An aldehyde oxidoreductase expressed predominantly in the LIVER; LUNGS; and KIDNEY. It catalyzes the oxidation of a variety of organic aldehydes and N-heterocyclic compounds to CARBOXYLIC ACIDS, and also oxidizes quinoline and pyridine derivatives. The enzyme utilizes molybdenum cofactor and FAD as cofactors.
Organic compounds containing a carbonyl group in the form -CHO.
Oxidoreductases that are specific for ALDEHYDES.
An iron-molybdenum flavoprotein containing FLAVIN-ADENINE DINUCLEOTIDE that oxidizes hypoxanthine, some other purines and pterins, and aldehydes. Deficiency of the enzyme, an autosomal recessive trait, causes xanthinuria.
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
Benzaldehydes are aromatic organic compounds consisting of a benzene ring connected to a formyl group (-CHO), which is the simplest and most representative compound being benzaldehyde (C6H5CHO).
An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.
A flavoprotein enzyme that catalyzes the univalent reduction of OXYGEN using NADPH as an electron donor to create SUPEROXIDE ANION. The enzyme is dependent on a variety of CYTOCHROMES. Defects in the production of superoxide ions by enzymes such as NADPH oxidase result in GRANULOMATOUS DISEASE, CHRONIC.
A metallic element with the atomic symbol Mo, atomic number 42, and atomic weight 95.94. It is an essential trace element, being a component of the enzymes xanthine oxidase, aldehyde oxidase, and nitrate reductase. (From Dorland, 27th ed)
Compounds based on pyrazino[2,3-d]pyrimidine which is a pyrimidine fused to a pyrazine, containing four NITROGEN atoms.
A plant genus of the family RUTACEAE. Members contain quinoline alkaloids.
Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
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).
An enzyme that catalyzes the oxidative deamination of naturally occurring monoamines. It is a flavin-containing enzyme that is localized in mitochondrial membranes, whether in nerve terminals, the liver, or other organs. Monoamine oxidase is important in regulating the metabolic degradation of catecholamines and serotonin in neural or target tissues. Hepatic monoamine oxidase has a crucial defensive role in inactivating circulating monoamines or those, such as tyramine, that originate in the gut and are absorbed into the portal circulation. (From Goodman and Gilman's, The Pharmacological Basis of Therapeutics, 8th ed, p415) EC
A XANTHINE OXIDASE inhibitor that decreases URIC ACID production. It also acts as an antimetabolite on some simpler organisms.
Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)
An enzyme oxidizing peptidyl-lysyl-peptide in the presence of water & molecular oxygen to yield peptidyl-allysyl-peptide plus ammonia & hydrogen peroxide. EC
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)
Flavoproteins are a type of protein molecule that contain noncovalently bound flavin mononucleotide or flavin adenine dinucleotide as cofactors, involved in various redox reactions and metabolic pathways, such as electron transfer, energy production, and DNA repair.
Potent cholinesterase inhibitor used as an insecticide and acaricide.
Phthalazines are heterocyclic aromatic organic compounds consisting of a benzene ring fused with a 1,2-diazine ring, which have been used as intermediates in the synthesis of various pharmaceuticals and dyes.
The rate dynamics in chemical or physical systems.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.

Aldehyde oxidase-dependent marked species difference in hepatic metabolism of the sedative-hypnotic, zaleplon, between monkeys and rats. (1/144)

A marked difference in hepatic activity of aldehyde oxidase between rats and monkeys was found to be responsible for the previously reported marked species difference in the metabolism of Zaleplon in vivo. In the postmitochondrial fractions, S-9s, from liver homogenates of these animals, Zaleplon was transformed in the presence of NADPH into the side chain oxidation product, N-desethyl-Zaleplon, and the aromatic ring oxidation product, 5-oxo-Zaleplon. In the rat S-9, N-desethyl-Zaleplon and 5-oxo-Zaleplon were a major and a very minor metabolites, respectively. However, in the monkey S-9, Zaleplon was transformed into 5-oxo-Zaleplon at a much higher rate than that for N-desethyl-Zaleplon formation. N-Desethyl-Zaleplon was formed in the monkey S-9 at a rate almost equal to that in the rat S-9. N-Desethyl-5-oxo-Zaleplon was formed at a minor rate only in the monkey S-9 through N-desethyl-Zaleplon as an obligatory intermediate. The hepatic activity for the formation of 5-oxo-Zaleplon in the monkey and rat was localized in cytosol and did not require NADPH. Sensitivity to various inhibitors and requirement of water as oxygen source, using H218O, strongly suggested that the hepatic cytosolic formation of 5-oxo-Zaleplon was mediated by aldehyde oxidase. N-Desethyl-Zaleplon was formed in the presence of NADPH by microsomes from the liver of rats and monkeys, and its formation was strongly suggested using various cytochrome P-450 inhibitors to be mediated by a number of cytochrome P-450 isoforms, such as 3A, 2C, and 2D subfamilies.  (+info)

A genetic linkage map of rat chromosome 9 with a new locus for variant activity of liver aldehyde oxidase. (2/144)

A genetic linkage map of rat chromosome 9 consisting of five loci including a new biochemical marker representing a genetic variation of the activity of the liver aldehyde oxidase, (Aox) was constructed. Linkage analysis of the five loci among 92 backcross progeny of (WKS/Iar x IS/Iar)F1 x WKS/Iar revealed significant linkages between these loci. Minimizing crossover frequency resulted in the best gene order: Aox-D9Mit4-Gls-Cryg-Tp53l1. The homologues of the Cryg, Gls, and Aox genes have been mapped on mouse chromosome 1 and human chromosome 2q. The present findings provide further evidence for the conservation of synteny among these regions of rat, mouse, and human chromosomes.  (+info)

