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.
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.
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.
A purine base found in most body tissues and fluids, certain plants, and some urinary calculi. It is an intermediate in the degradation of adenosine monophosphate to uric acid, being formed by oxidation of hypoxanthine. The methylated xanthine compounds caffeine, theobromine, and theophylline and their derivatives are used in medicine for their bronchodilator effects. (Dorland, 28th ed)
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)
Oxidoreductases that are specific for ALDEHYDES.
Organic compounds containing a carbonyl group in the form -CHO.
Oxidoreductases that are specific for KETONES.
Purine bases found in body tissues and fluids and in some plants.
Compounds based on pyrazino[2,3-d]pyrimidine which is a pyrimidine fused to a pyrazine, containing four NITROGEN atoms.
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.
Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)
Tungsten. A metallic element with the atomic symbol W, atomic number 74, and atomic weight 183.85. It is used in many manufacturing applications, including increasing the hardness, toughness, and tensile strength of steel; manufacture of filaments for incandescent light bulbs; and in contact points for automotive and electrical apparatus.
A XANTHINE OXIDASE inhibitor that decreases URIC ACID production. It also acts as an antimetabolite on some simpler organisms.
Inorganic compounds that contain tungsten as an integral part of the molecule.
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).
A genus of gram-negative, anaerobic cocci parasitic in the mouth and in the intestinal and respiratory tracts of man and other animals.
A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
A 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 xanthine oxidase inhibitor.
The white liquid secreted by the mammary glands. It contains proteins, sugar, lipids, vitamins, and minerals.
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)
A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
The rate dynamics in chemical or physical systems.
A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
Non-pathogenic ovoid to rod-shaped bacteria that are widely distributed and found in fresh water as well as marine and hypersaline habitats.
Enzymes which transfer sulfur atoms to various acceptor molecules. EC 2.8.1.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Catalyzes the reduction of tetrazolium compounds in the presence of NADH.
Dithionite. The dithionous acid ion and its salts.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
An oxidation product, via XANTHINE OXIDASE, of oxypurines such as XANTHINE and HYPOXANTHINE. It is the final oxidation product of purine catabolism in humans and primates, whereas in most other mammals URATE OXIDASE further oxidizes it to ALLANTOIN.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
A series of heterocyclic compounds that are variously substituted in nature and are known also as purine bases. They include ADENINE and GUANINE, constituents of nucleic acids, as well as many alkaloids such as CAFFEINE and THEOPHYLLINE. Uric acid is the metabolic end product of purine metabolism.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.
A plant genus of the family RUTACEAE. Members contain quinoline alkaloids.
Compounds based on 2-amino-4-hydroxypteridine.
An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
2-Amino-1,5-dihydro-4,6-pteridinedione. Pigment first discovered in butterfly wings and widely distributed in plants and animals.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Derivatives of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton. Flavin derivatives serve an electron transfer function as ENZYME COFACTORS in FLAVOPROTEINS.
Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.
A species of imperfect fungi from which the antibiotic nidulin is obtained. Its teleomorph is Emericella nidulans.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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 1.4.3.4.
Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.
An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14
Large woodland game BIRDS in the subfamily Meleagridinae, family Phasianidae, order GALLIFORMES. Formerly they were considered a distinct family, Melegrididae.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.
The 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.
An enzyme oxidizing peptidyl-lysyl-peptide in the presence of water & molecular oxygen to yield peptidyl-allysyl-peptide plus ammonia & hydrogen peroxide. EC 1.4.3.13.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
The sum of the weight of all the atoms in a molecule.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
An enzyme of the oxidoreductase class that catalyzes the conversion of beta-D-glucose and oxygen to D-glucono-1,5-lactone and peroxide. It is a flavoprotein, highly specific for beta-D-glucose. The enzyme is produced by Penicillium notatum and other fungi and has antibacterial activity in the presence of glucose and oxygen. It is used to estimate glucose concentration in blood or urine samples through the formation of colored dyes by the hydrogen peroxide produced in the reaction. (From Enzyme Nomenclature, 1992) EC 1.1.3.4.
A species of fruit fly much used in genetics because of the large size of its chromosomes.
Potent cholinesterase inhibitor used as an insecticide and acaricide.
A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.
"ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis ...
... in molybdenum cofactor biosynthesis causes absence of enzyme activity of xanthine dehydrogenase/oxidase and aldehyde oxidase. ... Sulfite oxidase Reiss J, Johnson JL (June 2003). "Mutations in the molybdenum cofactor biosynthetic genes MOCS1, MOCS2, and ... Usually this leads to death within months of birth, due to the lack of active sulfite oxidase. Furthermore, a mutational block ... xanthine, and uric acid in urine. Additionally, the disease produces characteristic MRI images that can aid in diagnosis. ...
... xanthine dehydrogenase/oxidase and aldehyde oxidase. Fosdenopterin was developed by José Santamaría-Araujo and Guenter Schwarz ... cPMP is a precursor to molybdopterin, which is required for the enzyme activity of sulfite oxidase, ...
... which is essential for the activity of enzymes like xanthine dehydrogenase, aldehyde oxidase, and sulfite oxidase in humans. ... xanthine oxidase, and aldehyde oxidase. Symptoms of MoCo deficiency are linked to the accumulation of toxic metabolites caused ... MoCo deficiency in humans results in the combined deficiency of the MoCo-containing enzymes: sulfite oxidase, ... by the reduced activity of these molybdoenzymes, especially sulfite oxidase. Genetic defects in MoCo biosynthesis lead to MoCo ...
... xanthine dehydrogenase, sulfite oxidase (mitochondrial precursor), aldehyde oxidase, erythropoietin receptor precursor and the ...
"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion". ... may result from a failure of the mechanism which inserts sulfur into the active sites of xanthine oxidase and aldehyde oxidase ... explaining why xanthine oxidase is being researched for links to cardiovascular health. Both xanthine oxidase and xanthine ... Because xanthine oxidase is a metabolic pathway for uric acid formation, the xanthine oxidase inhibitor allopurinol is used in ...
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain MOCOS Xanthine oxidase GRCh38: Ensembl release 89: ... xanthine-NAD+ oxidoreductase, xanthine/NAD+ oxidoreductase, and xanthine oxidoreductase. Defects in xanthine dehydrogenase ... Xanthine dehydrogenase can be converted to xanthine oxidase by reversible sulfhydryl oxidation or by irreversible proteolytic ... Xanthine dehydrogenase, also known as XDH, is a protein that, in humans, is encoded by the XDH gene. Xanthine dehydrogenase ...
... and xanthine dehydrogenase, a/b hammerhead domain Gordon AH, Green DE, Subrahmanyan V (May 1940). "Liver ... 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 ...
"Analysis of aldehyde oxidase and xanthine dehydrogenase/oxidase as possible candidate genes for autosomal recessive familial ... Aldehyde oxidase 1 is an enzyme that in humans is encoded by the AOX1 gene. Aldehyde oxidase produces hydrogen peroxide and, ... 1993). "cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase". Proc ... "Entrez Gene: aldehyde oxidase 1". Berger R, Mezey E, Clancy KP, Harta G, Wright RM, Repine JE, Brown RH, Brownstein M, ...
Sagi M, Fluhr R, Lips SH (1999). "Aldehyde oxidase and xanthine dehydrogenase in a flacca tomato mutant with deficient abscisic ... In enzymology, an abscisic-aldehyde oxidase (EC 1.2.3.14) is an enzyme that catalyzes the chemical reaction abscisic aldehyde ... Seo M, Koiwai H, Akaba S, Komano T, Oritani T, Kamiya Y, Koshiba T (2000). "Abscisic aldehyde oxidase in leaves of Arabidopsis ... Koornneef M, Kamiya Y, Koshiba T (2000). "The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in ...
"Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas". Science. 270 (5239): 1170-6. Bibcode ... an aldehyde dehydrogenase (FAD-independent) (EC 1.2.99.7) is an enzyme that catalyzes the chemical reaction an aldehyde + H2O ... Other names in common use include aldehyde oxidase, aldehyde oxidoreductase, Mop, and AORDd. As of late 2007, only one ... Fujishiro K, Aisaka K, Uwajima T (2003). "Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690 ...
Alcohol dehydrogenase. *Aldehyde ferredoxin oxidoreductase. *Aldehyde oxidase. *Aldehyde oxidase and xanthine dehydrogenase, a/ ...
... xanthine oxidase (N-terminal), phthalate dioxygenase reductase (C-terminal), succinate dehydrogenase iron-sulphur protein (N- ... This conserved region is also found as a domain in various metabolic enzymes and in multidomain proteins, such as aldehyde ... Reactions that reduce Fd include the oxidation of aldehydes to acids like the glyceraldehyde to glycerate reaction (-580 mV), ... the carbon monoxide dehydrogenase reaction (-520 mV), and the 2-oxoacid:Fd Oxidoreductase reactions (-500 mV) like the reaction ...
... carbon monoxide dehydrogenase, aldehyde oxidase. Prosthetic group of: formate dehydrogenase, purine hydroxylase, thiosulfate ... xanthine oxidase, DMSO reductase, sulfite oxidase, nitrate reductase, ethylbenzene dehydrogenase, glyceraldehyde-3-phosphate ... Enzymes that contain the molybdopterin cofactor include xanthine oxidase, DMSO reductase, sulfite oxidase, and nitrate ... In some enzymes, such as xanthine oxidase, the metal is bound to one molybdopterin, whereas, in other enzymes, e.g., DMSO ...
Other enzymes capable of producing superoxide are xanthine oxidase, NADPH oxidases and cytochromes P450. Hydrogen peroxide is ... and aldehyde dehydrogenases. The amino acid methionine is prone to oxidation, but oxidized methionine can be reversible. ... succinate dehydrogenase, and aspartate oxidase". J. Biol. Chem. 277 (45): 42563-71. doi:10.1074/jbc.M204958200. PMID 12200425. ... Cho KJ, Seo JM, Kim JH (July 2011). "Bioactive lipoxygenase metabolites stimulation of NADPH oxidases and reactive oxygen ...
... and xanthine oxidase involved in purine nucleotide catabolism. Noncatalytic functions that FAD can play in flavoproteins ... isovaleryl-CoA dehydrogenase), isoleucine, (short/branched-chain acyl-CoA dehydrogenase), valine (isobutyryl-CoA dehydrogenase ... MAO oxidizes primary, secondary and tertiary amines, which nonenzymatically hydrolyze from the imine to aldehyde or ketone. ... components of the succinate dehydrogenase complex, α-ketoglutarate dehydrogenase, and a component of the pyruvate dehydrogenase ...
... malate dehydrogenase (nadp+) MeSH D08.811.682.047.892 - xanthine dehydrogenase MeSH D08.811.682.047.928 - xanthine oxidase MeSH ... aldehyde dehydrogenase MeSH D08.811.682.657.163.249.750 - omega-crystallins MeSH D08.811.682.657.163.311 - aldehyde oxidase ... alanine dehydrogenase MeSH D08.811.682.664.500.125 - d-amino-acid oxidase MeSH D08.811.682.664.500.261 - d-aspartate oxidase ... glycine dehydrogenase MeSH D08.811.682.664.500.677 - l-amino acid oxidase MeSH D08.811.682.664.500.724 - leucine dehydrogenase ...
A Replica of a Fishy Enzyme and the reduced xanthine oxidase also have been made. Inhibition patterns in the Michaelis complex ... functional model for the tungsten-formate dehydrogenase of Clostridium thermoaceticum". Proceedings of the Indian Academy of ... "Modeling the Tungsten Sites of Inactive and Active Forms of Hyperthermophilic Pyrococcus furiosus Aldehyde Ferredoxin ... Mitra, Joyee; Sarkar, Sabyasachi (5 February 2013). "Modelling the reduced xanthine oxidase in active sulfo and inactive ...
Xanthine oxidase. 1.1.4: disulfide as acceptor. *Vitamin K epoxide reductase. *Vitamin-K-epoxide reductase (warfarin- ... a group of dehydrogenase enzymes that occur in many organisms and facilitate the conversion from a carbohydrate to an aldehyde ... Carbohydrate dehydrogenases are the most common quinoprotein oxidoreductases,[1] which are enzymes that oxidize a wide range of ... An example includes L-gulonolactone oxidase.. They are categorized under EC number 1.1. More specifically, they are in three ...
Nicotinate dehydrogenase (cytochrome) EC 1.17.2.1. *Category:EC 1.17.3 *Xanthine oxidase EC 1.17.3.2 ... Category:EC 1.2 (act on the aldehyde or oxo group of donors)Edit. *Category:EC 1.2.1 (with NAD+ or NADP+ as acceptor) * ... Category:EC 2.2 (transfer aldehyde or ketone groups)Edit. *Category:EC 2.2.1 *Transketolase EC 2.2.1.1 ... Category:EC 1.13.12 (With incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases)) * ...
Xanthine oxidase. 1.1.4: disulfide as acceptor. *Vitamin K epoxide reductase. *Vitamin-K-epoxide reductase (warfarin- ... Malate dehydrogenase (NADP+). *Malate dehydrogenase (oxaloacetate-decarboxylating). *Malate dehydrogenase (oxaloacetate- ...
Xanthine oxidase. 1.1.4: disulfide as acceptor. *Vitamin K epoxide reductase. *Vitamin-K-epoxide reductase (warfarin- ... Hydroxyacyl-Coenzyme A dehydrogenase. To acetyl-CoA. *Malonyl-CoA decarboxylase. Aldehydes. *Long-chain-aldehyde dehydrogenase ...
The oxidases xanthine oxidase, aldehyde oxidase, and sulfite oxidase[31] Legumes, whole grains, nuts[25] molybdenum deficiency ... Pervasive and required for several enzymes such as carboxypeptidase, liver alcohol dehydrogenase, and carbonic anhydrase ... Required component of many redox enzymes, including cytochrome c oxidase Liver, seafood, oysters, nuts, seeds; some: whole ...
... pteridine oxidase EC 1.17.3.2: xanthine oxidase EC 1.17.3.3: 6-hydroxynicotinate dehydrogenase EC 1.17.4.1: ribonucleoside- ... aldehyde dehydrogenase (NAD+) EC 1.2.1.4: aldehyde dehydrogenase (NADP+) EC 1.2.1.5: aldehyde dehydrogenase (NAD(P)+) EC 1.2. ... benzaldehyde dehydrogenase (NAD+) EC 1.2.1.29: aryl-aldehyde dehydrogenase EC 1.2.1.30: aryl-aldehyde dehydrogenase (NADP+) EC ... 4-hydroxyphenylpyruvate oxidase EC 1.2.3.14: Abscisic-aldehyde oxidase EC 1.2.4.1: pyruvate dehydrogenase (acetyl-transferring ...
