, L-histidinal is ... this step is performed by homocysteine methyltransferase or betaine-homocysteine S-methyltransferase.) Methionine biosynthesis ... Relevant enzymes include aspartokinase, aspartate-semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine O- ...
In enzymology, a betaine-aldehyde dehydrogenase (EC 1.2.1.8) is an enzyme that catalyzes the chemical reaction betaine aldehyde ... Other names in common use include betaine aldehyde oxidase, BADH, betaine aldehyde dehydrogenase, and BetB. This enzyme ... ROTHSCHILD HA, BARRON ES (1954). "The oxidation of betaine aldehyde by betaine aldehyde dehydrogenase". J. Biol. Chem. 209 (2 ... Eklund H; El-Ahmad, M; Ramaswamy, S; Hjelmqvist, L; Jörnvall, H; Eklund, H (1998). "Structure of betaine aldehyde dehydrogenase ...
We report here high-level expression of betaine aldehyde dehydrogenase (BADH) in cultured cells, roots, and leaves of carrot ( ... to 54-fold more betaine (93-101 μmol g−1 dry weight of β-Ala betaine and Gly betaine) than untransformed cells grown in liquid ... Plastid-Expressed Betaine Aldehyde Dehydrogenase Gene in Carrot Cultured Cells, Roots, and Leaves Confers Enhanced Salt ... Plastid-Expressed Betaine Aldehyde Dehydrogenase Gene in Carrot Cultured Cells, Roots, and Leaves Confers Enhanced Salt ...
Molecular cloning and functional characterization of two kinds of betaine-aldehyde dehydrogenase in betaine-accumulating ... Betaine aldehyde dehydrogenase (BADH). FJ595952. Spinacia oleracea. Juglans regia. salinity and drought. [161]. ... Betaine aldehyde dehydrogenase (BADH). JF776157. A. canescens. Solanum tuberosum. Salt stress. [160]. ... Introduction of the betaine aldehyde dehydrogenase (BADH) gene from Atriplex canescens into potato enhanced SS tolerance of ...
Yin, X.; Zhao, Y.; Luo, D.; Zhang, H. Isolating the promoter of a stress-induced gene encoding betaine aldehyde dehydrogenase ... aldehyde, β-amyrin. - exhibit effective activity against various bacterial, fungal, and yeast strains. - exhibit anti- ... These organic compounds (including terpene hydrocarbons and their oxygen derivatives, alcohols, aldehydes, and ketones) play an ...
Structure and function of betaine aldehyde dehydrogenase: An enzyme within the multienzyme aldehyde dehydrogenase system ... Distinct but parallel evolutionary patterns between alcohol and aldehyde dehydrogenases: Addition of fish/human betaine ... 11-hydroxythromboxane B2 dehydrogenase from porcine kidney is identical to cytosolic aldehyde dehydrogenase ... polyol dehydrogenases, threonine dehydrogenase, archaeon glucose dehydrogenase, and eye lens reductase-active zeta-crystallins ...
Manganese inactivation of renal betaine aldehyde dehydrogenase from swine See A method for determining states in the course of ...
Choline dehydrogenase catalyzes the oxidation of choline to glycine betaine via betaine aldehyde in glycine betaine ... betaine biosynthesis is catalyzed by choline monooxygenase in combination with betaine aldehyde dehydrogenase. In E. coli, the ... Choline dehydrogenase catalyzes the four electron oxidation of choline to glycine betaine via a betaine aldehyde intermediate ( ... It has been shown that four genes encoding choline dehydrogenase (betA), betaine aldehyde dehydrogenase (betB), a putative ...
... fragrant rice was generated by a SDN directed toward 1-bp deletion in the gene encoding betaine aldehyde dehydrogenase (BADH2 ...
Arabidopsis thaliana putative betaine aldehyde dehydrogenase. O.I.. H.G.. S.X.. Please select. TAIR (integral). KEGG (integral) ...
Betaine aldehyde dehydrogenase from spinach leaves: Purification, in vitro translation of the mRNA, and regulation by salinity ... Betaine aldehyde dehydrogenase polymorphism in spinach: Genetic and biochemical characterization Academic Article ...