Molecular cloning of the cDNA coding for mouse aldehyde oxidase: tissue distribution and regulation in vivo by testosterone. (3/144)

The cDNA coding for mouse aldehyde oxidase (AO), a molybdoflavoprotein, has been isolated and characterized. The cDNA is 4347 nt long and consists of an open reading frame predicting a polypeptide of 1333 amino acid residues, with 5' and 3' untranslated regions of 13 and 335 nt respectively. The apparent molecular mass of the translation product in vitro derived from the corresponding cRNA is consistent with that of the monomeric subunit of the AO holoenzyme. The cDNA codes for a catalytically active form of AO, as demonstrated by transient transfection experiments conducted in the HC11 mouse mammary epithelial cell line. The deduced primary structure of the AO protein contains consensus sequences for two distinct 2Fe-2S redox centres and a molybdopterin-binding site. The amino acid sequence of the mouse AO has a high degree of similarity with the human and bovine counterparts, and a significant degree of relatedness to AO proteins of plant origin. Northern blot and in situ hybridization analyses demonstrate that hepatocytes, cardiocytes, lung endothelial or epithelial cells and oesophagus epithelial cells express high levels of AO mRNA. In the various tissues and organs considered, the level of AO mRNA expression is not strictly correlated with the amount of the corresponding protein, suggesting that the synthesis of the AO enzyme is under translational or post-translational control. In addition, we observed sex-related regulation of AO protein synthesis. In the liver of male animals, despite similar amounts of AO mRNA, the levels of the AO enzyme and corresponding polypeptide are significantly higher than those in female animals. Treatment of female mice with testosterone increases the amounts of AO mRNA and of the relative translation product to levels similar to those in male animals.  (+info)

Production of homo- and hetero-dimeric isozymes from two aldehyde oxidase genes of Arabidopsis thaliana. (4/144)

Polyclonal antibodies were raised against synthetic peptides or recombinant polypeptides encoded by Arabidopsis atAO-1 and atAO-2 cDNAs, which have sequences similar to maize and animal aldehyde oxidase (AO) cDNAs. Anti-atAO-1 antibodies recognized AOalpha and AObeta among the three isoforms, AOalpha, AObeta, and AOgamma, detected in Arabidopsis seedlings after native PAGE, while anti-atAO-2 antibodies reacted with AObeta and AOgamma. The polypeptide specifically recognized by each antibody was collected as the Protein-A/IgG/antigen complex. The 150- and 145-kDa polypeptides were purified by SDS-PAGE and digested with Achromobacter Protease I. From the amino acid sequences and molecular masses of the derivative peptides, it was revealed that the 150- and 145-kDa polypeptides were the products of atAO-1 and atAO-2, respectively. Molecular masses of the native forms of AOalpha, AObeta, and AOgamma were estimated as approximately 290-300 kDa. These results suggest that AOalpha and AOgamma are homodimers consisting of atAO-1 and atAO-2 products, respectively, and that AObeta is a heterodimer of the atAO-1 and atAO-2 products.  (+info)

Thioguanine administered as a continuous intravenous infusion to pediatric patients is metabolized to the novel metabolite 8-hydroxy-thioguanine. (5/144)

Thiopurine antimetabolites have been in clinical use for more than 40 years, yet the metabolism of thiopurines remains only partially understood. Data from our previous pediatric phase 1 trial of continuous i.v. infusion of thioguanine (CIVI-TG) suggested that TG was eliminated by saturable mechanism, with conversion of the drug to an unknown metabolite. In this study we have identified this metabolite as 8-hydroxy-thioguanine (8-OH-TG). The metabolite coeluted with the 8-OH-TG standard on HPLC and had an identical UV spectrum, with a lambda(max) of 350 nm. On mass spectroscopy, the positive ion, single quad scan of 8-OH-TG yielded a protonated molecular ion at 184 Da and contained diagnostic ions at m/z 167, 156, 142, and 125 Da. Incubation of TG in vitro with partially purified aldehyde oxidase resulted in 8-OH-TG formation. 8-OH-TG is the predominant circulating metabolite found in patients receiving CIVI-TG and is likely generated by the action of aldehyde oxidase.  (+info)

The mouse aldehyde oxidase gene: molecular cloning, chromosomal mapping and functional characterization of the 5'-flanking region. (6/144)

In this article, we report on the chromosome mapping and molecular cloning of the genetic locus encoding the mouse molybdo-iron/sulfur-flavoprotein aldehyde oxidase. The aldehyde oxidase locus maps to mouse chromosome 1 band C1-C2, as determined by fluorescence in situ hybridization experiments conducted on metaphase chromosomes. The gene is approximately 83 kb long and consists of 35 exons. The exon/intron boundaries are perfectly conserved relative to the corresponding human homolog and almost completely conserved relative to the mouse xanthine oxidoreductase gene. This further supports the concept that the aldehyde oxidase and xanthine oxidoreductase loci evolved from the same ancestral precursor by a gene duplication event. The position of a major transcription start site was defined by primer extension and RNase mapping analysis. The 5'-flanking region of the mouse aldehyde oxidase gene contains a functional and orientation-dependent promoter as well as several putative binding sites for known cell-specific and general transcription factors. Deletion analysis of the 5'-flanking region defines an approximately 470 bp DNA stretch which is necessary and sufficient for the transcription of the mouse aldehyde oxidase gene.  (+info)