Xanthine oxidase. 1.1.4: disulfide as acceptor. *Vitamin K epoxide reductase. *Vitamin-K-epoxide reductase (warfarin- ... In Arabidopsis thaliana, the enzyme uses sinapaldehyde or coniferyl aldehyde or coumaraldehyde and NADPH to produce sinapyl ... Malate dehydrogenase (NADP+). *Malate dehydrogenase (oxaloacetate-decarboxylating). *Malate dehydrogenase (oxaloacetate- ...
Xanthine oxidase. 1.1.4: disulfide as acceptor. *Vitamin K epoxide reductase. *Vitamin-K-epoxide reductase (warfarin- ... alcohol dehydrogenase (NADP+) activity. • retinal dehydrogenase activity. • allyl-alcohol dehydrogenase activity. • NADP- ... cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases". The Journal of Biological Chemistry. 264 (16 ... AR belongs to the aldehyde-keto reductase superfamily, with a widely expression in human organs including the kidney, lens, ...
Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead (IPR000674). Short name: Ald_Oxase/Xan_DH_a/b ... The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain [PMID: ... Aldehyde oxidase (EC:1.2.3.1) catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and ... Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas.. Science 270 1170-6 1995 ...
Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain The name of this superfamily has been modified since the ...
... xanthine dehydrogenase; AO, aldehyde oxidase; GNMT, glycine-N-methyltransferase. ... S-sulphocysteine may not be detectable in plasma using routine methods in sulfite oxidase and molybdenum co-factor deficiencies ... Taurine, low cystine (B, U), elevated hypoxanthine and xanthine (U), low uric acid (B). ... CBS, cystathionine beta synthase; AdoHcyas, S-adenosylhomocysteine hydroxylase; SUOX, sulfate oxidase; XDH, ...
Combined deficiency of sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. *Combined molybdoflavoprotein enzyme ... The resulting loss of enzyme activity leads to buildup of certain chemicals, including sulfite, S-sulfocysteine, xanthine, and ... Tests reveal that affected individuals have high levels of chemicals called sulfite, S-sulfocysteine, xanthine, and ... Combined xanthine oxidase and sulfite oxidase and aldehyde oxidase deficiency. *Deficiency of molybdenum cofactor ...
Aldehyde ferredoxin oxidoreductase, C-terminal (IPR001203) Pfam signature: PF01314 Aldehyde oxidase/xanthine dehydrogenase, a/b ... Aldehyde dehydrogenase domain (IPR015590) Pfam signature: PF00171 Zn(2)-C6 fungal-type DNA-binding domain (IPR001138) Pfam ... 6-phosphogluconate dehydrogenase, C-terminal (IPR006114) Pfam signature: PF00393 Multicopper oxidase, type 1 (IPR001117) Pfam ... Acyl-CoA dehydrogenase/oxidase C-terminal (IPR009075) Pfam signature: PF00441 Peptidase C19, ubiquitin carboxyl-terminal ...
Xanthine dehydrogenase and aldehyde oxidase combined deficiency. XDH deficiency. Xanthine dehydrogenase deficiency. ...
Combined Deficiency of Sulfite Oxidase Xanthine Dehydrogenase and Aldehyde Oxidase , MOCOD , MPTS , MOCO1 , Molybdopterin ...
... xanthine dehydrogenase (XDH) in purine catabolism, aldehyde oxidase (AldOx), sulfite oxidase, the mitochondrial amidoxime- ... 2001) ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in ... aldehyde oxidase; ATM3, ABC transporter of the mitochondria 3; CNX, cofactor of nitrate reductase and xanthine dehydrogenase; ... 1998) Molecular cloning and characterization of aldehyde oxidases in Arabidopsis thaliana. Plant Cell Physiol. 39, 433-442 doi: ...
... and a combined deficiency of sulfite oxidase,xanthine dehydrogenase and aldehyde oxidase ...
Molybdenum cofactor in xanthine dehydrogenase, aldehyde oxidase and pyridoxal oxidase. Mol Gen Genet 184:92-96. ... 2000) Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. ... aldehyde oxidase. DCPIP. dichlorophenolindophenol. Moco. molybdenum cofactor. RT. room temperature. SNP. single-nucleotide ... Aldehyde oxidase (AO, EC1.2.3.1) is a molybdo-flavoenzyme present in the cytosol of many tissues in mammals (Garattini et al., ...
In humans, molybdenum is a cofactor for three enzyme classes-sulfiteoxidase, aldehyde dehydrogenase, and xanthine oxidase ( ...
"Analysis of aldehyde oxidase and xanthine dehydrogenase/oxidase as possible candidate genes for autosomal recessive familial ... Aldehyde oxidase 1 is an enzyme that in humans is encoded by the AOX1 gene. Aldehyde oxidase produces hydrogen peroxide and, ... 1993). "cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase". Proc ... "Entrez Gene: aldehyde oxidase 1". Berger R, Mezey E, Clancy KP, Harta G, Wright RM, Repine JE, Brown RH, Brownstein M, ...
MOCOS sulfurates the molybdenum cofactor of xanthine dehydrogenase (XDH\; MIM 607633) and aldehyde oxidase (AOX1\; MIM 602841 ...
DE SubName: Full=Aldehyde oxidase and xanthine dehydrogenase molybdopterin binding {ECO:0000313,EMBL:ACR41141.1}; GN ...
Sagi M, Fluhr R, Lips SH (1999). "Aldehyde oxidase and xanthine dehydrogenase in a flacca tomato mutant with deficient abscisic ... In enzymology, an abscisic-aldehyde oxidase (EC 1.2.3.14) is an enzyme that catalyzes the chemical reaction abscisic aldehyde ... Seo M, Koiwai H, Akaba S, Komano T, Oritani T, Kamiya Y, Koshiba T (2000). "Abscisic aldehyde oxidase in leaves of Arabidopsis ... Koornneef M, Kamiya Y, Koshiba T (2000). "The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in ...
Neighboring with xanthine dehydrogenase (b2868). BLAST: Probable aldehyde oxidase and xanthine dehydrogenase family protein ...
ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis ... abscisic aldehyde is oxidized to ABA by aldehyde oxidase 3 (encoded by AAO3) in the presence of a molybdenum cofactor (MOCO) ( ... 2000). The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in abscisic acid biosynthesis in leaves ... 2002). The short-chain alcohol dehydrogenase ABA2 catalyzes the conversion of xanthoxin to abscisic aldehyde. Plant Cell 14, ...
ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis ... and is catalyzed by an abscisic aldehyde oxidase. In Arabidopsis, four homologous aldehyde oxidase (AAO) genes have been ... Abscisic aldehyde is synthesized from xanthoxin, by an enzyme belonging to short-chain dehydrogenase/reductase family, which is ... 2002). The short-chain alcohol dehydrogenase ABA2 catalyzes the conversion of xanthoxin to abscisic aldehyde. Plant Cell 14, ...
... sulphite oxidase and, possibly, also of aldehyde oxidase are described. This remarkable coincidence of three inborn errors of ... Five patients with a combined deficiency of xanthine dehydrogenase, ... Five patients with a combined deficiency of xanthine dehydrogenase, sulphite oxidase and, possibly, also of aldehyde oxidase ... an inborn error of metabolism leading to a combined deficiency of sulphite oxidase and xanthine dehydrogenase. ...