Trossat, C., B. Rathinasabapathi, and A.D. Hanson (1997) Transgenically expressed betaine aldehyde dehydrogenase efficiently ... betaine aldehyde dehydrogenases lacking typical transit peptides are targeted to tobacco chloroplasts where they confer betaine ... BETA-ALANINE BETAINE ACCUMULATION: A METABOLIC ENGINEERI BETA-ALANINE BETAINE ACCUMULATION: A METABOLIC ENGINEERI ... Rathinasabapathi, B., K.F. McCue, D.A. Gage and A.D. Hanson (1994). Metabolic engineering of glycine betaine synthesis: plant ...
betaine aldehyde dehydrogenase NP_970697 normal 1 n/a Treponema denticola ATCC 35405 Bacteria -. ... alcohol dehydrogenase, iron-containing NP_970668 normal 1 n/a Treponema denticola ATCC 35405 Bacteria -. ... sorbitol dehydrogenase, putative NP_970692 normal 1 n/a Treponema denticola ATCC 35405 Bacteria -. ... methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase NP_970630 normal 1 n/a Treponema denticola ATCC ...
Funciton: Betaine aldehyde dehydrogenase (EC 1.2.1.8) Locus tag: BLi03269. Name: gbsB. Funciton: Choline dehydrogenase ...
choline dehydrogenase (RefSeq). 293, 409. BSU31060. gbsA. glycine betaine aldehyde dehydrogenase, NAD+-dependent (RefSeq). 293 ...
choline dehydrogenase (RefSeq). 293, 409. BSU31060. gbsA. glycine betaine aldehyde dehydrogenase, NAD+-dependent (RefSeq). 293 ... NAD(P)H-dependent glycerol-3-phosphate dehydrogenase (RefSeq). 37, 314. BSU23560. mleN. malate-H+/Na+-lactate antiporter ( ...
Betaine aldehyde dehydrogenase (BADH) catalyses the irreversible oxidation of betaine aldehyde to glycine betaine with the ... Betaine aldehyde dehydrogenase (BADH) catalyses the irreversible oxidation of betaine aldehyde to glycine betaine with the ... The osmoregulatory NAD-dependent betaine aldehyde dehydrogenase (betaine aldehyde:NAD oxidoreductase, EC 1.2.1.8), of ... The osmoregulatory NAD-dependent betaine aldehyde dehydrogenase (betaine aldehyde:NAD oxidoreductase, EC 1.2.1.8), of ...
Betaine aldehyde dehydrogenase polymorphism in spinach: Genetic and biochemical characterization. 26:143-151. 1988 ...
with Betaine Aldehyde Dehydrogenase Gene ZHOU Guo-Yan , , YANG Zheng-An , ZHANG Yin-Hua , GUO Feng-Gen ,. ZHOU Xiao-Gang , , ... betaine aldehyde dehydrogenase ) gene derived from spinach was transformed into the genome of cabbage line 03079 mediated by ...
Betaine aldehyde dehydrogenase. C. CHOX. (NRULE_0178). Choline oxidase. GOSPT_109_00030. ...
Betaine aldehyde dehydrogenase (BADH) belongs to the ALDH9 family and catalyses the irreversible oxidation of betaine aldehyde ... One of the most important osmoprotectants is betaine aldehyde dehydrogenase (Kumar et al., 2004). ... In our previous study we found that the total activity of aldehyde dehydrogenase in cancer ON123300 of RCC is at the same level ... The kidney was not able to balance the NADH excess even though an increase in malate dehydrogenase, lactate dehydrogenase, ...
Betaine aldehyde dehydrogenase (E.C.1.2.1.8) _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_ ... Betaine aldehyde dehydrogenase 57428.457 2 1.2.1.8 ? ? ? 2 non-polymer syn MAGNESIUM ION 24.305 5 ? ? ? ? 3 non-polymer syn ... betaine aldehyde dehydrogenase, Structural Genomics, Infectious Deseases, NAD, Oxidoreductase, PSI, Protein Structure ... 1.7 Angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betB) from Staphylococcus aureus _struct.pdbx_ ...
to candidate H281DRAFT_02464 H281DRAFT_02464 betaine aldehyde dehydrogenase. Query= BRENDA::P49189 (494 letters) > ... Align 4-trimethylammoniobutyraldehyde dehydrogenase (EC 1.2.1.47) (characterized) ...
