enzyme Name protoporphyrinogenoxidase EC number 1.3.3.4 IUBMB EC number 1 3 3 4 CAS number 53986 32 6 GO code 0070818 image width caption protein Name protoporphyrinogenoxidase caption image width HGNCid 9280 Symbol PPOX AltSymbols VP EntrezGene 5498 OMIM 600923 RefSeq NM 000309 UniProt P50336 PDB ECnumber 1.3.3.4 Chromosome 1 Arm q Band 22 LocusSupplementaryData Protoporphyrinogenoxidase EC number 1.3.3.4 is an enzyme that is responsible for the seventh step in heme production. Heme is the portion of hemoglobin that carries oxygen in the blood from the lung s to the rest of the body. Protoporphyrinogenoxidase removes hydrogen atoms from protoporphyrinogen IX the product of the sixth step in the production of heme to form protoporphyrin IX . One additional enzyme must modify protoporphyrin IX before it becomes heme. Image Heme synthesis.png center framed Heme synthesis&mdash note that some reactions occur in the cytoplasm and some in the mitochondrion yellow See also porphyrin 1.3 enzyme stub Membrane proteins CH CH oxidoreductases Porphyrin biosynthesis enzymes Category EC 1.3.3 de ProtoporphyrinogenOxidase it Protoporfirinogeno ossidasi ja ... more details
Unreferenced auto yes date December 2009 Chembox verifiedrevid 402048053 ImageFile Protoporphyrinogen IX.svg ImageSize 200 px IUPACName OtherNames Section1 Chembox Identifiers CASNo 7412 77 3 PubChem 1039 SMILES MeSHName protoporphyrinogen Section2 Chembox Properties Formula C sub 34 sub H sub 52 sub N sub 4 sub O sub 4 sub MolarMass 580.801 g mol Appearance Density MeltingPt BoilingPt Section3 Chembox Hazards Solubility MainHazards FlashPt Autoignition Protoporphyrinogen IX is a precursor for protoporphyrin IX . See Porphyrins for the pathway and more information. Image Heme synthesis.png center framed Heme synthesis note that some reactions occur in the cytoplasm and some in the mitochondrion yellow See also Protoporphyrinogenoxidase Tetrapyrroles Heme metabolism intermediates DEFAULTSORT Protoporphyrinogen Ix Chemistry stub Category Macrocycles it Protoporfirinogeno IX ja IX ... more details
An oxidase is any enzyme that catalyst catalyzes an redox oxidation reduction reaction involving molecular oxygen O sub 2 sub as the electron acceptor. In these reactions, oxygen is reduced to water H sub 2 sub O or hydrogen peroxide H sub 2 sub O sub 2 sub . The oxidases are a subclass of the oxidoreductase s. Examples An important example is cytochrome c oxidase , the key enzyme that allows the body to employ oxygen in the generation of energy and the final component of the electron transfer chain . Other examples are glucose oxidase monoamine oxidase cytochrome P450 oxidase NADPH oxidase Xanthine oxidase L gulonolactone oxidase laccase lysyl oxidaseOxidase test main Oxidase test In microbiology , the oxidase test is used as a Phenotype phenotypic characteristic for the identification of bacteria l strains it determines whether a given bacterium produces cytochrome oxidases and therefore utilizes oxygen with an electron transfer chain . External links Catalase & Oxidase tests http www.tgw1916.net movies.html video MeshName Oxidase Enzymes Category Oxidoreductases ar ca Oxidasa et Oks daas es Oxidasa eu Oxidasa fr Oxydase io Oxidazo nl Oxidase ja pl Oksydazy pt Oxidase sv Oxidaser uk ... more details
enzyme Name sarcosine oxidase EC number 1.5.3.1 IUBMB EC number 1 5 3 1 CAS number 9029 22 5 GO code 0008115 image width caption Sarcosine oxidase is an enzyme EC number 1.5.3.1 that catalyst catalyzes the oxidative demethylation of sarcosine to yield glycine , H sub 2 sub O sub 2 sub , 5,10 CH2 tetrahydrofolate in a chemical reaction reaction requiring H4 tetrahydrofolate and oxygen. Corynebacterium Corynebacterial sarcosine oxidase is a heterotetramer and is produced as an inducible enzyme when Corynebacterium sp. is grown with sarcosine as source of carbon and energy . External links MeshName Sarcosine Oxidase Category EC 1.5.3 1.5 enzyme stub Flavoproteins CH NH oxidoreductases it Sarcosina ossidasi ja ... more details
