• In enzymology, an abscisic-aldehyde oxidase (EC 1.2.3.14) is an enzyme that catalyzes the chemical reaction abscisic aldehyde + H2O + O2 ⇌ {\displaystyle \rightleftharpoons } abscisate + H2O2 The 3 substrates of this enzyme are abscisic aldehyde, H2O, and O2, whereas its two products are abscisate and H2O2. (wikipedia.org)
  • The selective estrogen receptor modulator, raloxifene, has been demonstrated as a potent uncompetitive inhibitor of human liver aldehyde oxidase-catalyzed oxidation of phthalazine, vanillin, and nicotine-Δ1′(5′)-iminium ion, with K i values of 0.87 to 1.4 nM. (aspetjournals.org)
  • Sulfite oxidase, for example, is located in the mitochondrial intermembrane space, where it catalyzes the oxidation of sulfite to sulfate, removing the reactive and potentially toxic sulfite from the cell. (wwu.edu)
  • Nitroalkane oxidase catalyzes the oxidation of neutral nitroalkanes to nitrite and the corresponding aldehydes or ketones. (rcsb.org)
  • The structure of the enzyme trapped with cyanide during oxidation of 1-nitrohexane shows the presence of the modified flavin. (rcsb.org)
  • The most common method for introducing aldehydes and ketones into polysaccharides and glycoproteins (including antibodies) is by periodate-mediated oxidation of vicinal diols. (thermofisher.com)
  • Figure 3.3.1 Sodium periodate oxidation of an N-terminal serine residue to an aldehyde, with the release of formaldehyde. (thermofisher.com)
  • Because galactose oxidase-mediated oxidation liberates a molecule of hydrogen peroxide for each molecule of aldehyde that is formed ( Figure 3.3.2 ), horseradish peroxidase-catalyzed oxidation of the Amplex Red reagent to red-fluorescent resorufin by hydrogen peroxide provides a ready means by which the number of aldehyde residues introduced into a biomolecule, including on a cell surface, can be quantitated. (thermofisher.com)
  • a) Cytochrome oxidase is a hemoprotein widely distributed in plants and animal tissues. (biologydiscussion.com)
  • 2 at-oms of Cu are also present which are asso-ciated with the cytochrome oxidase ac-tivity. (biologydiscussion.com)
  • hAOX1 metabolizes different classes of xenobiotics and is one of the main drug-metabolizing enzymes in the liver, along with cytochrome P450. (unl.pt)
  • Zaleplon is metabolized to a lesser extent by cytochrome P450 (CYP) 3A4 to form desethylZaleplon, which is quickly converted, presumably by aldehyde oxidase, to 5-oxo-desethylZaleplon. (healthyplace.com)
  • The aldehyde oxidase enzyme system is less well studied than the cytochrome P450 enzyme system. (medlibrary.org)
  • These reactions may be mediated by cytochrome P450 enzyme, aldehyde oxidase, glutathione-disulfide reductase, and glucuronate reductase. (bvsalud.org)
  • Neither valaciclovir nor acyclovir is metabolized by cytochrome P450 enzymes. (selfdecode.com)
  • Enzymes are proteins that help the body properly metabolize food. (treatforlife.com)
  • All of these alterations have deep effects on muscle proteins and also on proteolytic enzyme systems (Huff Lonergan et al. (earthwormexpress.com)
  • a) Enzymes that catalyse the removal of hy-drogen from a substrate but use only oxy-gen as a hydrogen acceptor to form water as a reaction product (with the exception of uricase and monoamine oxidase which form H 2 O 2 ). (biologydiscussion.com)
  • Cimetidine - zaleplon is a substrate of aldehyde oxidase and CYP3A4. (straighthealthcare.com)
  • Crystal structures to 2.2 A resolution or better of enzyme complexes with bound substrates and of a trapped substrate-flavin adduct are described. (rcsb.org)
  • The structure of the D402N enzyme crystallized in the presence of 1-nitrohexane or 1-nitrooctane shows the presence of the substrate in the binding site. (rcsb.org)
  • The aliphatic chain of the substrate extends into a tunnel leading to the enzyme surface. (rcsb.org)