Crystal structure of betaine aldehyde dehydrogenase from Burkholderia pseudomallei. Beard, Dylan K; Subramanian, Sandhya; ... This study reports apo and cofactor-bound crystal structures of the potential drug target betaine aldehyde dehydrogenase (BADH ... The crystal structure of a short-chain dehydrogenase from B. phymatum (BpSDR) was determined in space group C2221 at a ... The atomic structure of a putative dehydrogenase/reductase (SDR) from P. xenovorans (PxSDR) was determined in space group P21 ...
physiological parameters and the expression of betaine aldehyde dehydrogenase and proline 5-carboxylate synthase genes in ...
... betaine aldehyde dehydrogenase, aldehyde dehydrogenase, benzoylformate decarboxylase, hydroxyacylglutathione hydrolase, and ...
Betaine-aldehyde dehydrogenase. BIOMASS_Ec_iJO1366_core_53p95M. E. coli biomass objective function (iJO1366) - core - with ...
... 첫단계는 choline dehydrogenase (CDH)에 의해서 촉매되고(Bet A gene), bet B 유전자의 산물인 betaine aldehyde dehydrogenase(BADH)에 의해 수행된다. 본 실험에서는 ... Ginseng Transformation of Betaine Aldehyde Dehydrogenase Gene Relative Salt Resistant through Somatic Embryogenesis ... 염류내성관련 유전자 Betaine Aldehyde Dehydrogenase Gene의 인삼 체세포 배발생을 통한 형질전환 ... 염류내성 식물은 염류농도의 변화에 따라 세포내의 삼투압을 유지하기 위한 화합물을 합성하는 기작을 가지고 있는데 이런 화합물은 주로 proline, glycine, betaine, polyols, sugar등으로 체내에 ...
Key words: Transgenic tobacco enriched betaine aldehyde dehydrogenase gene, Chlorophyll fluorescence induction transient, ... in which betaine aldehyde dehydrogenase (BADH) gene had been introduced, were determined and compared with the parent plants. ... ate dehydrogenase, isocitric dehydrogenase and succinic dehydrogenase in tricarboxylic acid cycle had a slight increase, and ... malate dehydrogenase, isocitrate dehydrogenese, suecinate dehydrogenase and cytochrome C oxidase) and the activities of ...
... glycinebetaine accumulation and the betaine aldehyde dehydrogenase gene expression in two halophytic plants, Salicornia ... glycinebetaine accumulation and the betaine aldehyde dehydrogenase gene expression in two halophytic plants, Salicornia ...
Choline dehydrogenase catalyzes the conversion of exogenously supplied choline into the intermediate glycine betaine aldehyde, ... this enzyme is found associated in a transciptionally co-induced gene cluster with betaine aldehyde dehydrogenase, the second ... dehydrogenase, Rv0697 family. This model describes a set of dehydrogenases belonging to the glucose-methanol-choline ... utlizing a soluable choline oxidase or type III alcohol dehydrogenase instead of choline dehydrogenase. This enzyme is a member ...
  • Other names in common use include betaine aldehyde oxidase, BADH, betaine aldehyde dehydrogenase, and BetB. (wikipedia.org)
  • The osmoregulatory NAD-dependent betaine aldehyde dehydrogenase (betaine aldehyde:NAD oxidoreductase, EC 1.2.1.8), of Escherichia coli, was purified to apparent homogeneity from an over-producing strain carrying the structural gene for the enzyme (betB) on the plasmid vector pBR322. (rhea-db.org)
  • protein_coding" "AGT25156","N559_3508","Klebsiella pneumoniae","putative short-chain dehydrogenase/reductase SDR [Ensembl]. (ntu.edu.sg)
  • putative NAD-dependent aldehyde dehydrogenase [Ensembl]. (ntu.edu.sg)
  • We report here high-level expression of betaine aldehyde dehydrogenase (BADH) in cultured cells, roots, and leaves of carrot (Daucus carota) via plastid genetic engineering. (upenn.edu)
  • BADH enzyme activity was enhanced 8-fold in transgenic carrot cell cultures, grew 7-fold more, and accumulated 50- to 54-fold more betaine (93-101 μmol g−1 dry weight of β-Ala betaine and Gly betaine) than untransformed cells grown in liquid medium containing 100 mm NaCl. (upenn.edu)
  • 2004). Betaine aldehyde dehydrogenase (BADH) belongs to the ALDH9 family and catalyses the irreversible oxidation of betaine aldehyde to glycine betaine (N, N, N-trimethyl amine), a vital osmolyte accumulated in cells under osmotic stress (Chen and Murata, 2011). (precisionfda.org)