Image Dimethylphenylenediamine.png thumb DMPD Image Tetramethylphenylendiamine.png thumb TMPD The oxidase test is a test used in microbiology to determine if a bacterium produces certain cytochrome c oxidase s. ref name urlOxidase Test and Modified Oxidase Test cite web url http web.mst.edu microbio Lab Supplement Oxidase.html title Oxidase Test and Modified Oxidase Test format work accessdate 2008 11 07 ref It uses disks impregnated with a reagent such as Wurster s blue N,N,N ,N tetramethyl p phenylenediamine TMPD or N,N dimethyl p phenylenediamine DMPD , which is also a redox indicator. The reagent is a dark blue to Maroon color maroon color when oxidized, and colorless when reduced. Oxidase positive bacteria possess cytochrome oxidase or indophenol oxidase an iron containing hemoprotein ref . Isenberg HD, editor. Clinical Microbiology Procedures Handbook. American Society for Microbiology ... electron donor for the enzyme oxidase. The oxidized reagent forms the colored compound indophenol ... Strains may be either oxidase positive OX or oxidase negative OX . OX OX normally means the bacterium contains cytochrome c oxidase and can therefore use oxygen for energy production with an electron ... is the preliminary identification of Neisseria versus Moraxella genera. Neisseria is oxidase positive, Gram negative diplococci and Moraxella is also Oxidase positive. Many Gram negative, spiral curved rods are also oxidase positive, which includes Helicobacter pylori , Vibrio cholera , and Campylobacter jejuni . Also Legionella pneumophila is oxidase positive. A trick to remember the most medical ... does not contain cytochrome c oxidase and, therefore, either cannot use oxygen for energy production ... will result in a light pink or absence of coloration. References reflist External links Oxidase test http www.tgw1916.net movies.html video http www.microbeid.com Methods oxidase.html Oxidase Test Procedure Category Microbiology techniques bacteria stub ar de Oxidase Test es Prueba ... more details
enzyme Name glycerol 3 phosphate oxidase EC number 1.1.3.21 CAS number 9046 28 0 IUBMB EC number 1 1 3 21 GO code 0004369 image width caption In enzymology , a glycerol 3 phosphate oxidase EC number 1.1.3.21 is an enzyme that catalysis catalyzes the chemical reaction sn glycerol 3 phosphate O sub 2 sub math rightleftharpoons math glycerone phosphate H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are sn glycerol 3 phosphate and oxygen O sub 2 sub , whereas its two product chemistry products are glycerone phosphate and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is sn glycerol 3 phosphate oxygen 2 oxidoreductase . Other names in common use include glycerol phosphate oxidase , glycerol 1 phosphate oxidase , glycerol phosphate oxidase , L alpha glycerophosphate oxidase , alpha glycerophosphate oxidase , and L alpha glycerol 3 phosphate oxidase . This enzyme participates in glycerophospholipid metabolism . It employs one cofactor biochemistry cofactor , FAD . References reflist 1 cite journal author Gancedo C, Gancedo JM, Sols A date 1968 title Glycerol metabolism in yeasts. Pathways of utilization and production journal Eur. J. Biochem. volume 5 pages 165&ndash 72 pmid 5667352 doi 10.1111 j.1432 1033.1968.tb00353.x issue 2 cite journal author Koditschek LK, Umbreit WW date 1969 title Alpha glycerophosphate oxidase in Streptococcus faecium F 24 journal J. Bacteriol. volume 98 pages 1063&ndash 8 pmid 5788698 issue 3 pmc 315296 1.1 enzyme stub Category EC 1.1.3 Category Flavin enzymes Category Enzymes of unknown structure it Glicerolo 3 fosfato ossidasi ja 3 ... more details
enzyme Name Catechol oxidase EC number 1.10.3.1 CAS number 9002 10 2 IUBMB EC number GO code image width caption Catechol oxidase is an enzyme that Catalysis catalyses the oxidation of phenol s such as catechol . Catechol oxidase is a copper containing enzyme whose activity is similar to that of tyrosinase , a related class of copper oxidase s. Catechol oxidase carries out the oxidation of phenols such as catechol, using dioxygen O sub 2 sub . In the presence of catechol , benzoquinone is formed see reaction below . Hydrogens removed from catechol combine with oxygen to form water . This reaction, producing the brown