  • Classic xanthinuria is one form of xanthinuria that is divided into 2 types based on the enzyme deficiency. (medscape.com)
  • Xanthinuria is only a marker in this setting because (1) the clinical presentation is overshadowed by neurologic manifestations and (2) death in the first year of life is caused by the deficiency of sulfite oxidase, which is the final step in cysteine metabolism. (medscape.com)
  • Deficiency of the enzyme, an autosomal recessive trait, causes xanthinuria. (lookformedical.com)
  • Molybdenum cofactor, which contains the element molybdenum, is essential to the function of several enzymes. (medlineplus.gov)
  • Without the cofactor, the metabolic enzymes that rely on it cannot function. (medlineplus.gov)
  • Sulfite, which is normally broken down by one of the molybdenum cofactor-dependent enzymes, is toxic, especially to the brain. (medlineplus.gov)
  • Enzymes that require Mo cannot use this metal unless it is chelated with an organic complex called the Mo cofactor. (wwu.edu)
  • We hypothesize that an increase in MOCS1 gene expression may have protective effects, by permitting the enzymes that depend on Mo and its cofactor to function more efficiently. (wwu.edu)
  • The aldehyde vanillin commonly used as a food flavoring is rapidly oxidized by aldehyde oxidase into the carboxylic acid vanillic acid. (wikidot.com)
  • Xanthine continues to accumulate, despite the recycling of hypoxanthine, because of the metabolism of guanine to xanthine by the enzyme guanase (see image below). (medscape.com)
  • The relevance of these data to the mechanistic understanding of aldehyde oxidase catalysis, as well as to the potential for raloxifene to cause drug interactions with agents for which aldehyde oxidase-mediated metabolism is important, such as zaleplon or famciclovir, is discussed. (aspetjournals.org)
  • Identify atomic sites vulnerable to metabolism by multiple enzyme families to guide compound design towards improved stability. (optibrium.com)
  • Discover compounds with multiple routes of metabolism to avoid potential drug-drug interactions, and identify the most important enzymes to ensure coverage for during experimental testing. (optibrium.com)
  • With regioselectivity models, identify the sites at which metabolism is likely to occur and corresponding potential metabolites for a range of enzyme families, again spanning human CYPs, AOXs, FMOs, UGTs and SULTs, plus rat, mouse and dog CYP. (optibrium.com)
  • An example output from the Metabolism module in Card View, with labelled molecules depicting sites of metabolism by enzyme, pie charts showing which enzymes and isoforms are most likely to metabolise the molecule, and a bar chart showing vulnerability of each site to metabolism. (optibrium.com)
  • Cimetidine inhibits both aldehyde oxidase ( in vitro ) and CYP3A4 ( in vitro and in vivo ), the primary and secondary enzymes, respectively, responsible for zaleplon metabolism. (medlibrary.org)
  • Xanthine Oxidase - This enzyme converts xanthine into uric acid, xanthine is produced from the metabolism of nucleotides (purines or pyrimidines) like DNA and RNA. (umzu.com)
  • Aldehyde oxidase detoxifies acetaldehyde which is a harmful substance that is formed as a byproduct of yeast and alcohol metabolism. (healwithfood.org)
  • Sulfite oxidase may also play a role in forming nitric oxide from nitrate. (umzu.com)
  • The action of bacterial nitrate reductases on the tongue and mammalian enzymes that have nitrate reductase activity in tissues are noted by the number 1. (sleepadvice.ca)
  • Cimetidine inhibits both enzymes and increases zaleplon exposure. (straighthealthcare.com)
  • Zaleplon is primarily metabolized by aldehyde oxidase to form 5-oxo-Zaleplon. (healthyplace.com)
  • CYP3A4 is ordinarily a minor metabolizing enzyme of zaleplon. (medlibrary.org)
  • The coadministration of a potent CYP3A4 enzyme inducer, although not posing a safety concern, thus could lead to ineffectiveness of zaleplon. (medlibrary.org)