  • The transient characteristics of chlorophyll fluorescence induction, the activities of respiratory enzymes (malate dehydrogenase, isocitrate dehydrogenese, suecinate dehydrogenase and cytochrome C oxidase) and the activities of photorespiratory enzymes (hydroxypyruvate reductase, glycolate oxidase and catalase) in the transgenic tobacco (Nicotiana tabacum L. ), in which betaine aldehyde dehydrogenase (BADH) gene had been introduced, were determined and compared with the parent plants. (jipb.net)
  • Choline dehydrogenase catalyzes the oxidation of choline to glycine betaine via betaine aldehyde in glycine betaine biosynthesis. (scialert.net)
  • Glycine betaine is a compatible solute, able to restore and maintain osmotic balance of living cells under stress. (scialert.net)
  • In this study, choline dehydrogenase ( betA ) gene encoding for glycine betaine biosynthesis in Escherichia coli isolated from salted shark ( Scoliodon sp. (scialert.net)
  • In E . coli , the biosynthetic pathway for the production of glycine betaine from choline has been well characterized at the genetic level ( Landfald and Strom, 1986 ). (scialert.net)
  • Recently, bacterial glycine betaine synthesizing enzymes have become a major target in developing stress tolerant crop plants of economic interest. (scialert.net)
  • Choline dehydrogenase ( betA ) of E . coli catalyses the first step in glycine betaine biosynthesis, the oxidation of choline. (scialert.net)
  • Glycine betaine plays a key role in halotolerant eubacteria as a osmoprotectant to cope with the osmotic stress (Meena et al. (precisionfda.org)
  • Choline dehydrogenase catalyzes the conversion of exogenously supplied choline into the intermediate glycine betaine aldehyde, as part of a two-step oxidative reaction leading to the formation of osmoprotectant betaine. (unl.edu)
  • As in Escherichia coli , Staphylococcus xylosus , and Sinorhizobium meliloti, this enzyme is found associated in a transciptionally co-induced gene cluster with betaine aldehyde dehydrogenase, the second catalytic enzyme in this reaction. (unl.edu)
  • The systematic name of this enzyme class is betaine-aldehyde:NAD+ oxidoreductase. (wikipedia.org)
  • This model describes a set of dehydrogenases belonging to the glucose-methanol-choline oxidoreductase (GMC oxidoreductase) family. (unl.edu)
  • This enzyme is a member of the GMC oxidoreductase family (pfam00732 and pfam05199), sharing a common evoluntionary origin and enzymatic reaction with alcohol dehydrogenase. (unl.edu)
  • The kidney was not able to balance the NADH excess even though an increase in malate dehydrogenase, lactate dehydrogenase, aspartate and alanine transaminase activities was noted [23]. (precisionfda.org)
  • malate dehydrogenase 1 [Source:HGNC Sym. (gsea-msigdb.org)
  • lactaldehyde dehydrogenase [Ensembl]. (ntu.edu.sg)
  • Probable methylmalonate-semialdehyde dehydrogenase MmsA. (ntu.edu.sg)
  • The MDR superfamily with ~350-residue subunits contains the classical liver alcohol dehydrogenase (ADH), quinone reductase, leukotriene B4 dehydrogenase and many more forms. (researchgate.net)
  • Zinc binding to the peptide replica and analogs to residues 93-115 of horse liver alcohol dehydrogenase (ADH) was examined by competition of the peptides and the chromophoric chelator 4-(2- pyridylazo)resorcinol for zinc and X-ray absorption fine structure analysis of the zinc ligands. (researchgate.net)
  • We also found that renal cell cancer patients have significantly higher total activity of alcohol dehydrogenase and its class I isoenzyme in the serum. (precisionfda.org)
  • Many recent data revealed that kidney alcohol dehydrogenase activity increased significantly after ethanol administration what affected the capacity of the kidney to prevent NADH accumulation in the cytosol. (precisionfda.org)
  • Other gram-positive organisms have been shown to employ a different enzymatic system, utlizing a soluable choline oxidase or type III alcohol dehydrogenase instead of choline dehydrogenase. (unl.edu)
  • succinylglutamic semialdehyde dehydrogenase [Ensembl]. (ntu.edu.sg)