2004) Contribution of aldehyde oxidase, xanthine oxidase, and aldehyde dehydrogenase on the oxidation of aromatic aldehydes. ... aldehyde oxidase. DACA. N-[(2-dimethylamino)ethyl]acridine-4-carboxamide. DDI. drug-drug interaction. HLC. human liver cytosol ... 2010) Aldehyde oxidase: an enzyme of emerging importance in drug discovery. J Med Chem 53:8441-8460. ... Aldehyde oxidase (AO) is a member of the molybdo-flavin family of enzymes, a group that is characterized by containing ...
The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are ... Sulfite oxidase protects plants against sulfur dioxide toxicity.. Brychkova G, Xia Z, Yang G, Yesbergenova Z, Zhang Z, Davydov ... Formation of xanthine and the use of purine metabolites as a nitrogen source in Arabidopsis plants. ... Sulfite Oxidase Activity Is Essential for Normal Sulfur, Nitrogen and Carbon Metabolism in Tomato Leaves. ...
... sulphite oxidase and xanthine oxidoreductases. Nature has developed two scaffolds holding molybdenum in place, the iron- ... ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis ... Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc. ... The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in abscisic acid biosynthesis in leaves. Proc. ...
Some examples are aldehyde dehydrogenase (14), xanthine oxidase (15), and cytochrome b5 reductase (16). Borate apparently ... Roush A, Norris E. The inhibition of xanthine oxidase by borates. Arch Biochem Biophys. 1950;29:344-347 ... Deitrich R. Diphosphopyridine nucleotide-linked aldehyde dehydrogenase III. Sulfhydril characteristics of the enzyme. Arch ... NADH oxidase of plasma membranes. J Bioenerg Biomembr. 1991;23:469-489 ...
... xanthine stone disease); two types of the disease; causes, signs, and management; dog and cat breeds at risk. ... Type II xanthinuria is characterized by a deficiency of xanthine dehydrogenase and aldehyde oxidase. When there is a deficiency ... Xanthine urolithiasis in a cat: a case report and evaluation of a candidate gene for xanthine dehydrogenase. Journal of Feline ... Type I xanthinuria is the result of a deficiency of xanthine dehydrogenase enzyme. ...
ABA3 is essential for activation of the molybdenum enzymes AO and xanthine dehydrogenase (XDH). AO itself catalyzes the last ... This paper investigates the importance of Moco-sulphurase ABA3 and aldehyde oxidase (AO) on ABA-biosynthesis in Populus × ... AAO (abscisic-aldehyde oxidase), ABA (abscisic acid), AO (aldehyde oxidase), ABA2 (short-chain dehydrogenase), ABA3 (Moco- ... Domain structures of Arabidopsis thaliana aldehyde oxidases (AAOs) and Populustrichocarpa aldehyde oxidases (PtAOs). AAOs are a ...
Aldehyde oxidase and xanthine dehydrogenase in a flacca tomato mutant with deficient abscisic acid and wilty phenotype ... The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in abscisic acid biosynthesis in leaves. ... While abscisic aldehyde is the best substrate, the enzyme also acts with indole-3-aldehyde, 1-naphthaldehyde and benzaldehyde ... Acting on the aldehyde or oxo group of donors;. With oxygen as acceptor. ...
... and the enzymes xanthine and aldehyde oxidase, and succinic dehydrogenase. ... glutamic dehydrogenase, alkaline phosphatase, pyridine nucleotide dehydrogenase, alcohol dehydrogenase, superoxide dismutase, ... For example, copper is a component of the enzymes cytochrome oxidase, uricase, tyrosinase, superoxide dismutase, amine oxidase ... phosphate transferases and phosphate dehydrogenases), particularly those concerned with the citric acid cycle including ...
Xanthine dehydrogenase and aldehyde oxidase, but not sulfite oxidase and nitrate reductase, require the post-translational ... xanthine dehydrogenase, which is involved in purine catabolism and reactive oxygen production, (3) aldehyde oxidase, which ... All Mo-enzymes, except plant sulfite oxidase, need at least one more redox active center, many of them involving iron in ... In eukaryotes, the most prominent Mo-enzymes are (1) sulfite oxidase, which catalyzes the final step in the degradation of ...
Molybdopterin is the Mo cofactor for xanthine dehydrogenase/oxidase, aldehyde oxidase and sulfite oxidase enzymes. The ... Serum sorbitol, malate, isocitrate, glutamate dehydrogenases, and activities of aldolases and liver monoamine oxidase were ...
Recombinant Protein and Aldehyde oxidase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are ... Molecular Function: aldehyde oxidase activity; FAD binding; xanthine dehydrogenase activity. Biological Process: inflammatory ... Aldehyde oxidase GLOX. Aldehyde oxidase GLOX ELISA Kit. Aldehyde oxidase GLOX Recombinant. Aldehyde oxidase GLOX Antibody ... Aldehyde oxidase GLOX1. Aldehyde oxidase GLOX1 ELISA Kit. Aldehyde oxidase GLOX1 Recombinant. Aldehyde oxidase GLOX1 Antibody ...
  • The systematic name of this enzyme class is abscisic-aldehyde:oxygen oxidoreductase. (wikipedia.org)
  • Molybdenum cofactor is a cofactor required for the activity of enzymes such as sulfite oxidase, xanthine oxidoreductase, and aldehyde oxidase. (hmdb.ca)
  • Molybdenum cofactor functions directly in ethylbenzene dehydrogenase, glyceraldehyde-3-phosphate ferredoxin oxidoreductase, and respiratory arsenate reductase. (hmdb.ca)
  • Herein, we will review the current knowledge on two of those "non-dedicated nitrite reductases", the molybdoenzymes xanthine oxidoreductase and aldehyde oxidase, discussing the in vitro and in vivo studies to provide the current picture of the role of these enzymes on the NO metabolism in humans. (unl.pt)
  • Maia, LB & Moura, JJG 2018, ' Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes ', Redox Biology , vol. 19, pp. 274-289. (unl.pt)
  • Xanthine oxidase (XO, sometimes 'XAO') is a form of xanthine oxidoreductase, a type of enzyme that generates reactive oxygen species. (wikipedia.org)
  • Xanthine oxidoreductase (XOR) is a cytosolic molybdenum containing enzyme mainly responsible for final reactions of uric acid production from oxidizing oxypurines, hypoxanthine and xanthine [2-5]. (ijps.ir)
  • The thermodynamics of xanthine oxidoreductase catalysis. (thefreedictionary.com)
  • Molybdenum hydroxylases, which include aldehyde oxidase and xanthine oxidoreductase, are involved in the metabolism of some medicines in humans. (nih.gov)
  • On the other hand, xanthine oxidoreductase activity is present widely among species. (nih.gov)
  • Drug-drug interactions associated with aldehyde oxidase and xanthine oxidoreductase are of potential clinical significance. (nih.gov)
  • Mutations Associated with Functional Disorder of Xanthine Oxidoreductase and Hereditary Xanthinuria in Humans. (explainmedicine.com)
  • The Moco (molybdenum cofactor) sulfurase ABA3 from Arabidopsis thaliana catalyses the sulfuration of the Moco of aldehyde oxidase and xanthine oxidoreductase, which represents the final activation step of these enzymes. (helmholtz-hzi.de)
  • The strictly conserved Cys430 in the NifS-like domain binds a persulfide intermediate, which is abstracted from the substrate L-cysteine and finally needs to be transferred to the Moco of aldehyde oxidase and xanthine oxidoreductase. (helmholtz-hzi.de)
  • Reductive Half-Reaction of Aldehyde Oxidoreductase toward Acetaldehyde: A Combined QM/MM Study. (aroundtheyear.com)