  • The resulting loss of enzyme activity leads to buildup of certain chemicals, including sulfite, S-sulfocysteine, xanthine, and hypoxanthine (which can be identified in urine), and low levels of uric acid in the blood. (medlineplus.gov)
  • Xanthine oxidase also helps the body to oxidize purines and pyrimidines as well as to produce uric acid, an important waste product. (vitasave-us.com)
  • Hypha Discovery offer a comprehensive suite of techniques for provision of even the most difficult-to-synthesise metabolite, comprising chemical synthesis , recombinant enzymes such as PolyCYPs , microbial biotransformation , mammalian liver fractions as well as the purification of metabolites from biological matrices. (hyphadiscovery.com)
  • The following points highlight the five main enzymes involved in oxidative process. (biologydiscussion.com)
  • Diphenhydramine is reported to be a weak inhibitor of aldehyde oxidase in rat liver, but its inhibitory effects in human liver are not known. (medlibrary.org)
  • Molybdenum is absorbed through the intestines where it heads predominantly to the liver and kidney where it is integrated into a number of enzymes. (umzu.com)
  • After a variable period of time, the resolution of rigor mortis happens, with a progressive softening of the muscles due to the action of proteolytic enzymes (Warriss 2000). (earthwormexpress.com)
  • Mammalian enzymes with nitrite reductase activity are noted by the number 3. (sleepadvice.ca)
  • Sulfite Oxidase - This enzyme converts sulfite (SO2-) to sulfate (SO3-) which can readily be detoxified and excreted from the body. (umzu.com)
  • A hydrolase enzyme that converts L-asparagine and water to L-aspartate and NH3. (lookformedical.com)
  • The absence of sulfite oxidase in metabolic disorder can lead to death at an early age. (vitasave-us.com)
  • Aldehydes and ketones are present in a number of low molecular weight molecules such as drugs, steroid hormones, reducing sugars and metabolic intermediates (e.g., pyruvate and α-ketoglutarate). (thermofisher.com)
  • These introduced aldehydes and ketones can then be modified with fluorescent or biotinylated hydrazine, hydroxylamine or amine derivatives to label the polysaccharide or glycoprotein. (thermofisher.com)
  • Alkenes from unsaturated fatty acids and ceramides can also be converted to glycols by osmium tetroxide and then oxidized by periodate to aldehydes, and periodate will oxidize certain β-aminoethanol derivatives such as the hydroxylysine residues in collagen, as well as methionine (to its sulfoxide) and certain thiols (usually to disulfides). (thermofisher.com)
  • The aldehyde thus formed from the protein can be subsequently modified with a variety of hydrazine, hydroxylamine or amine derivatives. (thermofisher.com)
  • This enzyme participates in carotenoid biosynthesis. (wikipedia.org)
  • Even those aldehydes and ketones that are found in the open-ring form of simple carbohydrates are usually in equilibrium with the closed-ring form of the sugar. (thermofisher.com)
  • The infrequent occurrence of aldehydes and ketones in biomolecules has stimulated the development of techniques to selectively introduce these functional groups, thus providing unique sites for chemical modification and greatly extending the applications of the probes found in this section. (thermofisher.com)
  • Aldehyde oxidase (AO) is a metabolizing enzyme , located in the cytosolic compartment of tissues in many organisms. (wikidot.com)
  • Have confidence in your results, with accurate, transferable predictions based on fundamental mechanistic understanding of Phase I and II enzyme family reactions. (optibrium.com)
  • Raloxifene has also been shown to be a noncompetitive inhibitor of an aldehyde oxidase-catalyzed reduction reaction of a hydroxamic acid-containing compound, with a K i of 51 nM. (aspetjournals.org)