Functional expression of two Arabidopsis aldehyde oxidases in the yeast Pichia pastoris. (7/144)

To investigate the biochemical and enzymatic properties of two aldehyde oxidase (AO) isoforms of Arabidopsis thaliana, we expressed AAO1 and AAO2 cDNAs in a heterologous yeast (Pichia pastoris) system and successfully obtained the proteins in active forms. The expressed AAO1 and AAO2 proteins gave activity bands with the same mobilities on native gel electrophoresis and exhibited the same substrate preferences on zymograms with 8 aldehydes as those of AOalpha and AOgamma in Arabidopsis seedlings, respectively. Furthermore, anti-AAO1 and anti-AAO2 antibodies, which specifically recognize the seedling AOalpha and AOgamma, respectively, reacted with the AAO1 and AAO2 proteins produced in P. pastoris, respectively. These results indicate that these AO proteins are accurately produced in the yeast system, as in Arabidopsis seedlings. Using AO preparations from P. pastoris, the enzymatic properties of Arabidopsis AOalpha and AOgamma were investigated. AOalpha showed a relatively wide substrate specificity for 7 aldehydes tested, with high affinity to benzaldehyde and indole-3-aldehyde, while AOgamma could most efficiently oxidize naphthaldehyde. AOalpha was strongly inhibited by iodoacetate and KCN, while AOgamma was inhibited not only by iodoacetate and KCN but also by 2-mercaptethanol, dithiothreitol, menadion, and estradiol. AOalpha and AOgamma showed the highest activity at around 65 and 50 degrees C, respectively, and exhibited pH dependence around pH 8.0. These results indicate that the two AO isoforms in Arabidopsis seedlings have different enzymatic properties and may have different physiological roles in vivo.  (+info)

Metabolism of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) in perfused rat liver: involvement of hepatic aldehyde oxidase as a detoxification enzyme. (8/144)

To elucidate the toxicological relevance of hepatic aldehyde oxidase (AO) as a detoxification enzyme of 1-methyl-4-phenyl-1,2,3, 6-tetrahydropyridine (MPTP), we studied the metabolism and the hepatotoxicity of MPTP in intact rat livers exhibiting different AO activities by using a recirculating perfusion method. In the perfusate during a 90-min recirculation of 1 mM MPTP, the perfused liver from Jcl:Wistar rat, a strain showing high AO activity, generated almost equal amounts of 1-methyl-4-phenylpyridinium species (MPP(+)) and 1-methyl-4-phenyl-5,6-dihydro-2-pyridone (MPTP lactam) as major metabolites, together with 4-phenyl-1,2,3, 6-tetrahydropyridine, 1-methyl-4-phenyl-2-pyridone (MP 2-pyridone) and 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine N-oxide. However, a marked decrease of MPTP lactam as well as MP 2-pyridone and a concomitant increase of MPP(+) were caused by coinfusion of 2-hydroxypyrimidine (2-OH PM), a competitive inhibitor of AO, into Jcl:Wistar rat liver. A quite similar metabolic profile was obtained on perfusion of AO-deficient WKA/Sea rat liver. Rather large amounts of MPP(+) were retained in the liver in all cases, but especially in Jcl:Wistar rat in the presence of 2-OH PM. Lactate dehydrogenase leakage into the perfusate from rat liver perfused with 1 mM MPTP was greater in the strain with lower AO activity, WKA/Sea, than in that with higher AO activity, Jcl:Wistar. Furthermore, inhibition of AO in Jcl:Wistar rat in the presence of 2-OH PM caused an enhancement of lactate dehydrogenase leakage. These results suggest that hepatic AO is a key detoxification enzyme for MPTP.  (+info)

Aldehyde oxidase is an enzyme found in the liver and other organs that helps to metabolize (break down) various substances, including drugs, alcohol, and environmental toxins. It does this by catalyzing the oxidation of aldehydes, which are organic compounds containing a functional group consisting of a carbon atom bonded to a hydrogen atom and a double bond to an oxygen atom. Aldehyde oxidase is a member of the molybdenum-containing oxidoreductase family, which also includes xanthine oxidase and sulfite oxidase. These enzymes all contain a molybdenum cofactor that plays a critical role in their catalytic activity.

Aldehyde oxidase is an important enzyme in the metabolism of many drugs, as it can convert them into more water-soluble compounds that can be easily excreted from the body. However, variations in the activity of this enzyme between individuals can lead to differences in drug metabolism and response. Some people may have higher or lower levels of aldehyde oxidase activity, which can affect how quickly they metabolize certain drugs and whether they experience adverse effects.

In addition to its role in drug metabolism, aldehyde oxidase has been implicated in the development of various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. For example, elevated levels of aldehydes produced by lipid peroxidation have been linked to oxidative stress and inflammation, which can contribute to the progression of these conditions. Aldehyde oxidase may also play a role in the detoxification of environmental pollutants, such as polycyclic aromatic hydrocarbons (PAHs) and heterocyclic amines (HCAs), which have been associated with an increased risk of cancer.

Overall, aldehyde oxidase is an important enzyme that plays a critical role in the metabolism of drugs and other substances, as well as in the development of various diseases. Understanding its activity and regulation may help to develop new strategies for treating or preventing these conditions.