  • Xanthine oxidoreductase and cardiovascular disease: molecular mechanisms and pathophysiological implications. (scholarena.co)
  • 10873) /locus_tag="OB2597_00040" /note="COG2080 Aerobic-type carbon monoxide dehydrogenase, small subunit CoxS/CutS homologs" /codon_start=1 /transl_table=11 /product="isoquinoline 1-oxidoreductase, alpha subunit" /protein_id="ZP_01001616.1" /db_xref="GI:84503569" /db_xref="CDD:11788" /translation="MAKLTINGAARSVDLSDEVPLLWALRDGLNMTGTKFGCGVAACG ACTVHIDGEAVRSCQVAVGDVWGPVTTIEGIGTPEDLSVLQQAWIDNQVAQCGYCQSG QIMQAAALLAETPRPTDDEIDAAMAGNLCRCGTYPRIRAAIHDAAQKMQEA" misc_feature complement(10418. (roseobase.org)
  • This activity is often found in a bifunctional enzyme with xanthine oxidase ( EC:1.1.3.22 ) activity too. (ebi.ac.uk)
  • The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups. (ebi.ac.uk)
  • 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)
  • In humans, molybdenum is a cofactor for three enzyme classes-sulfiteoxidase, aldehyde dehydrogenase, and xanthine oxidase (Kisker et al. (cdc.gov)
  • Aldehyde oxidase (AOX1) is an enzyme with broad substrate specificity, catalyzing the oxidation of a wide range of endogenous and exogenous aldehydes as well as N-heterocyclic aromatic compounds. (aspetjournals.org)
  • Aldehyde oxidase 1 is an enzyme that in humans is encoded by the AOX1 gene. (wikipedia.org)
  • 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)
  • 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)
  • Type I xanthinuria is the result of a deficiency of xanthine dehydrogenase enzyme. (gopetsamerica.com)
  • Allopurinol, an inhibitor of xanthine oxidase enzyme, is sometimes recommended to decrease urinary uric acid excretion. (gopetsamerica.com)
  • This is primarily due to the azaheterocycle-oxidase activity that the enzyme exhibits. (aspetjournals.org)
  • While abscisic aldehyde is the best substrate, the enzyme also acts with indole-3-aldehyde, 1-naphthaldehyde and benzaldehyde as substrates, but more slowly [3]. (genome.jp)
  • Two inherited forms of xanthinuria principally result from a deficiency of the enzyme xanthine dehydrogenase, which is the enzyme responsible for degrading hypoxanthine and xanthine to uric acid. (medscape.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 effects of acidic and intestinal proteolytic environments on bovine milk xanthine oxidase (XO) activity were determined in order to evaluate the extent to which this enzyme was absorbed in biologically active form. (meta.org)
  • Xanthine oxidase is defined as an enzyme activity (EC 1.17.3.2). (wikipedia.org)
  • hypoxanthine (one oxygen atom) xanthine (two oxygens) uric acid (three oxygens) Because XO is a superoxide-producing enzyme, with general low specificity, it can be combined with other compounds and enzymes and create reactive oxidants, as well as oxidize other substrates. (wikipedia.org)
  • Xanthine oxidase is a superoxide-producing enzyme found normally in serum and the lungs, and its activity is increased during influenza A infection. (wikipedia.org)
  • Type II xanthinuria may result from a failure of the mechanism which inserts sulfur into the active sites of xanthine oxidase and aldehyde oxidase, a related enzyme with some overlapping activities (such as conversion of allopurinol to oxypurinol). (wikipedia.org)
  • This is due to the genetic deficiency of enzyme, xanthine dehydrogenase [1] that is responsible for degrading hypoxanthine and xanthine to uric acid leaving excess hypoxanthine and xanthine amounts. (explainmedicine.com)
  • gigas enzyme does not catalyze electron transfer from xanthine to an artificial electron acceptor but can nonetheless oxidize xanthine (3). (jailcalls.com)
  • 2006. Plant sulfite oxidase as novel producer of H2O2 combination of enzyme catalysis with a subsequent non-enzymatic reaction step. (ac.ir)
  • The process is mediated by an enzyme called xanthine oxidase (XO). (aroundtheyear.com)
  • Here, copper's ability to alter XO activity and structure was investigated in vitro after pre-incubation of the enzyme with … 171 Under normophysiological circumstances, the circulating XO concentration is low (10%-20%) and the isoform xanthine dehydrogenase (XDH) predominates. (aroundtheyear.com)
  • Sulfite oxidase, the most significant molybdenum-dependent enzyme in humans, makes sulfite oxidize into sulfate, the last step in the metabolism of sulfur-containing amino acids. (megavitamins.com.au)
  • There are only a few Moco enzymes known in eukaryotes: xanthine dehydrogenase (XDH) in purine catabolism, aldehyde oxidase (AldOx), sulfite oxidase, the mitochondrial amidoxime-reducing components mARC1 and mARC2, and nitrate reductase [ 3 , 4 ]. (biochemj.org)
  • The trace element molybdenum is essential for nearly all organisms and forms the catalytic centre of a large variety of enzymes such as nitrogenase, nitrate reductases, sulphite oxidase and xanthine oxidoreductases. (nature.com)
  • When there is a deficiency of one or two enzymes, xanthine accumulates in the plasma and urine and causes disorders of blood vessels, muscles, kidneys, bladder stones, and kidney failure . (gopetsamerica.com)
  • ABA3 is essential for activation of the molybdenum enzymes AO and xanthine dehydrogenase (XDH). (scirp.org)
  • Aldehyde oxidase (AO) is a member of the molybdo-flavin family of enzymes, a group that is characterized by containing molybopterin and FAD groups that are essential for catalytic activity. (aspetjournals.org)
  • All Mo-enzymes, except plant sulfite oxidase, need at least one more redox active center, many of them involving iron in electron transfer. (nih.gov)
  • This condition is inherited recessively and is caused by a congenital defect of a molybdenum-containing cofactor essential for the function of 3 distinct enzymes (ie, xanthine dehydrogenase, aldehyde oxidase, sulfite oxidase). (medscape.com)
  • Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. (uniprot.org)
  • Molybdenum cofactor, which contains the element molybdenum, is essential to the function of several enzymes called sulfite oxidase, aldehyde oxidase, xanthine dehydrogenase, and mitochondrial amidoxime reducing component (mARC). (nih.gov)
  • These enzymes catalyze the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. (wikipedia.org)
  • Aldehyde oxidases are a group of enzymes with important functions in the context of drug and xenobiotic metabolism. (unl.pt)
  • The molybdenum cofactor sulfurase ABA3 from Arabidopsis thaliana specifically regulates the activity of the molybdenum enzymes aldehyde oxidase and xanthine dehydrogenase by converting their molybdenum cofactor from the desulfo-form into the sulfo-form. (meta.org)
  • In vitro, the NifS-like domain of ABA3 activates aldehyde oxidase and xanthine dehydrogenase in the absence of the C-terminal domain, but in vivo, the C-terminal domain is required for proper activation of both target enzymes. (meta.org)
  • The xanthine oxidase family is the largest and most diverse group of molybdenum cofactor (Mo-co)-containing enzymes, which usually transfer an oxygen atom to or from a substrate in a two-electron transfer reaction (7). (jailcalls.com)