  • c) They are flavoprotein enzymes having FMN (flavin mononucleotide) or FAD (Flavin adenine dinucleotide) as pros-thetic groups. (biologydiscussion.com)
  • d) Many of the flavoprotein enzymes con-tain a metal for which they are known as metalloflavoprotein enzymes. (biologydiscussion.com)
  • These enzymes help break down (metabolize) different substances in the body, some of which are toxic if not metabolized. (medlineplus.gov)
  • Aldehydes are a consequence of metabolizing substances such as alcohols and must be detoxified from the body because they are extremely reactive and toxic in the body. (umzu.com)
  • Therefore, in order to minimise potential DDIs, compounds generally need to be metabolised by more than one enzyme family or isoform. (optibrium.com)
  • It helps to convert glycogen into energy during exercise and works with various enzymes in order to detoxify certain compounds in the body. (nutriwins.com)
  • Furthermore, we inspected the thermostability of wild-type hAOX1 and hAOX1 with various SNPs (L438V, R1231H, G1269R or S1271L) by CD spectroscopy and ThermoFAD, revealing that amino acid exchanges close to the Moco site can impact protein stability up to 10 °C. These results correlated with biochemical and structural data and enhance our understanding of hAOX1 and the effect of SNPs in the gene encoding this enzyme in the human population. (unl.pt)
  • Consequently, these results provide important structural descriptions of several steps along the nitroalkane oxidase reaction cycle. (rcsb.org)
  • The role of vitamins and minerals as components of enzymes and hormones in the body was established. (nursingce.com)
  • See which enzymes or isoforms are most likely to metabolise your compound to inform experiment prioritisation and reduce the risk of drug-drug interactions. (optibrium.com)
  • PolyCYPs+ screening kits comprise 18 PolyCYP isoforms together with the addition of other phase 1 enzymes. (hyphadiscovery.com)
  • Human aldehyde oxidase (AOX1) and the main human hepatic flavin-containing monooxygenase (FMO3) are included in the kit, with the other human FMO isoforms, available separately at Hypha. (hyphadiscovery.com)
  • These enzymes confer a protective function on the cell, by removing toxic catabolites. (wwu.edu)
  • Sulfite oxidase (SO) is responsible for the sulfoxidation process through which sulfites - which may have adverse health effects in sensitive individuals - are metabolized into non-toxic sulfates. (healwithfood.org)
  • Sulfite oxidase is necessary for the body to be able to break down the sulfur-containing amino acids like methionine and cysteine. (umzu.com)
  • If this enzyme is not functioning properly this can result in conditions like hypermethioninemia or hyperhomocysteinemia in which an excess of these amino acids are in the blood. (umzu.com)
  • This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. (wikipedia.org)
  • The systematic name of this enzyme class is abscisic-aldehyde:oxygen oxidoreductase. (wikipedia.org)
  • Exogenous agents are also impli- aldehyde) to form various pro-mu- tion, resisting cell death, enabling cated in the generation of reactive tagenic exocyclic adduct s (Bartsch replicative immortality, inducing oxygen. (who.int)
  • Mitochondrial Amidoxime Reducing Component - The exact enzymological functions of this enzyme aren't known, but it's believe to play a few roles in the body including detoxification of drugs and toxins. (umzu.com)
  • Alongside these regioselectivity models, our WhichEnzyme™ and WhichP450™ models help you predict the enzyme family or specific human CYP isoform which will be most likely overall to metabolise your compound. (optibrium.com)
  • Human aldehyde oxidase (hAOX1) is a molybdenum enzyme with high toxicological importance, but its physiological role is still unknown. (unl.pt)
  • The D402N enzyme has no detectable activity with neutral nitroalkanes [Valley, M. P., and Fitzpatrick, P. F. (2003) J. Am. Chem. (rcsb.org)