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.

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.

Xanthine oxidase is an enzyme that catalyzes the oxidation of xanthine to uric acid, which is the last step in purine metabolism. It's a type of molybdenum-containing oxidoreductase that generates reactive oxygen species (ROS) during its reaction mechanism.

The enzyme exists in two interconvertible forms: an oxidized state and a reduced state. The oxidized form, called xanthine oxidase, reduces molecular oxygen to superoxide and hydrogen peroxide, while the reduced form, called xanthine dehydrogenase, reduces NAD+ to NADH.

Xanthine oxidase is found in various tissues, including the liver, intestines, and milk. An overproduction of uric acid due to increased activity of xanthine oxidase can lead to hyperuricemia, which may result in gout or kidney stones. Some medications and natural compounds are known to inhibit xanthine oxidase, such as allopurinol and febuxostat, which are used to treat gout and prevent the formation of uric acid stones in the kidneys.

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.

Benzaldehyde is an organic compound with the formula C6H5CHO. It is the simplest aromatic aldehyde, and it consists of a benzene ring attached to a formyl group. Benzaldehyde is a colorless liquid with a characteristic almond-like odor.

Benzaldehyde occurs naturally in various plants, including bitter almonds, cherries, peaches, and apricots. It is used in many industrial applications, such as in the production of perfumes, flavorings, and dyes. In addition, benzaldehyde has been used in medical research for its potential therapeutic effects, such as its anti-inflammatory and antimicrobial properties.

However, it is important to note that benzaldehyde can be toxic in high concentrations and may cause irritation to the skin, eyes, and respiratory system. Therefore, it should be handled with care and used in accordance with appropriate safety guidelines.

Xanthine dehydrogenase (XDH) is an enzyme involved in the metabolism of purines, which are nitrogen-containing compounds that form part of DNA and RNA. Specifically, XDH helps to break down xanthine and hypoxanthine into uric acid, a waste product that is excreted in the urine.

XDH can exist in two interconvertible forms: a dehydrogenase form (XDH) and an oxidase form (XO). In its dehydrogenase form, XDH uses NAD+ as an electron acceptor to convert xanthine into uric acid. However, when XDH is converted to its oxidase form (XO), it can use molecular oxygen as an electron acceptor instead, producing superoxide and hydrogen peroxide as byproducts. These reactive oxygen species can contribute to oxidative stress and tissue damage in the body.

Abnormal levels or activity of XDH have been implicated in various diseases, including gout, cardiovascular disease, and neurodegenerative disorders.

NADPH oxidase is an enzyme complex that plays a crucial role in the production of reactive oxygen species (ROS) in various cell types. The primary function of NADPH oxidase is to catalyze the transfer of electrons from NADPH to molecular oxygen, resulting in the formation of superoxide radicals. This enzyme complex consists of several subunits, including two membrane-bound components (gp91phox and p22phox) and several cytosolic components (p47phox, p67phox, p40phox, and rac1 or rac2). Upon activation, these subunits assemble to form a functional enzyme complex that generates ROS, which serve as important signaling molecules in various cellular processes. However, excessive or uncontrolled production of ROS by NADPH oxidase has been implicated in the pathogenesis of several diseases, such as cardiovascular disorders, neurodegenerative diseases, and cancer.

I'm sorry for any confusion, but "Molybdenum" is not a medical term. It is an element with the symbol Mo and atomic number 42 on the periodic table. Molybdenum is used in various industries, including medicine, for example in the production of surgical instruments and some prosthetics due to its strength and resistance to corrosion. However, it is not a term used to describe a medical condition or bodily process. If you have any questions related to elements and their uses in medicine, I'd be happy to help with those!

Pteridines are a class of heterocyclic aromatic organic compounds that are structurally related to pterins, which contain a pyrimidine ring fused to a pyrazine ring. They are naturally occurring substances that can be found in various living organisms such as bacteria, fungi, plants, and animals.

Pteridines have several important biological functions. For instance, they play a crucial role in the synthesis of folate and biotin, which are essential cofactors for various metabolic reactions in the body. Additionally, some pteridines function as chromophores, contributing to the coloration of certain organisms such as butterflies and birds.

In medicine, pteridines have been studied for their potential therapeutic applications. For example, some synthetic pteridine derivatives have shown promising results in preclinical studies as antitumor, antiviral, and antibacterial agents. However, further research is needed to fully understand the medical implications of these compounds.

"Ruta" is a botanical name for the herb commonly known as Rue. In a medical context, it may refer to the dried leaves of this plant (Ruta graveolens), which have been used in traditional medicine for various purposes such as treating anxiety, menstrual cramps, and skin conditions. However, it's important to note that the use of Ruta in modern medicine is not well-studied, and its effectiveness for these uses is not established. Additionally, Ruta can have toxic effects and should be used with caution under the guidance of a healthcare professional.

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

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

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

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

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

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

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.

Monoamine oxidase (MAO) is an enzyme found on the outer membrane of mitochondria in cells throughout the body, but primarily in the gastrointestinal tract, liver, and central nervous system. It plays a crucial role in the metabolism of neurotransmitters and dietary amines by catalyzing the oxidative deamination of monoamines. This enzyme exists in two forms: MAO-A and MAO-B, each with distinct substrate preferences and tissue distributions.