  • Enzymic determination of inorganic phosphates, organic phosphates and phosphate-liberating enzymes by use of nucleoside phosphorylase-xanthine oxidase (dehydrogenase)-coupled reactions. (scholarena.co)
  • Enzymes that contain the molybdopterin cofactor include xanthine oxidase, DMSO reductase, sulfite oxidase, and nitrate reductase. (wikipedia.org)
  • Tungsten-using enzymes typically reduce free carboxylic acids to aldehydes. (wikipedia.org)
  • The ABA2 gene product belongs to the family of short-chain dehydrogenases/reductases, which are known to be NAD- or NADP-dependent oxidoreductases. (plantcell.org)
  • Aldehyde oxidases (AOXs) and xanthine oxidoreductases (XORs) are structurally and evolutionarily linked molybdoflavoproteins. (unl.pt)
  • Purification and Characterisation of Xanthine Oxidoreductases from Local Bovids in Malta. (scholarena.co)
  • Although a tungsten-containing xanthine dehydrogenase from bacteria has been found to contain tungsten-molybdopterin and also non-protein-bound selenium (thus removing the possibility of selenium in selenocysteine or selenomethionine form), a tungsten-selenium molybdopterin complex has not been definitively described. (wikipedia.org)
  • Xanthinuria is a descriptive term for excess urinary excretion of xanthine. (gopetsamerica.com)
  • Type II xanthinuria is characterized by a deficiency of xanthine dehydrogenase and aldehyde oxidase . (gopetsamerica.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)
  • Xanthinuria is a rare genetic disorder where the lack of xanthine oxidase leads to high concentration of xanthine in blood and can cause health problems such as renal failure. (wikipedia.org)
  • Type I xanthinuria has been traced directly to mutations of the XDH gene which mediates xanthine oxidase activity. (wikipedia.org)
  • Type II xanthinuria, a type of classical xanthinuria (see this term), is a rare autosomal recessive disorder of purine metabolism (see this term) characterized by the deficiency of both xanthine dehydrogenase and aldehyde oxidase, leading to the formation of urinary xanthine urolithiasis and leading, in some patients, to kidney failure. (cdc.gov)
  • An important gene associated with Hereditary Xanthinuria is XDH (Xanthine Dehydrogenase), and among its related pathways/superpathways are Metabolism and Thiopurine Pathway, Pharmacokinetics/Pharmacodynamics . (malacards.org)
  • Xanthinuria is excess urinary excretion of the xanthine which is a hereditary condition. (explainmedicine.com)
  • Tests reveal that affected individuals have high levels of chemicals called sulfite, S-sulfocysteine, xanthine, and hypoxanthine in the urine and low levels of a chemical called uric acid in the blood. (medlineplus.gov)
  • The following chemical reactions are catalyzed by xanthine oxidase: hypoxanthine + H2O + O2 ⇌ {\displaystyle \rightleftharpoons } xanthine + H2O2 xanthine + H2O + O2 ⇌ {\displaystyle \rightleftharpoons } uric acid + H2O2 Xanthine oxidase can also act on certain other purines, pterins, and aldehydes. (wikipedia.org)
  • In the reaction with xanthine to form uric acid, an oxygen atom is transferred from molybdenum to xanthine, whereby several intermediates are assumed to be involved. (wikipedia.org)
  • Because xanthine oxidase is a metabolic pathway for uric acid formation, the xanthine oxidase inhibitor allopurinol is used in the treatment of gout. (wikipedia.org)
  • Catalyzes the conversion of hypoxanthine to xanthine and then to uric acid. (thefreedictionary.com)
  • It is characterized by high levels of a compound called xanthine and very low levels of another compound called uric acid in the blood and urine. (malacards.org)
  • Information about how to use the RightsLink permission system can be found at XO produces uric acid and hydrogen peroxide from xanthine or hypoxanthine. (aroundtheyear.com)
  • Xanthine oxidase (xanthine dehydrogenase) deficiency, type I, is an uncommon autosomal recessive disorder characterized by the excretion of urinary xanthine and hypoxanthine as the chief end products of purine metabolism, and by low serum and urinary uric acid levels. (aroundtheyear.com)
  • fluorescence approach for the determination of uric acid and monitoring of xanthine oxidase activity. (aroundtheyear.com)
  • Xanthine Oxidase (XO) located predominantly in the liver and intestine in mammalian tissues and catalyzes the hydroxylation of hypoxanthine to xanthine and then to uric acid and hydrogen peroxide. (aroundtheyear.com)
  • Absence of hepatic molybdenum cofactor: an inborn error of metabolism leading to a combined deficiency of sulphite oxidase and xanthine dehydrogenase. (biomedsearch.com)
  • Sulfite Oxidase Activity Is Essential for Normal Sulfur, Nitrogen and Carbon Metabolism in Tomato Leaves. (nih.gov)
  • Xanthine is a nitrogenous by-product of the metabolism of certain proteins. (gopetsamerica.com)
  • Since xanthine oxidase is involved in the metabolism of 6-mercaptopurine, caution should be taken before administering allopurinol and 6-mercaptopurine, or its prodrug azathioprine, in conjunction. (wikipedia.org)
  • The effect of ischemia/reperfusion on adenine nucleotide metabolism and xanthine oxidase production in skeletal muscle. (thefreedictionary.com)
  • Because molybdenum - as an essential cofactor for sulfite oxidase - enhances sulfite metabolism, supplementation with molybdenum glycinate benefits individuals who suffer sensitivity to sulfites used in meat, fish, salad bar items, and dehydrated fruits and vegetables. (iherb.com)
  • 1978. Combined deficiency of xanthine oxidase and sulphite oxidase: a defect of molybdenum metabolism or transport? (ac.ir)
  • Inhibitory Effect of Ruta graveolens L. Extract on Guinea Pig Liver and Bovine Milk Xanthine Oxidase', Iranian Journal of Pharmaceutical Sciences , 5(3), pp. 163-170. (ijps.ir)
  • Distribution of milk xanthine oxidase activity in desi cows, SRTMU's RES. (scholarena.co)
  • The goal of this study was to provide a reasonable assessment of how probe substrate selection may impact the results of in vitro aldehyde oxidase (AO) inhibition experiments. (aspetjournals.org)
  • The relevance of these data to the mechanistic understanding of aldehyde oxidase inhibition and potential implications on drug-drug interactions is discussed. (aspetjournals.org)
  • Inhibition of xanthine dehydrogenase by allopurinol may lead to accumulation and urinary excretion of xanthine. (medscape.com)
  • The inhibition of XO by folic acid and the relative affinities of XO for the oxidation of palmitaldehyde, stearaldehyde, and xanthine were compared. (meta.org)
  • Bovine xanthine oxidase (from milk) was originally thought to have a binding site to reduce cytochrome c with, but it has been found that the mechanism to reduce this protein is through XO's superoxide anion byproduct, with competitive inhibition by carbonic anhydrase. (wikipedia.org)
  • Inhibition of xanthine oxidase has been proposed as a mechanism for improving cardiovascular health. (wikipedia.org)
  • Xanthine oxidase activity was expressed as percent inhibition of xanthine oxidase, calculated as (1 - B/A) x100, where A is the change in absorbance of the assay without the plant extract (Dabs. (thefreedictionary.com)
