• Molybdenum cofactor is associated with the enzymes sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase (see the image below). (medscape.com)
  • [ 2 ] The enzyme sulfite oxidase depends on the molybdenum-containing pterin cofactor, as do the enzymes xanthine dehydrogenase and aldehyde oxidase. (medscape.com)
  • Xanthine dehydrogenase catalyzes the hydroxylation of xanthine and hypoxanthine to produce uric acid. (medscape.com)
  • The flavoenzyme nitroalkane oxidase is a member of the acyl-CoA dehydrogenase superfamily. (rcsb.org)
  • Mutations in MOCS1 cause a disease in humans known as Molybdenum cofactor (MoCo) deficiency, which ultimately results in a combined deficiency of three essential enzymatic functions that depend on Mo: sulfite oxidase, xanthine dehydrogenase and aldehyde oxidase. (wwu.edu)
  • AO catalyzes the oxidation of aldehydes into carboxylic acid, an action also performed by xanthine oxidase (XO) and aldehyde dehydrogenase (ALDH). (wikidot.com)
  • Previous analyses of mutants in plants indicated that the genetic locus aba3 is involved in this step leading to activation of the molybdenum enzymes aldehyde oxidase and xanthine dehydrogenase. (unipr.it)
  • Oxidoreductases also incorporate oxidase, oxygenase, peroxidase, dehydrogenase, and others, which are compounds that catalyze redox response in living life forms and in the research centre. (vedantu.com)
  • Choline dehydrogenase catalyzes the oxidation of choline to glycine betaine via betaine aldehyde in glycine betaine biosynthesis. (scialert.net)
  • betaine biosynthesis is catalyzed by choline monooxygenase in combination with betaine aldehyde dehydrogenase. (scialert.net)
  • Growth on CO requires the enzyme carbon monoxide dehydrogenase (CODH) that catalyzes the reversible conversion between CO and CO 2 . (hindawi.com)
  • Ethanol is metabolized by the enzyme alcohol dehydrogenase (ADH) pathway, which is located in the liver and gastric mucosa, and by the cytochrome P-450 mixed function oxidase (MFO) system in the liver. (medscape.com)
  • The mixed function oxidase component is subject to greater inducibility than alcohol dehydrogenase. (medscape.com)
  • Through interaction with aldehyde dehydrogenase, ethylene glycol is then metabolized to glycolic acid (GA). A profound acidosis often ensues with this intoxication which is attributable to the glycolic acid in circulation. (medscape.com)
  • The rate-limiting step of ethylene glycol metabolism is the alcohol dehydrogenase-catalyzed step. (medscape.com)
  • The aldehyde vanillin commonly used as a food flavoring is rapidly oxidized by aldehyde oxidase into the carboxylic acid vanillic acid. (wikidot.com)
  • The second route, in turn, opts for the reduction of yet another sustainable feedstock chemical, a carboxylic acid (6), into its aldehyde (1) with a wild-type (non-engineered) enzyme known as carboxylic acid reductase. (chembites.org)
  • Galactose oxidase oxidizes terminal galactose residues to aldehydes, particularly in glycoproteins. (thermofisher.com)
  • Galactose oxidase-modified lipopolysaccharides (LPS) have been modified with Alexa Fluor 488 hydrazide ( A10436 ) to probe for LPS-binding sites on cells. (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)
  • Their precise function, has not, as yet, been defined, though they are mostly found in sugar-utilising enzymes, such as galactose oxidase. (unl.edu)
  • C-terminal Early set domain associated with the catalytic domain of galactose oxidase. (unl.edu)
  • 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. (unl.edu)
  • The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. (unl.edu)
  • Subfamily AA5_2 contains galactose 6-oxidases ( EC 1.1.3.9 ), which oxidize the C-6 hydroxyl of diverse galactosides to the corresponding aldehyde [ 4 , 5 , 6 ]. (cazypedia.org)
  • The first biochemically characterized member of AA5 was the galactose 6-oxidase from the phytopathogenic fungus Fusarium graminearum (previously known as Polyporus circinatus and Cladobotryum (Dactylium) dendroides [ 11 ]), which was originally reported in 1959 following isolation from cultures [ 12 , 13 ]. (cazypedia.org)
  • Subsequently, the Fusarium graminearum galactose 6-oxidase became the defining member of AA5_2 [ 2 ]. (cazypedia.org)