compound benzoquinone, is a form of Browning chemical process enzymatic browning exhibited in many foods upon exposure to oxygen e.g., in banana s . Image Catechol Quinone.svg 500px References cite journal author Edward I. Solomon Solomon, E.I. Chen, P. Metz, M. Lee, S. K. Palmer, A.E. title Oxygen Binding, Activation, and Reduction to Water by Copper Proteins journal Angewandte Chemie Angew. Chem. Int. Ed. year 2001 volume 40 pages 4570 4590 pmid 12404359 doi 10.1002 1521 3773 20011217 40 24 4570 AID ANIE4570 3.0.CO 2 4 issue 24 . External links MeshName Catechol Oxidase Category enzymes Category EC 1.10.3 Category Copper enzymes Diphenol family oxidoreductases it Catecolo ossidasi ja ... more details
File Crystal Structure of Human Diamine Oxidase.png thumb Ribbon representation of human diamine oxidase. ref name pmid19764817 PDB 3HI7 cite journal author McGrath AP, Hilmer KM, Collyer CA, Shepard EM, Elmore BO, Brown DE, Dooley DM, Guss JM title Structure and inhibition of human diamine oxidase journal Biochemistry volume 36 pages 9810 9822 year 2009 pmid 19764817 doi 10.1021 bi9014192 url issn rendered with http pymol.sourceforge.net PyMOL ref protein Name amiloride binding protein 1 amine oxidase copper containing caption image width HGNCid 80 Symbol ABP1 AltSymbols EntrezGene 26 OMIM 104610 RefSeq NM 001091 UniProt P19801 PDB ECnumber 1.4.3.6 Chromosome 7 Arm q Band 34 LocusSupplementaryData qter Amine oxidase is an enzyme involved in the metabolism of histamine . External links MeshName Amine Oxidase Copper Containing CH NH2 oxidoreductases Neurotransmitter metabolism enzymes Histaminergics References references oxidoreductase stub de Diaminoxidase pt Diamina oxidase zh ... more details
Merge to Tyrosinase date November 2010 Generalize date October 2009 enzyme Name Polyphenol oxidase EC number 1.14.18.1 CAS number 9002 10 2 IUBMB EC number 1 14 18 1 GO code 0004503 image width caption Polyphenol oxidase PPO or monophenol monooxygenase is a tetramer that contains four atoms of copper per molecule, and binding sites for two aromatic compounds and oxygen ref http www.worthington biochem.com TY default.html, Polyphenol Oxidase Worthington Enzyme Manual. Accessed 13th September, 2011 ref . The enzyme catalyses the o hydroxylation of monophenols phenol molecules in which the benzene ring contains a single hydroxyl substituent to Pyrocatechol o diphenols phenol molecules containing two hydroxyl substituents . They can also further catalyse the oxidation of o diphenols to produce quinone o quinones . It is the rapid polymerisation of o quinones to produce black, brown or red pigments ... issue 21 ref Enzyme nomenclature differentiates between monophenol oxidase enzymes tyrosinase s and o diphenol oxygen oxidoreductase enzymes catechol oxidase s . Therefore, please refer to the tyrosinase and catechol oxidase articles for more information on polyphenol oxidase enzymes. A mixture of monophenol oxidase and catechol oxidase enzymes is present in nearly all plant tissues ... from 4 alkylcatechols a novel reaction catalyzed by cuticular polyphenol oxidase journal FEBS ... the polyphenol oxidase activity from seedlings of higher plants. ref name Duke 1982 cite journal author Duke SO, Vaughn KC title Lack of involvement of polyphenol oxidase in ortho hydroxylation of phenolic ... issue 4 pages 381 385 doi 10.1111 j.1399 3054.1982.tb00696.x ref Tropolone is a grape polyphenol oxidase Enzyme inhibitor inhibitor . ref Time dependent inhibition of grape polyphenol oxidase by tropolone ... PubMed&dopt Citation&list uids 22182754 doi 10.1016 j.abb.2011.11.020 ref See also catechol oxidase References Reflist DEFAULTSORT Polyphenol Oxidase Category Enzymes Category Copper enzymes Biochemistry ... more details