MAO-A preferentially metabolizes serotonin, norepinephrine, and dopamine, while MAO-B is mainly responsible for breaking down phenethylamines and benzylamines, as well as dopamine in some cases. Inhibition of these enzymes can lead to increased neurotransmitter levels in the synaptic cleft, which has implications for various psychiatric and neurological conditions, such as depression and Parkinson's disease. However, MAO inhibitors must be used with caution due to their potential to cause serious adverse effects, including hypertensive crises, when combined with certain foods or medications containing dietary amines or sympathomimetic agents.

Allopurinol is a medication used to treat chronic gout and certain types of kidney stones. It works by reducing the production of uric acid in the body, which is the substance that can cause these conditions when it builds up in high levels. Allopurinol is a xanthine oxidase inhibitor, meaning it blocks an enzyme called xanthine oxidase from converting purines into uric acid. By doing this, allopurinol helps to lower the levels of uric acid in the body and prevent the formation of new kidney stones or gout attacks.

It is important to note that allopurinol can have side effects, including rash, stomach upset, and liver or kidney problems. It may also interact with other medications, so it is essential to inform your healthcare provider of any other drugs you are taking before starting allopurinol. Your healthcare provider will determine the appropriate dosage and monitoring schedule based on your individual needs and medical history.

Metalloproteins are proteins that contain one or more metal ions as a cofactor, which is required for their biological activity. These metal ions play crucial roles in the catalytic function, structural stability, and electron transfer processes of metalloproteins. The types of metals involved can include iron, zinc, copper, magnesium, calcium, or manganese, among others. Examples of metalloproteins are hemoglobin (contains heme-bound iron), cytochrome c (contains heme-bound iron and functions in electron transfer), and carbonic anhydrase (contains zinc and catalyzes the conversion between carbon dioxide and bicarbonate).

Protein-Lysine 6-Oxidase (PLOX) is an enzyme that belongs to the family of copper-containing oxidases. It catalyzes the oxidative deamination of specific lysine residues in proteins, resulting in the formation of lysine-6-aldehydes, ammonia, and hydrogen peroxide. This enzyme plays a crucial role in various biological processes, including the regulation of protein function, modification of extracellular matrices, and the maintenance of copper homeostasis. Mutations in the gene encoding PLOX have been associated with certain diseases, such as Menkes disease, a rare X-linked recessive disorder characterized by copper deficiency and neurological symptoms.

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.

Flavoproteins are a type of protein molecule that contain noncovalently bound flavin mononucleotide (FMN) or flavin adenine dinucleotide (FAD) as cofactors. These flavin cofactors play a crucial role in redox reactions, acting as electron carriers in various metabolic pathways such as cellular respiration and oxidative phosphorylation. Flavoproteins are involved in several biological processes, including the breakdown of fatty acids, amino acids, and carbohydrates, as well as the synthesis of steroids and other lipids. They can also function as enzymes that catalyze various redox reactions, such as oxidases, dehydrogenases, and reductases. Flavoproteins are widely distributed in nature and found in many organisms, from bacteria to humans.

Fenthion is a type of pesticide called an organophosphate insecticide. It works by inhibiting the enzyme cholinesterase, which leads to an accumulation of acetylcholine and ultimately results in nervous system dysfunction in insects. Fenthion can be used to control a variety of pests, including flies, mosquitoes, and ticks. However, it is also toxic to non-target organisms, including humans, and has been linked to various health effects such as neurological damage and cancer. As a result, the use of fenthion has been restricted or banned in many countries.

Phthalazines are not a medical term, but a chemical one. They refer to a class of heterocyclic organic compounds that contain a phthalazine ring in their structure. The phthalazine ring is made up of two benzene rings fused to a single six-membered saturated carbon ring containing two nitrogen atoms.

Phthalazines have no specific medical relevance, but some of their derivatives are used in the pharmaceutical industry as building blocks for various drugs. For example, certain phthalazine derivatives have been developed as potential medications for conditions such as hypertension, heart failure, and cancer. However, these compounds are still in the experimental stages and have not yet been approved for medical use.

It's worth noting that some phthalazines have been found to have toxic effects on living organisms, so their use in medical applications is carefully regulated.

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.

Species specificity is a term used in the field of biology, including medicine, to refer to the characteristic of a biological entity (such as a virus, bacterium, or other microorganism) that allows it to interact exclusively or preferentially with a particular species. This means that the biological entity has a strong affinity for, or is only able to infect, a specific host species.

For example, HIV is specifically adapted to infect human cells and does not typically infect other animal species. Similarly, some bacterial toxins are species-specific and can only affect certain types of animals or humans. This concept is important in understanding the transmission dynamics and host range of various pathogens, as well as in developing targeted therapies and vaccines.