  • An AA5 enzyme from Arabidopsis thaliana has been demonstrated in vivo to have galactose 6-oxidase activity and promote cell-to-cell adhesion in the seed coat epidermis [ 15 ] (see also [ 16 ]. (cazypedia.org)
  • The archetypal CRO and AA5 member is the Fusarium graminearum galactose 6-oxidase ( Fgr GalOx), which catalyzes the regioselective oxidation of the C6-hydroxyl group on the monosaccharide galactose ( EC 1.3.3.7 ) [ 12 , 13 ]. (cazypedia.org)
  • In stage I of drug digestion, oxidoreductase compounds, for example, cytochrome P450 oxidases add polar or receptive gatherings into drugs. (vedantu.com)
  • In phase I, enzymes such as cytochrome P450 oxidases introduce reactive or polar groups into xenobiotics. (bionity.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)
  • Consequently, these results provide important structural descriptions of several steps along the nitroalkane oxidase reaction cycle. (rcsb.org)
  • 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)
  • Adding alkyl groups to amines constitutes an essential step en route to many pharmaceuticals, agrochemicals, resins, and polymers, but current methods require large amounts of compounds, high temperatures, long reaction times, or the use of toxic or expensive reagents. (chembites.org)
  • This allows for an efficient single-pot reaction utilizing either the oxidase-aminase or reductase-aminase routes. (chembites.org)
  • AbstractEnzymes catalyzing the reduction reaction of xenobiotics are mainly members of the aldo-keto reductase (AKR) and s. (cn1699.cn)
  • Each black arrow represents a biochemical reaction and the blue and yellow ellipses on the arrows contain the acronyms of the enzymes that catalyze the reactions. (biomedcentral.com)
  • Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. (bvsalud.org)
  • Aldehyde oxidase produces hydrogen peroxide and, under certain conditions, can catalyze the formation of superoxide. (wikipedia.org)
  • Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. (unl.edu)
  • a) They catalyse the removal of hydrogen from a substrate and use either oxygen or artificial substances such a methylene blue as hydrogen acceptor. (biologydiscussion.com)
  • a) They catalyze the removal of hydrogen from a substrate but not able to use oxy-gen as hydrogen acceptor. (biologydiscussion.com)
  • Basic principle involved in Biogenic amines biosensor is the action of diamine oxidase (DAO) that catalyzes the oxidative deamination of primary amines to the corresponding aldehydes, hydrogen peroxide and ammonia. (ijpsr.com)
  • In contrast, hydrogenases catalyse the interconversion between hydrogen gas and protons (water) at rates and efficiencies higher than platinum but using the common elements iron and nickel. (ukri.org)
  • Glyoxal oxidase N-terminus. (unl.edu)
  • This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. (unl.edu)
  • Subfamily AA5_1 contains characterized glyoxal oxidases ( EC 1.2.3.15 ) [ 3 ]. (cazypedia.org)
  • The first characterized member of what is now known as AA5_1 is the glyoxal oxidase from Phanerochaete chrysosporium , which was likewise isolated from fungal culture [ 14 ]. (cazypedia.org)
  • The AA5_1 members are generally known as glyoxal oxidases ( EC 1.2.3.15 ), characterized members of which typically accept a range of simple aldehydes, α-hydroxycarbonyl, and α-dicarbonyl compounds as substrates, with the highest activities observed on glyoxal, methylglyoxal and glycolaldehyde [ 1 , 14 , 18 , 19 , 20 ]. (cazypedia.org)
  • In contrast, two glyoxal oxidases form Pycnoporus cinnabarinus demonstrated the highest catalytic efficiency on glyoxylic acid [ 21 ]. (cazypedia.org)
  • [ 3 ] Aldehyde oxidase hydroxylates hypoxanthine into xanthine and functions in detoxification. (medscape.com)
  • An iron-molybdenum flavoprotein containing FLAVIN-ADENINE DINUCLEOTIDE that oxidizes hypoxanthine, some other purines and pterins, and aldehydes. (lookformedical.com)
  • Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1 . (expasy.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)
  • However, this enzyme also catalyses the second step, the dehydrogenation of betaine aldehyde to betaine ( Landfald and Strom, 1986 ). (scialert.net)