Distinguish aldehyde dehydrogenase enzyme Name Aldehyde oxidase EC number 1.2.3.1 CAS number 9029 07 6 IUBMB EC number 1 2 3 1 GO code 0004031 image width caption protein Name aldehyde oxidase 1 caption image width HGNCid 553 Symbol aldehyde oxidase 1 AOX1 AltSymbols EntrezGene 316 OMIM 602841 RefSeq NM 001159 UniProt Q06278 PDB ECnumber 1.2.3.1 Chromosome 2 Arm q Band 33 LocusSupplementaryData Aldehyde oxidase is an enzyme which generates carboxylic acid s from aldehyde s. ref name pmid16747217 cite journal author Gordon AH, Green DE, Subrahmanyan V title Liver aldehyde oxidase journal Biochem. J. volume 34 issue 5 pages 764 74 year 1940 month May pmid 16747217 pmc 1265340 doi url issn ref It catalyzes the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide . an aldehyde H sub 2 sub O O sub 2 sub a carboxylate H sub 2 sub O sub 2 sub H sup sup The enzyme is a homodimer, and requires FAD , molybdenum and two 2FE 2S clusters as cofactor biochemistry cofactors . See also Aldehyde oxidase and xanthine dehydrogenase, a b hammerhead domain References Reflist External links MeshName Aldehyde oxidase Category EC 1.2.3 enzyme stub de Aldehydoxidase it Aldeide ossidasi ja ... more details
enzyme Name methanethiol oxidase EC number 1.8.3.4 CAS number 112821 28 0 IUBMB EC number 1 8 3 4 GO code 0018549 image width caption In enzymology , a methanethiol oxidase EC number 1.8.3.4 is an enzyme that catalysis catalyzes the chemical reaction methanethiol O sub 2 sub H sub 2 sub O math rightleftharpoons math formaldehyde hydrogen sulfide H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are methanethiol , oxygen O sub 2 sub , and water H sub 2 sub O , whereas its 3 product chemistry products are formaldehyde , hydrogen sulfide , and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on a sulfur group of donors with oxygen as acceptor. The systematic name of this enzyme class is methanethiol oxygen oxidoreductase . Other names in common use include methylmercaptan oxidase , methyl mercaptan oxidase , MM oxidase , and MT oxidase . References reflist 1 cite journal author Suylen GMH, Large PJ, van Dijken JP and Kuenen JG date 1987 title Methylmercaptan oxidase, a key enzyme in the metabolism of methylated sulphur compounds by Hyphomicrobium EG journal J. Gen. Microbiol. volume 133 pages 2989&ndash 2997 1.8 enzyme stub Category EC 1.8.3 Category Enzymes of unknown structure it Metanotiolo ossidasi ja ... more details
Image NADP phys.svg thumb 200px NADP The NADPH oxidase nicotinamide adenine dinucleotide phosphate oxidase is a membrane bound enzyme complex. It can be found in the plasma membrane as well as in the membranes of phagosome s used by neutrophil white blood cells to engulf microorganisms. Subunits It is made ... oxidase . gp91 PHOX contains heme Nox2 p22phox p40phox p47phox p67phox Function image superoxide.svg ... respiratory burst . NADPH oxidase generates superoxide by transferring electrons from NADPH inside ... agent in bleach . Role in pathology NADPH oxidase is a major cause of atherosclerosis, and NADPH oxidase inhibitors may reverse atherosclerosis. Atherosclerosis is caused by the accumulation of macrophages containing cholesterol foam cells in artery walls in the intima . NADPH oxidase produces ... actin fibers . This process is counterbalanced by NADPH oxidase inhibitors, and by antioxidants ... oxidase inhibitors apocynin and diphenyleneiodonium, along with the antioxidants N acetyl cystine ... Reversing Atherosclerosis? N Engl J Med 2009 360 1114 1116 ref Mutations in the NADPH oxidase subunit ... for NADPH oxidase in ketamine induced loss of neuronal parvalbumin and GAD67 expression. ref name ... LL title Ketamine induced loss of phenotype of fast spiking interneurons is mediated by NADPH oxidase ... ref Similar loss is observed in schizophrenia , and the results may point at the NADPH oxidase ... in NADPH oxidase therefore, the phagocyte is unable to make the reactive oxygen species or radicals ... sub 2 sub NADP sup sup 2O sub 2 sub sup sup H sup sup Inhibition NADPH oxidase can be inhibited by apocynin and DPI diphenylene iodonium . Apocynin prevents the assembly of the NADPH oxidase subunits. Using apocynin to inhibit NADPH oxidase may have clinical benefits in the treatment of influenza as it lessens ..., Grant R. Drummond, Stavros Selemidis title Inhibition of Nox2 Oxidase Activity Ameliorates Influenza ... 2 External links MeshName NADPH Oxidase EC number 1.6.3.1 NADH or NADPH oxidoreductases Flavoproteins ... more details