Aldehyde oxidase is very concentrated in the liver, where it oxidizes multiple aldehydes and nitrogenous heterocyclic compounds ... Aldehyde oxidase is a member of the molybdenum flavoprotein family and has a very complex evolutionary profile-as the genes of ... Aldehyde oxidase is thought to have a significant impact on pharmacokinetics. AO is capable of oxidizing many drugs in the ... Aldehyde+oxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Articles with short ...
Aldehyde Oxidase-Dependent Marked Species Difference in Hepatic Metabolism of the Sedative-Hypnotic, Zaleplon, Between Monkeys ... Aldehyde Oxidase-Dependent Marked Species Difference in Hepatic Metabolism of the Sedative-Hypnotic, Zaleplon, Between Monkeys ... Aldehyde Oxidase-Dependent Marked Species Difference in Hepatic Metabolism of the Sedative-Hypnotic, Zaleplon, Between Monkeys ... Aldehyde Oxidase-Dependent Marked Species Difference in Hepatic Metabolism of the Sedative-Hypnotic, Zaleplon, Between Monkeys ...
AAO3-abscisic-aldehyde oxidase; A-ARR-type A Arabidopsis response regulator; ABA-abscisic acid; ABF-ABA response factor; ABI- ... AAO3-abscisic-aldehyde oxidase; A-ARR-type A Arabidopsis response regulator; ABA-abscisic acid; ABF-ABA response factor; ABI- ... and abscisic-aldehyde oxidase (AAO3), were down-regulated while an ABA hydroxylase and a carotenoid cleavage dioxygenase 8 ( ... GA2ox-GA 2-oxidase; GA3ox-GA 3-oxidase; GAMT-GA methyl transferase; GH3-Gretchen Hagen3 family protein; GID1-GA insensitive ...
Combined deficiency of sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. *Combined molybdoflavoprotein enzyme ... Genetic Testing Registry: Sulfite oxidase deficiency due to molybdenum cofactor deficiency type A ... Genetic Testing Registry: Sulfite oxidase deficiency due to molybdenum cofactor deficiency type B ... Genetic Testing Registry: Sulfite oxidase deficiency due to molybdenum cofactor deficiency type C ...
Individuals affected with sulfite oxidase deficiency most commonly present in the neonatal period with intractable seizures, ... Sulfite oxidase deficiency is an inborn error of the metabolism of sulfated amino acids. ... Deficiency of xanthine oxidase and aldehyde oxidase is not known to cause neurologic disease and may not produce symptoms. [4] ... Molybdenum cofactor is associated with the enzymes sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase (see the image ...
There are no known clinically relevant inhibitors or inducers of aldehyde oxidase.. Intramuscular Pharmacokinetics Systemic ... There are no known clinically relevant inhibitors or inducers of aldehyde oxidase. Less than one-third of ziprasidone metabolic ... reaction is mediated primarily by chemical reduction by glutathione as well as by enzymatic reduction by aldehyde oxidase and ... ziprasidone is metabolized via a combination of chemical reduction by glutathione and enzymatic reduction by aldehyde oxidase. ...
M2 and M3, the major metabolites in human faeces, were formed from M2 and lenvatinib, respectively, by aldehyde oxidase. ... The main metabolic pathways in humans were identified as oxidation by aldehyde oxidase, demethylation via CYP3A4, glutathione ...
Combined Sulfite Oxidase Xanthine Dehydrogenase Deficit Is Aldehyde Oxidase - Type A. 00:46. ... Combined Sulfite Oxidase Xanthine Dehydrogenase Deficit Is Aldehyde Oxidase - Type B. 00:54. ...
Capmatinib is primarily metabolized by CYP3A4 and aldehyde oxidase; in vitro, it is also a P-gp substrate. Capmatinib inhibits ...
Aldehyde oxidases (AOXs). *Uridine diphosphate glucuronosyltransferases (UGTs). *Sulfotransferases (SULTs). In addition, the ...
Mammalian metalloproteins and enzymes that have nitrate reductase activity include aldehyde oxidase, heme proteins, ...
2008). Aldehyde oxidase-catalyzed metabolism of N1-methylnicotinamide in vivo and in vitro in chimeric mice with humanized ... and 1-methyl-4-pyridone-3-carboxamide by aldehyde oxidase (Zhou et al., 2009; Mayneris-Perxachs et al., 2016). 2Py and 1- ... and transitory glucose oxidation via glucose oxidase during unregulated glucose metabolism. According to a growing body of ...
Grapevine U-box E3 ubiquitin ligase VlPUB38 negatively regulates fruit ripening by facilitating abscisic-aldehyde oxidase ... and Cytochrome C oxidase (CCO) (Jin et al.,2013). When their activities decrease will affect the function of mitochondria, and ...
Two new alleles of the abscisic aldehyde oxidase 3 gene reveal its role in abscisic acid biosynthesis in seeds. González-Guzmán ... Mutations in nicotinamide adenine dinucleotide phosphate oxidase homolog genes (atrbohB and D), ABA biosynthesis mutants (aba1 ...
Aburas, Omaro A Emhmed (2014) Investigation of aldehyde oxidase and xanthine oxidoreductase in rainbow trout (Oncorhynchus ...
Chloral hydrate oxidation is thought to be catalyzed by an aldehyde oxidase, whereas trichloroethanol oxidation is catalyzed ...
... aldehyde oxidase 4; ACBP6: acyl-CoA-binding protein; ACP4: acyl carrier protein 4; ACX1, ACX4: acyl-CoA-oxidase; Amido-IAA: ...
aldehyde oxidase 1 [Source:HGNC Symbo.... 205206_at. 3730. ANOS1. anosmin 1 [Source:HGNC Symbol;Acc:HGN.... ...