  • Sulfite oxidase is located in the mitochondrial intermembranous space and is involved in electron transport. (medscape.com)
  • Acrolein, a byproduct of lipid peroxidation, can damage critical biomolecules, deplete endogenous antioxidant defenses, and cause mitochondrial dysfunction, which catalyzes and perpetuates oxidative stress. (purdue.edu)
  • 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)
  • Oxidoreductase is a chemical that catalyzes the exchange of electrons from one atom, the reductant, which is also known as electron donor, to another, the oxidant that is called the electron acceptor. (vedantu.com)
  • Oxidoreductase chemicals catalyze response including oxygen addition, hydride move, proton extraction, and other fundamental advances. (vedantu.com)
  • Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.2.3.14 (abscisic-aldehyde oxidase), EC 1.13.11.51 (9- cis -epoxycarotenoid dioxygenase) and EC 1.14.13.93 [(+)-abscisic acid 8′-hydroxylase]. (enzyme-database.org)
  • A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (lookformedical.com)
  • It is produced by the actions of the enzyme lysyl oxidase in the extracellular matrix and is essential in the crosslink formation that stabilizes collagen and elastin. (hmdb.ca)
  • Nitroalkane oxidase catalyzes the oxidation of neutral nitroalkanes to nitrite and the corresponding aldehydes or ketones. (rcsb.org)
  • 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)
  • 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)
  • 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)
  • 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)
  • 2012 ). The first committed step of ABA biosynthesis involves the oxidative cleavage of a C 40 9- cis -epoxycarotenoid, such as 9'- cis -neoxanthin or 9- cis -violaxanthin, to a C 15 xanthoxin (the primary precursor) and a C 25 by-product, which is catalyzed in plastids by 9- cis -epoxycarotenoid dioxygenase (NCED) (Schwartz et al. (springeropen.com)
  • Biosynthesis of the aldehydic sex pheromone components released by females of Heliothis zea was found to be catalyzed by primary alcohol oxidases residing in the cuticle that covers the glands. (psu.edu)
  • Teal, PEA & Tumlinson, III, JH 1988, ' Properties of cuticular oxidases used for sex pheromone biosynthesis by Heliothis zea ', Journal of Chemical Ecology , vol. 14, no. 11, pp. 2131-2145. (psu.edu)
  • Sulfite oxidase deficiency is an inborn error of the metabolism of sulfated amino acids. (medscape.com)
  • Sulfite oxidase deficiency and molybdenum cofactor deficiency in the metabolism of sulfated amino acids. (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)
  • Both reactive manifolds can meet at this point, and the aldehyde (1) can be converted to the alkylated amine product (7) directly via an enzyme-catalyzed reductive amination using a reductive aminase and the biological reductant NADPH as a source of electrons. (chembites.org)
  • Examples of these specific detoxification systems are the glyoxalase system, which removes the reactive aldehyde methylglyoxal, [3] and the various antioxidant systems that eliminate reactive oxygen species. (bionity.com)
  • 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)
  • 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)
  • The aldehyde thus formed from the protein can be subsequently modified with a variety of hydrazine, hydroxylamine or amine derivatives. (thermofisher.com)
  • In a fully defined in vitro system, the purified protein was able to activate aldehyde oxidase by using L-cysteine as sulfur donor. (unipr.it)
  • Individuals affected with sulfite oxidase deficiency most commonly present in the neonatal period with intractable seizures, characteristic dysmorphic features, and profound intellectual disability. (medscape.com)
  • Molybdenum cofactor deficiency, which affects the functioning of sulfite oxidase, leads to a similar phenotype. (medscape.com)
  • Inherited defects in the sulfite oxidase enzyme can cause the phenotype of sulfite oxidase deficiency. (medscape.com)
  • Deficiency of xanthine oxidase and aldehyde oxidase is not known to cause neurologic disease and may not produce symptoms. (medscape.com)
  • As sulfite oxidase deficiency and molybdenum cofactor deficiency have virtually identical phenotypes, the CNS toxicity appears to be secondary to loss of function of sulfite oxidase. (medscape.com)