enzyme Name retinal oxidase EC number 1.2.3.11 CAS number 9033 52 7 IUBMB EC number 1 2 3 11 GO code 0050250 image width caption In enzymology , a retinal oxidase EC number 1.2.3.11 is an enzyme that catalysis catalyzes the chemical reaction retinal O sub 2 sub H sub 2 sub O math rightleftharpoons math retinoic acid H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are retinal , oxygen O sub 2 sub , and water H sub 2 sub O , whereas its two product chemistry products are retinoic acid and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is retinal oxygen oxidoreductase . This enzyme is also called retinene oxidase . This enzyme participates in retinol metabolism . References reflist 1 cite journal author Mandal SK, Datta Chaudhuri B date 1987 title Enzymic oxidation of vitamin A aldehyde to vitamin A acid by rat livers of experimental thyroid disorders journal Indian. J. Exp. Biol. volume 25 pages 796&ndash 7 pmid 3452601 issue 11 cite journal author Huang DY, Furukawa A, Ichikawa Y date 1999 title Molecular cloning of retinal oxidase aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli journal Arch. Biochem. Biophys. volume 364 pages 264&ndash 72 pmid 10190983 doi 10.1006 abbi.1999.1129 issue 2 1.2 enzyme stub Category EC 1.2.3 Category Enzymes of unknown structure it Retinale ossidasi ja zh ... more details
enzyme Name sulfite oxidase EC number 1.8.3.1 CAS number 9029 38 3 IUBMB EC number 1 8 3 1 GO code 0008482 image Sulfite oxidase reaction.png width 292px caption Sulfite oxidase catalyses the oxidation reduction reaction of sulfite and water, yielding sulfate. PBB geneid 6821 Sulfite oxidase EC number ... of a novel bacterial sulfite oxidase with no heme binding domain from Deinococcus ... Isolated sulfite oxidase deficiency a case report with a novel mutation and review of the literature ... S, Kessler DL, Rajagopalan KV title Hepatic sulfite oxidase. Congruency in mitochondria of prosthetic ... and the sulfate is excreted. Sulfite oxidase is a metallo enzyme that utilizes a molybdopterin ... super family of molybdenum oxotransferase s that also includes DMSO reductase , xanthine oxidase , and nitrite reductase . In mammals, the expression levels of sulfite oxidase is high in the liver ... , sulfite oxidase contains two identical subunits with an N terminus N terminal domain and a C ... Image Sulfite oxidase mechanism.png thumb left 300px A proposed mechanism of the oxidation of sulfite to sulfate by sulfite oxidase. The active site of sulfite oxidase contains the molybdopterin ... . Deficiency Sulfite oxidase is required to metabolize the sulfur containing amino acids cysteine and methionine in foods. Lack of functional sulfite oxidase causes a disease known as sulfite oxidase ... deformities, the degradation of the brain, and death. Reasons for the lack of functional sulfite oxidase ... E, Kisker C title Structural analysis of missense mutations causing isolated sulfite oxidase deficiency ... oxidase. ref name pmid16475804 cite journal author Wilson HL, Wilkinson SR, Rajagopalan KV title The G473D mutation impairs dimerization and catalysis in human sulfite oxidase journal Biochemistry ... reflist Further reading refbegin 2 Kisker, C. Sulfite oxidase , Messerschimdt, A. Huber, R ... 160 in intramolecular electron transfer in human sulfite oxidase. journal Biochemistry volume ... more details
enzyme Name pteridine oxidase EC number 1.17.3.1 CAS number 74082 65 8 IUBMB EC number 1 17 3 1 GO code 0050227 image width caption In enzymology , a pteridine oxidase EC number 1.17.3.1 is an enzyme that catalysis catalyzes the chemical reaction 2 amino 4 hydroxypteridine O sub 2 sub math rightleftharpoons math 2 amino 4,7 dihydroxypteridine ? Thus, the two substrate biochemistry substrates of this enzyme are 2 amino 4 hydroxypteridine and oxygen O sub 2 sub , whereas its product chemistry product is 2 amino 4,7 dihydroxypteridine . This enzyme belongs to the family of oxidoreductase s, specifically those acting on CH or CH2 group with oxygen as acceptor. The systematic name of this enzyme class is 2 amino 4 hydroxypteridine oxygen oxidoreductase 7 hydroxylating . References reflist 1 cite journal author Yong Y N date 1980 title Detection of a pteridine oxidase in plants journal Plant Sci. Lett. volume 18 pages 169&ndash 175 1.17 enzyme stub Category EC 1.17.3 Category Enzymes of unknown structure it Pteridina ossidasi ja ... more details