Seven enzymes like different subunits of cytochrome c oxidase, cytochrome c reductase, aldehyde dehydrogenase and ATP synthase ... Y. Tong and M. R. Kanost, "Manduca sexta serpin-4 and serpin-5 inhibit the prophenol oxidase activation pathway: cDNA cloning, ... The proteins involved in house keeping functions included 41 energy metabolism enzymes such as cytochrome c oxidase subunits, ... Serpins are implicated in prophenol oxidase activation, an innate immune response in anthropods [27]. Various proteases and ...
Indeed, as a combination of high capacity dehydrogenase (alcohol (ADH) and aldehyde (ALD) dehydrogenase and oxidase enzymes is ... Justification for read-across : a read across approach is proposed with heptanoic acid as aldehydes are rapidly oxidized to the ... Based on the known biochemical fate of straight chain aliphatic aldehydes and carboxylic acid, it is concluded that the ... Based on the known biochemical fate of straight chain aliphatic aldehydes and carboxylic acid, it is concluded that the ...
ALDH1_ARTAN / C5I9X1 Aldehyde dehydrogenase 1; Artemisinic aldehyde oxidase; Artemisinate synthase; Dihydroartemisinic aldehyde ... b3588 aldehyde dehydrogenase B (EC from Escherichia coli K-12 substr. MG1655. P37685 aldehyde dehydrogenase B (EC 1.2. ... b1415 aldehyde dehydrogenase A (EC; EC from Escherichia coli K-12 substr. MG1655. P25553 aldehyde ... A1B4L2 aldehyde dehydrogenase (NAD+) (EC from Paracoccus denitrificans (strain Pd 1222). ALDH_PARDP / A1B4L2 Aldehyde ...
aldehyde oxidase 2 pseudogene 0.405578 F13B coagulation factor XIII, B polypeptide 0.405267 ...
Mouse aldehyde oxidase 1 ELISA Kit;Mouse aldehyde oxidase 2 ELISA Kit;. ... Mouse azaheterocycle hydroxylase 1 ELISA Kit;Mouse retinal oxidase ELISA Kit;Mouse Ao ELISA Kit;Mouse Ro ELISA Kit;Mouse ...
... aldehyde oxidase, AAO) synthesis were significantly up-regulated. In addition, the bitter tasting amino acids, alkaloids and ... Catecol Oxidase/genética , Catecol Oxidase/metabolismo , Eletrólitos/metabolismo , Frutas/genética , Perfilação da Expressão ... polyphenol oxidase, PPO). Moreover, the genes that are involved in ethylene (1-aminocyclopropane- 1-carboxylate oxidase, ACO; 1 ... and polyphenol oxidase genes (PPO1 and PPO5), were noticed in Wujiuxiang as compared to Yali. The results indicated that ...
Combined deficiency of xanthine dehydrogenase and aldehyde oxidase. *Xeroderma pigmentosum (De Sanctis-Cacchione syndrome) ... Sulfite oxidase (SO) deficiency, isolated or in association with xanthine oxidase (XO) deficiency. Molybdenum Cofactor ... Peroxisomal acyl-CoA-oxidase deficiency. Pseudoneonatal adrenoleukodystrophy . Pseudo-NALD. ACOX1 .. *Peroxisomal disorders. ... Hyperprolinemia Type I. Proline Oxidase Deficiency *Hyperprolinemia type II. Pyrroline-5-carboxylate dehydrogenase deficiency. ...
Sulfite oxidase - helps prevent dangerous buildup of sulfites in the body.. *Aldehyde oxidase - helps the liver break down ... Xanthine oxidase - helps break down nucleotides, the building blocks of DNA, excreting them in the urine ...
There are no known clinically relevant inhibitors or inducers of aldehyde oxidase. ... reaction is mediated primarily by chemical reduction by glutathione as well as by enzymatic reduction by aldehyde oxidase and ...
  • ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana. (
  • This enzyme is necessary for the normal function of xanthine dehydrogenase, described above, and another enzyme called aldehyde oxidase. (
  • Mutations in the MOCOS gene prevent xanthine dehydrogenase and aldehyde oxidase from being turned on (activated). (
  • Patients with classic xanthinuria type I are deficient in xanthine dehydrogenase, whereas patients with type II have a dual deficiency of xanthine dehydrogenase and aldehyde oxidase. (
  • Xanthine oxidase/dehydrogenase (XDH) and aldehyde oxidase (AO) compete with TPMT to inactivate AZA. (
  • The other two pathways, thiopurine methyltransferase (TPMT) and xanthine oxidase/dehydrogenase ( XDH ) both produce metabolites which are thought to be inactive and are the first steps in eliminating thiopurines from the body. (
  • In humans, molybdenum is a cofactor for three enzyme classes-sulfiteoxidase, aldehyde dehydrogenase, and xanthine oxidase (Kisker et al. (
  • However, Nrf2 increased mRNA of many other phase-I enzymes, such as aldo-keto reductases, carbonyl reductases, and aldehyde dehydrogenase 1. (
  • For instance, the enzyme called alcohol dehydrogenase, which transforms alcohols like ethanol into aldehydes by means of an oxidation reaction, functions properly only when sufficient supplies of zinc are available. (
  • ANX/DEP ALC may be related to dopamine and serotonin, which are catalyzed by monoamine oxidase A (MAOA) and acetaldehyde dehydrogenase 2 (ALDH2). (
  • Post-release, serotonin interacts with receptors in postsynaptic neurons and is metabolized by monoamine oxidase (MAO) and aldehyde dehydrogenase (ALDH), producing 5-hydroxyindoleacetaldehyde (5-HIAA), which is subsequently excreted through urine. (
  • In the subsequent metabolic phase, the enzyme called aldehyde oxidase transforms aldehyde into an acidic substance, which can be eliminated from the body along with urine . (
  • Molybdenum is a structural constituent of molybdopterin, a cofactor synthesized by the body and required for the function of four enzymes: sulfite oxidase, xanthine oxidase, aldehyde oxidase, and mitochondrial amidoxime reducing component (mARC). (
  • The best-known molybdenum enzymes include sulfite oxidase, aldehyde oxidase, and xanthine oxidase. (
  • Molybdenum (Mo) is a component of coenzymes necessary for the activity of xanthine oxidase, sulfite oxidase, and aldehyde oxidase. (