  • 6 g) exhibited significant xanthine oxidase inhibition activity at 150 ug/ml as compared to the reference standard allopurinol 67. (thefreedictionary.com)
  • Research Article Evaluation of Anti-MRSA and Xanthine Oxidase Inhibition Activities of Phenolic Constituents from Plumula nelumbinis XiaoDing, 1,2 Ming-AnOuyang, 1,3 andYuan-ShuaiShen 3 Key Laboratory of Bio-Pesticide and Chemistry-Biology, Ministry of … Catalyzes the oxidation of hypoxanthine to xanthine. (aroundtheyear.com)
  • Xanthine Oxidase: Isolation, Assays of Activity, and Inhibition. (scholarena.co)
  • The distinction between the 2 types is based on the ability or inability to oxidize allopurinol, a substrate for xanthine dehydrogenase and aldehyde oxidase. (medscape.com)
  • however, allopurinol is not converted in patients with type II, who lack aldehyde oxidase activity. (medscape.com)
  • Patients with Lesch-Nyhan syndrome or patients with partial HGPRT deficiency have developed xanthine nephropathy, acute kidney failure, and stones following treatment with allopurinol. (medscape.com)
  • [ 3 ] A few incidents of xanthine nephropathy and renal failure have been reported in patients treated with allopurinol during chemotherapy for malignancy. (medscape.com)
  • A study found that patients with chronic obstructive pulmonary disease (COPD) had a decrease in oxidative stress, including glutathione oxidation and lipid peroxidation, when xanthine oxidase was inhibited using allopurinol. (wikipedia.org)
  • In type I, the conversion of allopurinol to oxypurinol is not impaired, whereas in type II the additional deficiency of aldehyde oxidase blocks the conversion of allopurinol to oxypurinol. (jailcalls.com)
  • Current research on xanthine oxidase has favored a mechanism involving base-catalyzed proton abstraction from a Mo−OH group, allowing nucleophilic attack on the substrate and hydride transfer from the substrate to MoS group in the active site. (aroundtheyear.com)
  • Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. (nature.com)
  • 2013. Metabolic stroke in a late-onset form of isolated sulfite oxidase deficiency. (ac.ir)
  • Mutations in the gene for sulfite oxidase ( SUOX ) produce a similar phenotype to that produced by molybdenum cofactor deficiency (MCD). (endocrinologyadvisor.com)
  • The same protein, which in humans has the HGNC approved gene symbol XDH, can also have xanthine dehydrogenase activity (EC 1.17.1.4). (wikipedia.org)
  • The XOR predominantly exists as xanthine dehydrogenase (XD, EC 1.17.1.4) in liver and intestine, but it is occasionally converted to xanthine oxidase (XO, EC 1.17.3.2) either by oxidation of SH-group of cystein residue 535 and 992 [6], reversibly or due to proteolytic reaction with Ca 2+ -stimulated protease, irreversibly [7, 8]. (ijps.ir)
  • Isolation of different animal liver xanthine oxidase containing fractions and determination of kinetic parameters for xanthine. (scholarena.co)
  • Purification and characterization of mouse liver xanthine oxidase. (scholarena.co)
  • They include aldehyde oxidase ( EC 1.2.3.1 ), that converts an aldehyde and water to an acid and hydrogen peroxide, and xanthine dehydrogenase ( EC 1.1.1.204 ), that converts xanthine to urate. (embl.de)
  • Holmes, R.S., 1978b, Genetics and ontogeny of aldehyde dehydrogenase isozymes in the mouse: localization of Ahd-1 encoding the mitochondrial isozymes on chromosome 4, Biochem. (springer.com)
  • Activity of the plant mitochondrial alternative oxidase (AOX) can be regulated by organic acids, notably pyruvate. (biomedsearch.com)
  • Purification of xanthine oxidase from bovine milk by affinity chromatography with a novel gel. (scholarena.co)
  • Human aldehyde oxidase (hAOX1): structure determination of the Moco-free form of the natural variant G1269R and biophysical studies of single nucleotide polymorphisms. (uni-potsdam.de)
  • The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain [ PMID: 7502041 , PMID: 10430865 ]. (ebi.ac.uk)
  • Recombinant ABA2 protein produced in Escherichia coli exhibits a K m value for xanthoxin of 19 μM and catalyzes in a NAD-dependent manner the conversion of xanthoxin to abscisic aldehyde, as determined by HPLC-mass spectrometry. (plantcell.org)
  • Most of the protein in the liver exists in a form with xanthine dehydrogenase activity, but it can be converted to xanthine oxidase by reversible sulfhydryl oxidation or by irreversible proteolytic modification. (wikipedia.org)
  • The central domain of eukaryotic succinate dehydrogenase (ubiquinone) iron- sulfur protein. (expasy.org)
  • Finally direct and mediated spectroelectrochemistry protein with high structure complexity such as the xanthine dehydrogenase from Rhodobacter capsulatus and its high homologues the mouse aldehyde oxidase homolog 1. (uni-potsdam.de)
  • Deficiency of xanthine dehydrogenase results in plasma accumulation and excess urinary excretion of the highly insoluble xanthine, which may lead to arthropathy, myopathy, crystal nephropathy, urolithiasis, or renal failure. (medscape.com)
  • Catalyzes the oxidation of aldehydes to the corresponding carboxylic acids by coupling the reaction to the reduction of dioxygen to hydrogen peroxide. (mybiosource.com)
  • Complex metalloprotein that catalyzes oxidative hydroxylation of a variety of aromatic heterocycles and simple aldehydes. (aroundtheyear.com)
  • Disease description A disorder characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. (aroundtheyear.com)
  • Identification and biochemical characterization of Arabidopsis thaliana sulfite oxidase. (nature.com)
  • We report here on the molecular cloning of GLUCOSE INSENSITIVE1 ( GIN1 ) and ABSCISIC ACID DEFICIENT2 ( ABA2 ) which encodes a unique Arabidopsis short-chain dehydrogenase/reductase (SDR1) that functions as a molecular link between nutrient signaling and plant hormone biosynthesis. (plantcell.org)
  • ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana. (helmholtz-hzi.de)
  • Kidney complications are initiated by the formation of xanthine crystals in the tubules, leading to stone formation. (gopetsamerica.com)
  • Xanthine can form crystals in the tubules, later parenchymal deposits and calculi formation. (explainmedicine.com)
  • Blair AH, Bodley FH (1969) Human liver aldehyde dehydrogenase: partial purification and properties. (springer.com)
  • Xanthine Oxidase from Human Liver: Purification and Characterization. (scholarena.co)
  • Purification and characterization of xanthine oxidase from liver of the water buffalo Bubalus bubalis. (scholarena.co)
  • Novel affinity purification of xanthine oxidase from Arthrobacter M3. (scholarena.co)
  • Purification and characterization of xanthine oxidase from livers of vitamin e deficient rabbits. (scholarena.co)
  • Aldehyde oxidase is a candidate gene for amyotrophic lateral sclerosis. (wikipedia.org)
  • Xanthine urolithiasis in a cat: a case report and evaluation of a candidate gene for xanthine dehydrogenase. (gopetsamerica.com)
  • Moreover, by microarray analysis we found that an ACC oxidase (ACO) was significantly upregulated in the aba2 mutant, whereas the 9-CIS-EPOXYCAROTENOID DIOXYGENASE 3 (NCED3) gene in ein2 was upregulated, and both the ABSCISIC ACID INSENSITIVE1 (ABI1) and cytochrome P450, family 707, subfamily A, polypeptide 2 (CYP707A2) genes in etr1-1 were downregulated. (deepdyve.com)