enzyme Name bilirubin oxidase EC number 1.3.3.5 CAS number 80619 01 8 IUBMB EC number 1 3 3 5 GO code 0047705 image MvBO 2xll thumb.png width 220px caption Cartoon representation of the X ray structure of bilirubin oxidase from Myrothecium verrucaria based on PDB accession code PDB link 2xll . The protein ribbon is rainbow colored with the N terminus in blue and the C terminus in red. The four copper atoms are shown as spheres and the Glycan glycans shown as sticks. In enzymology , a bilirubin oxidase EC number 1.3.3.5 is an enzyme that catalysis catalyzes the chemical reaction 2 bilirubin O sub 2 sub math rightleftharpoons math 2 biliverdin 2 H sub 2 sub O Thus, the two substrate biochemistry substrates of this enzyme are bilirubin and oxygen O sub 2 sub , whereas its two product chemistry products are biliverdin and water H sub 2 sub O . This enzyme belongs to the family of oxidoreductase s, to be specific those acting on the CH CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is bilirubin oxygen oxidoreductase . This enzyme is also called bilirubin oxidase M 1 . This enzyme participates in porphyrin and chlorophyll metabolism. ref cite journal author Murao S and Tanaka N date 1981 title A new enzyme bilirubin oxidase produced by Myrothecium verrucaria MT 1 journal Agric. Biol. Chem. volume 45 pages 2383&ndash 2384 ref ref cite journal author Tanaka N and Murao S date 1985 title Reaction of bilirubin oxidase produced by Myrothecium verrucaria MT 1. Agr journal Biol. Chem. volume 49 pages 843&ndash 844 ref Two structures of bilirubin oxidase from the ascomycete Myrothecium verrucaria have been deposited in the Protein Data Bank accession codes PDB link 3abg and PDB link 2xll . ref Citation first Kimihiko last Mizutani first2 Mayuko last2 ... X ray analysis of bilirubin oxidase from Myrothecium verrucaria at 2.3 Å resolution using a twinned ... first3 Edward D. last3 Lowe first4 Christopher F. last4 Blanford title Bilirubin oxidase from Myrothecium ... more details
enzyme Name ecdysone oxidase EC number 1.1.3.16 CAS number 56803 12 4 IUBMB EC number 1 1 3 16 GO code 0047875 image width caption In enzymology , an ecdysone oxidase EC number 1.1.3.16 is an enzyme that catalysis catalyzes the chemical reaction ecdysone O sub 2 sub math rightleftharpoons math 3 dehydroecdysone H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are ecdysone and oxygen O sub 2 sub , whereas its two product chemistry products are 3 dehydroecdysone and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is ecdysone oxygen 3 oxidoreductase . This enzyme is also called beta ecdysone oxidase . References reflist 1 cite journal author Koolman J, Karlson P date 1975 title Ecdysone Oxidase, an enzyme from the blowfly Calliphora erythrocephala Meigen journal Hoppe. Seylers. Z. Physiol. Chem. volume 356 pages 1131&ndash 8 pmid 297 issue 7 doi 10.1515 bchm2.1975.356.2.1131 1.1 enzyme stub Category EC 1.1.3 Category Enzymes of unknown structure it Ecdisone ossidasi ja ... more details
oxidase shown as part of the complete electron transport chain . UQ is coenzyme Q10 ubiquinol ubiquinone , C is cytochrome c and AOX is the alternative oxidase. The alternative oxidase ... Branched mitochondrial electron transport in the Animalia presence of alternative oxidase in several ... 1521 6540400000876 ref ref cite journal author Sluse FE, Jarmuszkiewicz W title Alternative oxidase ... 10.1590 S0100 879X1998000600003 ref Sequences similar to the plant oxidase have also been identified ... orthologues of mitochondrial alternative oxidase and plastid terminal oxidase journal Plant ... 