  • Only nominal studies in characterization of choline dehydrogenase from E . coli have been reported to date. (scialert.net)
  • In this study, we report the characterization and structural analysis of choline dehydrogenase in E . coli . (scialert.net)
  • Purification and characterization of osmoregulatory betaine aldehyde dehydrogenase of Escherichia coli. (rhea-db.org)
  • Outgrouping from this model, Caulobacter crescentus shares sequence homology with choline dehydrogenase, yet other genes participating in this enzymatic reaction have not currently been identified [Cellular processes, Adaptations to atypical conditions]. (unl.edu)
  • In enzymology, a betaine-aldehyde dehydrogenase (EC 1.2.1.8) is an enzyme that catalyzes the chemical reaction betaine aldehyde + NAD+ + H2O ⇌ {\displaystyle \rightleftharpoons } betaine + NADH + 2 H+ The 3 substrates of this enzyme are betaine aldehyde, NAD+, and H2O, whereas its 3 products are betaine, NADH, and H+. (wikipedia.org)
  • This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. (wikipedia.org)
  • However, this enzyme also catalyses the second step, the dehydrogenation of betaine aldehyde to betaine ( Landfald and Strom, 1986 ). (scialert.net)
  • signifying the practical applications of choline dehydrogenase. (scialert.net)
  • Moreover, the sequence analysis of choline dehydrogenase from our isolate shows several base substitutions with that of reported sequences in GenBank, resulting in the altered amino acid sequences of the translated proteins. (scialert.net)
  • Moreover, H-GBHs exposure perturbed mitochondrial membrane fusion and electron transport in mitochondrial respiratory chains by increasing the mRNA expression of mitofusin-2 (MFN2) and succinate dehydrogenase subunit A (SDHA), causing mitochondrial dysfunction. (nih.gov)
  • Short-chain dehydrogenases/reductases (SDRs) constitute a large family of NAD(P)(H)-dependent oxidoreductases, sharing sequence motifs and displaying similar mechanisms. (researchgate.net)
  • the activities of ma]ate dehydrogenase, isocitric dehydrogenase and succinic dehydrogenase in tricarboxylic acid cycle had a slight increase, and the activity of eytochrome C oxidase in the terminal oxidative pathway had a significant increase. (jipb.net)
  • Gamma-aminobutyraldehyde dehydrogenase [Ensembl]. (ntu.edu.sg)
  • aldehyde dehydrogenase B [Ensembl]. (ntu.edu.sg)
  • phenylacetaldehyde dehydrogenase [Ensembl]. (ntu.edu.sg)
  • aldehyde dehyrogenase [Ensembl]. (ntu.edu.sg)
  • Numerous in vitro experiments have indicated that betaine acts as an osmoprotectant by stabilizing both the quaternary structure of proteins and cellular membrane against the adverse effects of high salinity and extreme temperatures ( Gorham, 1995 ). (scialert.net)
  • betaine biosynthesis is catalyzed by choline monooxygenase in combination with betaine aldehyde dehydrogenase. (scialert.net)
  • Aldehyde dehydrogenase domain [InterProScan]. (ntu.edu.sg)
  • betaine/carnitine/choline family transporter, BCCT transporter family [InterProScan]. (ntu.edu.sg)
  • dehydrogenase, Rv0697 family. (unl.edu)
  • Benzaldehyde Dehydrogenase (NADP+)" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ucdenver.edu)
  • In our previous study we found that the total activity of aldehyde dehydrogenase in cancer ON123300 of RCC is at the same level as in normal renal tissue [10]. (precisionfda.org)
  • H-GBHs increased the activity of glutathione peroxidase (GPX) and levels of methane dicarboxylic aldehyde (MDA), hydrogen peroxide (H 2 O 2 ) and inflammatory factors (tumor necrosis factor-α (TNF-α), interleukin-1β (IL-1β), interleukin-6 (IL-6), interleukin-10 (IL-10)) in suckling piglets and activated Nrf2-mediated antioxidant signaling pathway. (nih.gov)
  • The dehydrogenase was highly specific for betaine aldehyde. (rhea-db.org)
  • This graph shows the total number of publications written about "Benzaldehyde Dehydrogenase (NADP+)" by people in this website by year, and whether "Benzaldehyde Dehydrogenase (NADP+)" was a major or minor topic of these publications. (ucdenver.edu)