  • The pathogenesis of the brain damage in those with sulfite oxidase deficiency is not known but may be related to sulfite accumulation or lack of sulfate in the CNS. (medscape.com)
  • Worldwide, approximately 50 cases of sulfite oxidase deficiency have been reported. (medscape.com)
  • In most cases, sulfite oxidase deficiency is fatal in infancy or early childhood. (medscape.com)
  • Survivors of sulfite oxidase deficiency often have profound intellectual disability. (medscape.com)
  • Traditionally, infants with sulfite oxidase deficiency were reported to present in the neonatal period. (medscape.com)
  • The first option consists of a starting primary alcohol (5) that gets oxidized to its corresponding aldehyde (1) by an engineered oxidase enzyme called AcCO6 under aerobic conditions. (chembites.org)
  • Activity, as indicated by conversion of primary alcohol to aldehyde, was as high in cell-free cuticle as it was in intact pheromone glands. (psu.edu)
  • AA5_2 also contains the more recently discovered general alcohol oxidases ( EC 1.1.3.13 ) [ 6 , 7 , 8 ] and aryl alcohol oxidases ( EC 1.1.3.7 ) [ 9 , 10 ]. (cazypedia.org)
  • HYALURONIDASES are a family of enzymes that catalyze the degradation of the glycosaminoglycan, hyaluronic acid. (bioassaysys.com)
  • Methionine and cysteine normally are metabolized to sulfite and then are oxidized to sulfate by the enzyme sulfite oxidase (see the image below). (medscape.com)
  • The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds (which can be catalyzed by EC 1.8.4.7 in the presence of glutathione disulfide) or limited proteolysis, which results in irreversible conversion. (expasy.org)
  • In histamine biosensor consisting of diamine oxidase (DAO) and a conventional oxygen electrode transducer was developed and applied for the determination of standard histamine solutions. (ijpsr.com)
  • Figure 3.3.1 Sodium periodate oxidation of an N-terminal serine residue to an aldehyde, with the release of formaldehyde. (thermofisher.com)
  • The xanthine oxidase class of molybdenum enzyzmes requires a terminal sulfur ligand at the active site. (unipr.it)
  • c) It catalyzes the oxidative deamination of the unnatural (D-) forms of amino acids. (biologydiscussion.com)
  • c) It catalyzes the oxidative deamination of naturally occurring L-amino acids. (biologydiscussion.com)
  • During their training, medicinal chemists are also taught to apply physical and mechanistic organic chemistry concepts (e.g., valence electrons, resonance effects, acidity, nucleophilicity, electrophilicity, etc.) to rationalize the biochemistry of enzyme-catalyzed reactions, and even understand the chemical basis for conversion of a substrate into product. (aspetjournals.org)
  • Also, they noticed that the product spectrum of the oxidase and the reductase overlap quite nicely with the substrate spectrum of the reductive aminase with little tendency for side reactions. (chembites.org)
  • [11] The variety of crucial reactions catalyzed by these latter enzymes means that molybdenum is an essential element for all higher eukaryote organisms, including humans. (knowpia.com)
  • The last distinct group of AA5_2 enzymes based on substrate specificity are the raffinose-specific oxidases ( EC 1.3.3.- ). (cazypedia.org)
  • An apparent distinction between the AA5_1 and AA5_2 subfamilies is that while AA5_1 enzymes catalyze the oxidation of aldehydes to carboxylic acids [ 1 ], AA5_2 members oxidize primary alcohols to the corresponding aldehyde (and, in some instances, also oxidize the aldehyde to the acid, albeit much more slowly) [ 4 , 22 ]. (cazypedia.org)
  • g) This enzyme system contains copper, a component of several oxidase enzymes. (biologydiscussion.com)
  • The oxidase was functional in both dichloromethane and hexane, suggesting that this enzyme system may have applications for organic synthesis of aldehydes. (psu.edu)
  • Under this approach, an aldehyde (1) is reacted with a primary amine (2) to form an imine intermediate (3) which then gets selectively reduced to the wanted secondary amine product (4). (chembites.org)
  • Catalyzes the oxidative deamination of neurotransmitters and biogenic amines. (expasy.org)