  • Holmes, R. S., 1977, The genetics of a-hydroxyacid oxidase and alcohol dehydrogenase in the mouse: evidence for multiple gene loci and linkage between Hao-2 and Adh-3, Genetics 87:709. (springer.com)
  • Holmes, R. S., 1979a, Genetics and ontogeny of alcohol dehydrogenase isozymes in the mouse - evidence for a cis-acting regulator gene (Adh-3-t) controlling C 2 isozyme expression in reproductive tissues and close linkage of Adh-3 and Adh-3-t on chromosome 3, Biochem. (springer.com)
  • Recently, the sitiens gene was identified as an aldehyde oxidase apoenzyme [ 10 ], completing the genetic identification of all three tomato ABA-deficient mutants. (biomedcentral.com)
  • Polyphenol oxidase (PPO) of nettle (Urtica dioica L.) was extracted and purified through (NH4)2SO4 precipitation, dialysis, and CM-Sephadex ion-exchange chromatography and was used for its characterization. (biomedsearch.com)
  • Xanthine dehydrogenase ( EC:1.1.1.204 ) catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. (ebi.ac.uk)
  • Xanthine + H(2)O + O(2) = urate + H(2)O(2). (ebi.ac.uk)
  • Other substrates that are oxidized by aldehyde oxidase, such as pyrazinamide and N -methylnicotinamide, can be used to distinguish between types I and II. (medscape.com)
  • We also identified a mutant allele in CNX2 , cofactor of nitrate reductase and xanthine dehydrogenase 2 , encoding GTP 3′,8-cyclase, the first step in Moco biosynthesis which is localized in the mitochondria. (biochemj.org)
  • Xanthine dehydrogenase and aldehyde oxidase, but not sulfite oxidase and nitrate reductase, require the post-translational sulfuration of their Mo-site for becoming active. (nih.gov)
  • Aldehyde oxidase produces hydrogen peroxide and, under certain conditions, can catalyze the formation of superoxide. (wikipedia.org)
  • Another reaction catalyzed by xanthine oxidase is the decomposition of S-Nitrosothiols (RSNO), a reactive nitrogen species, to nitric oxide (NO), which reacts with a superoxide anion to form peroxynitrite under aerobic conditions. (wikipedia.org)
  • Superoxide production by an unusual aldehyde oxidase in guinea pig granulocytes. (ac.ir)
  • Prosthetic group of: formate dehydrogenase, purine hydroxylase, thiosulfate reductase. (wikipedia.org)
  • Six genes, POX1 through POX6, encode six acyl-CoA oxidase isozymes in Y. lipolytica. (biomedsearch.com)
  • Xanthine oxidase family genes in E. coli. (jailcalls.com)
  • Flavonoids could serve as potent inhibitors of xanthine oxidase (XO). (ijps.ir)
  • Synthesis and evaluation of naphthoflavones as a new class of non purine xanthine oxidase inhibitors. (aroundtheyear.com)
  • Xanthine oxidase inhibitors: a patent survey. (aroundtheyear.com)
  • Aldehyde oxidase ( EC:1.2.3.1 ) catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. (ebi.ac.uk)
  • Agarwal DP, Harada S, Goedde HW (1981) Racial differences in biological sensitivity to ethanol: the role of alcohol dehydrogenase and aldehyde dehydrogenase isozymes. (springer.com)
  • Alcohol dehydrogenase also catalyzed the oxidation of hydroxytolbutamide, and the product of this reaction was oxidized by both xanthine oxidase and aldehyde dehydrogenase. (aspetjournals.org)
  • Carboxytolbutamide was formed from the oxidation of hydroxytolbutamide catalyzed by alcohol dehydrogenase and aldehyde dehydrogenase. (aspetjournals.org)
  • Zinc and vitamin B3 are involved in the conversion from alcohol to aldehyde, using alcohol dehydrogenase [ 5]. (encognitive.com)
  • Alcohol is partly detoxified by aldehyde oxidase, which uses the same nutrients. (encognitive.com)
  • R. S., 1978c, Genetics of hydroxyacid oxidase isozymes in the mouse: localization of Hao-2 on linkage group XVI, Heredity 41: 403. (springer.com)
  • Holmes, R. S., 1979b, Genetics, ontogeny and testosterone inducibility of aldehyde oxidase isozymes in the mouse: evidence for two genetic loci (Aox-1 and Aox-2) closely linked on chromosome 1, Biochem. (springer.com)
  • Degradation primarily by xanthine oxidase. (drugbank.ca)
  • Out of these two, hypoxanthine can be metabolized using hypoxanthine guanine phosphoribosyltransferase where xanthine is accumulated in plasma. (explainmedicine.com)
  • Aldehyde oxidase able to catalyze the oxidation of retinaldehyde into retinoate. (mybiosource.com)
  • Phenylacetaldehyde is formed when the xenobiotic and biogenic amine 2-phenylethylamine is inactivated by a monoamine oxidase-catalyzed oxidative deamination. (biomedsearch.com)
  • BACKGROUND/AIMS: Homovanillamine is a biogenic amine that it is catalyzed to homovanillyl aldehyde by monoamine oxidase A and B, but the oxidation of its aldehyde to the acid derivative is usually ascribed to aldehyde dehydrogenase and a potential contribution of aldehyde oxidase and xanthine oxidase is usually ignored. (biomedsearch.com)
  • Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.1.1.288 , (xanthoxin dehydrogenase), EC 1.13.11.51 (9-cis-epoxycarotenoid dioxygenase) and EC 1.14.13.93 [(+)-abscisic acid 8'-hydroxylase]. (genome.jp)
  • The results of this work are discussed in the context of previous genetic and biochemical evidence regarding ABA biosynthesis, confirming the xanthoxin→abscisic aldehyde→ABA transition as the last steps of the major ABA biosynthetic pathway. (plantcell.org)
  • The widely accepted pathway for ABA biosynthesis [ 8 ] commences with the oxygenation of 9' cis -neoxanthin or 9- cis -violaxanthin to give the C-15 aldehyde, xanthoxin. (biomedcentral.com)
  • Encodes the aldehyde oxidase delta isoform catalyzing the final step in abscisic acid biosynthesis. (riken.jp)
  • Among the at least 5 subunits cre-ating a functional NADPH oxidase, a molecular defect located in any of the gp91phox, p22phox, p47phox, or p67phox subunits may cause CGD. (prednisone2020.site)
  • Another variant, M3-5, was found to exhibit activity towards free and N-Cbz-protected aliphatic and aromatic amino alcohols allowing the synthesis of lactams such as 3,4-dihydronaphthalen-1(2H)-one, 2-pyrrolidone and valerolactam in one-pot tandem reactions with xanthine dehydrogenase (XDH) or aldehyde oxidase (PaoABC). (manchester.ac.uk)
  • In this study, we investigated whether caffeic acid regulates Rac1 GTPase activity, a partner of NADPH oxidase. (biomedsearch.com)
  • The increase in XOR activity detected in atherosclerosis patients reflects the detail that the catabolic pathway is increased in a way to produce hypoxanthine and xanthine in order to permit its readiness to recycle to IMP. (thefreedictionary.com)
  • They exhibit oxidase activity towards various heterocyclic compounds and aldehydes. (nih.gov)
  • The liver cytosol of various mammals also exhibits a significant reductase activity toward nitro, sulfoxide, N-oxide and other moieties, catalyzed by aldehyde oxidase. (nih.gov)
  • There is considerable variability of aldehyde oxidase activity in liver cytosol of mammals: humans show the highest activity, rats and mice show low activity, and dogs have no detectable activity. (nih.gov)
  • Interindividual variation of aldehyde oxidase activity is present in humans. (nih.gov)
  • A simple and sensitive method for activity staining of xanthine oxidase. (scholarena.co)