2004 pmid 15087133 doi 10.1016 j.gene.2004.01.015 ref The oxidase provides an alternative route ... pumping steps are bypassed in this alternative pathway, activation of the oxidase reduces ATP generation. This enzyme was first identified as a distinct oxidase pathway from cytochrome c oxidase as the alternative oxidase is resistant to enzyme inhibitor inhibition by the poison cyanide . ref cite ... oxidase of plant mitochondria journal Biochim. Biophys. Acta volume 1059 issue 2 pages 121 40 ... oxidase diverges from the cytochrome linked electron transport chain at the coenzyme Q10 ubiquinone pool. ref cite journal author Juszczuk IM, Rychter AM title Alternative oxidase in higher plants url .... The expression of the alternative oxidase gene AOX is influenced by stresses such as cold, reactive ... Alternative oxidase From Gene to Function journal Annual Review of Plant Physiology and Plant Molecular ... of tandem arranged alternative oxidase genes in rice are increased by low temperature journal ... DP, Wang Y, McIntosh L title The alternative oxidase lowers mitochondrial reactive oxygen production ... of African trypanosomiasis sleeping sickness , depends entirely on the alternative oxidase pathway ... M, Ott RD, Hill GC title Trypanosome alternative oxidase from molecule to function journal Trends ... forms of the parasite Trypanosoma brucei brucei is dependent on a plant like alternative oxidase ... more details
enzyme Name tetrahydroberberine oxidase EC number 1.3.3.8 CAS number 114705 00 9 IUBMB EC number 1 3 3 8 GO code 0050328 image width caption In enzymology , a tetrahydroberberine oxidase EC number 1.3.3.8 is an enzyme that catalysis catalyzes the chemical reaction S tetrahydroberberine 2 O sub 2 sub math rightleftharpoons math berberine 2 H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are S tetrahydroberberine and oxygen O sub 2 sub , whereas its two product chemistry products are berberine and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is S tetrahydroberberine oxygen oxidoreductase . This enzyme is also called S THB oxidase . This enzyme participates in alkaloid biosynthesis. References reflist 1 cite journal author Amann M, Nagakura N and Zenk MH date 1984 title S Tetrahydroprotoberberine oxidase the final enzyme in protoberberine biosynthesis journal Tetrahedron Lett. volume 25 issue 9 pages 953&ndash 954 doi 10.1016 S0040 4039 01 80071 X cite journal doi 10.1016 0031 9422 88 80255 3 author Okada N, Shinmyo A, Okada H and Yamada Y date 1988 title Purification and characterization of S tetrahydroberberine oxidase from cultured Coptis japonica cells journal Phytochemistry journal Phytochemistry volume 27 issue 4 pages 979&ndash 982 Category EC 1.3.3 Category Enzymes of unknown structure 1.3 enzyme stub it Tetraidroberberina ossidasi ja ... more details
enzyme Name galactose oxidase EC number 1.1.3.9 CAS number 9028 79 9 IUBMB EC number 1 1 3 9 GO code 0045480 image width caption In enzymology , a galactose oxidase EC number 1.1.3.9 is an enzyme that catalysis catalyzes the chemical reaction D galactose O sub 2 sub math rightleftharpoons math D galacto hexodialdose H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are D galactose and oxygen O sub 2 sub , whereas its two product chemistry products are D galacto hexodialdose and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is D galactose oxygen 6 oxidoreductase . Other names in common use include D galactose oxidase , and beta galactose oxidase . It employs two cofactor biochemistry cofactors , copper and an active site amino acid derived post translational modification involving the covalent cross linking of Cys228 and Tyr272 and which represents the site of the catalytic free radical . Structural studies As of late 2007, 9 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1GOF , PDB link 1GOG , PDB link 1GOH , PDB link 1K3I , PDB link 1T2X , PDB link 2EIB , PDB link 2EIC , PDB link 2EID , and PDB link 2EIE . References reflist 1 cite journal author AVIGAD G, AMARAL D, ASENSIO C, HORECKER BL date 1962 title The D galactose oxidase of Polyporus circinatus journal J. Biol. Chem. volume 237 pages 2736&ndash 43 pmid 13863403 1.1 enzyme stub Category EC 1.1.3 Category Copper enzymes Category Enzymes of known structure it Galattosio ossidasi ja ... more details