  • Genetic sulfite oxidase deficiency was described in 1967 in a child. (
  • Molybdenum deficiency resulting in decreased activity of sulfite oxidase and sulfite toxicity occurred in a patient receiving long-term total parenteral nutrition. (
  • 1. Systematic exploration of predicted destabilizing nonsynonymous single nucleotide polymorphisms (nsSNPs) of human aldehyde oxidase: A Bio-informatics study. (
  • 2. The impact of single nucleotide polymorphisms on human aldehyde oxidase. (
  • 3. Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. (
  • 7. A single nucleotide polymorphism causes enhanced radical oxygen species production by human aldehyde oxidase. (
  • 8. Inactivation of Human Aldehyde Oxidase by Small Sulfhydryl-Containing Reducing Agents. (
  • menafn - the express wire) human aldehyde oxidase market insights 2023. (
  • Monoamine neurotransmitters are enzymatically converted to aldehydes via monoamine oxidase followed by further metabolism such as carbonyl oxidation/reduction. (
  • These results provide strong evidence that aldehyde oxidase and not xanthine oxidase is responsible for the 6-oxidation of BRL 42359 to penciclovir in human liver cytosol, and this is likely to reflect the in vivo situation. (
  • It catalyzes the oxidation of a variety of organic aldehydes and N-heterocyclic compounds to CARBOXYLIC ACIDS , and also oxidizes quinoline and pyridine derivatives. (
  • Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. (
  • Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. (
  • Aldehydes differ from ketones in that the carbonyl is placed at the end of a carbon skeleton rather than between two carbon atoms. (
  • The aldehyde and ketone (an organic chemical amalgam) reduction involves converting aldehydes and ketones into an alcohol . (
  • Does genetic variability in aldehyde oxidase and molybdenum cofactor sulfurase predict nonresponse to allopurinol? (
  • Using inhibitors of xanthine oxidase (allopurinol) and aldehyde oxidase (menadione and isovanillin), the relative roles of these enzymes in this process were determined. (
  • Allopurinol is oxidized to oxypurinol by aldehyde oxidase. (
  • These lipid aldehydes, some including an α,β-unsaturated carbonyl, target important proteins such as α-synuclein, proteasome degradation and G-protein-coupled signaling. (
  • The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme--an aldehyde oxidoreductase. (
  • The most important enzymes that are needed for Phase I detoxification to take place include the cytochrome P-450 monooxygenase system as well as the mixed-function amine oxidase system. (
  • Aldehydes, such as acetaldehyde and formaldehyde, are one such type of chemical compound. (
  • Aldehyde oxidase is a molybdenum enzyme that can detoxify aldehyde, which is a metabolic waste product. (
  • An aldehyde / ˈ æ l d ᵻ h aɪ d / or alkanal is an organic compound containing a formyl group. (
  • Aldehydes are common in organic chemistry . (
  • The biogenic aldehydes produced from dopamine, norepinephrine and serotonin are known to be toxic, generate reactive oxygen species and/or cause aggregation of proteins such as α-synuclein. (
  • Biogenic Aldehyde-Mediated Mechanisms of Toxicity in Neurodegenerative Disease. (
  • Oxidative decomposition of several biomolecules produces reactive aldehydes. (
  • For example, autoxidation of a common molecule known as an aldehyde produces a molecule known as a peracid. (
  • Reduction reactions involve azo reduction, aromatic nitro reduction, reductive halogenations as well as aldehyde and ketone reduction. (
  • The loss of aldehyde oxidase activity does not appear to cause any health problems. (
  • The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. (
  • A pharmacogenetic study of aldehyde oxidase I in patients treated with XK469. (
  • Xanthine oxidase, aldehyde oxidase, and mARC are also involved in metabolizing drugs and toxins [ 3-6 ]. (
  • On the other hand, the enzyme called mixed-function amine oxidase system decontaminates the chemical groups known as amines, which comprise hydrogen and nitrogen. (
  • This enzyme belongs to the family of oxidoreductases , to be specific, those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. (
  • The group without R is called the aldehyde group or formyl group . (
  • Related to (i), the aldehyde group is somewhat polar . (
  • Aldehydes Disrupt Enzyme Function Previous research has already established that several types of aldehydes are detrimental to human health. (
  • Their precise function, has not, as yet, been defined, though they are mostly found in sugar-utilising enzymes, such as galactose oxidase. (
  • Role of aldehyde oxidase in the in vitro conversion of famciclovir to penciclovir in human liver. (
  • C-terminal Early set domain associated with the catalytic domain of galactose oxidase. (
  • This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. (
  • MENAFN - The Express Wire ) Explore the Perilla Aldehyde Market with a focus on future growth prospects, market size analysis, and the latest trends from 2024 to 2031. (
  • Aldehydes feature an sp 2 -hybridized, planar carbon center that is connected by a double bond to oxygen and a single bond to hydrogen. (
  • The actions of the enzyme aldehyde oxidase are subject to ample supplies of iron and molybdenum . (