enzyme Name malate oxidase EC number 1.1.3.3 CAS number 9028 73 3 IUBMB EC number 1 1 3 3 GO code 0019157 image width caption In enzymology , a malate oxidase EC number 1.1.3.3 is an enzyme that catalysis catalyzes the chemical reaction S malate O sub 2 sub math rightleftharpoons math oxaloacetate H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are S malate and oxygen O sub 2 sub , whereas its two product chemistry products are oxaloacetate and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is S malate oxygen oxidoreductase . Other names in common use include FAD dependent malate oxidase , malic oxidase , and malic dehydrogenase II . This enzyme participates in pyruvate metabolism . It employs one cofactor biochemistry cofactor , FAD . References reflist 1 cite journal author COHN DV date 1958 title The enzymatic formation of oxalacetic acid by nonpyridine nucleotide malic dehydrogenase of Micrococcus lysodeikticus journal J. Biol. Chem. volume 233 pages 299&ndash 304 pmid 13563491 issue 2 cite journal author Narindrasorasak S, Goldie AH, Sanwal BD date 1979 title Characteristics and regulation of a phospholipid activated malate oxidase from Escherichia coli journal J. Biol. Chem. volume 254 pages 1540&ndash 5 pmid 368072 issue 5 1.1 enzyme stub Category EC 1.1.3 Category Flavin enzymes Category Enzymes of unknown structure it Malato ossidasi ja ... more details
enzyme Name S 6 hydroxynicotine oxidase EC number 1.5.3.5 CAS number 37256 29 4 IUBMB EC number 1 5 3 5 GO code 0018531 image width caption In enzymology , a S 6 hydroxynicotine oxidase EC number 1.5.3.5 is an enzyme that catalysis catalyzes the chemical reaction S 6 hydroxynicotine H sub 2 sub O O sub 2 sub math rightleftharpoons math 1 6 hydroxypyridin 3 yl 4 methylamino butan 1 one H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are S 6 hydroxynicotine , water H sub 2 sub O , and oxygen O sub 2 sub , whereas its two product chemistry products are 1 6 hydroxypyridin 3 yl 4 methylamino butan 1 one and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is S 6 hydroxynicotine oxygen oxidoreductase . Other names in common use include L 6 hydroxynicotine oxidase , 6 hydroxy L nicotine oxidase , and 6 hydroxy L nicotine oxygen oxidoreductase . It employs one cofactor biochemistry cofactor , FAD . References reflist 1 cite journal author Dai VD, Decker K, Sund H date 1968 title Purification and properties of L 6 hydroxynicotine oxidase journal Eur. J. Biochem. volume 4 pages 95&ndash 102 pmid 5646150 doi 10.1111 j.1432 1033.1968.tb00177.x issue 1 cite journal author Decker K, Bleeg H date 1965 title Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans journal Biochim. Biophys. Acta. volume 105 pages 313&ndash 24 pmid 5849820 issue 2 Category EC 1.5.3 Category Flavin enzymes Category Enzymes of unknown structure it S 6 idrossinicotina ossidasi ja S 6 ... more details
enzyme Name xanthine oxidase dehydrogenase EC number 1.17.3.2 IUBMB EC number 1 17 3 2 CAS number 9002 ... of bovine xanthine oxidase. ref name pmid11005854 PDB 1FIQ cite journal author Enroth C, Eger BT ... and xanthine oxidase structure based mechanism of conversion journal Proc. Natl. Acad. Sci. U.S.A. .... protein Name xanthine oxidase dehydrogenase caption image width HGNCid 12805 Symbol Xanthine dehydrogenase ... 1.17.3.2 Chromosome 2 Arm p Band 23.1 LocusSupplementaryData Xanthine oxidase XO sometimes XAO is a form ... on xanthine oxidoreductase xanthine oxidase in mammalian corneal epithelium journal Acta Histochem ... issue 6 pages 774 97 year 2002 pmid 12208366 doi 10.1016 S0891 5849 02 00956 5 ref Xanthine oxidase ... to xanthine oxidase by reversible sulfhydryl oxidation or by irreversible proteolytic modification ... oxidase hypoxanthine H sub 2 sub O O sub 2 sub math rightleftharpoons math xanthine H sub 2 sub ... 2 sub Xanthine oxidase can also act on certain other purines, pterins, and aldehydes. For example ... W. title A Combined QM MM Study on the Reductive Half Reaction of Xanthine Oxidase Substrate Orientation ... from dioxygen O sub 2 sub . Clinical significance Xanthine oxidase is a superoxide producing enzyme ... severe liver damage, xanthine oxidase is released into the blood, so a blood assay for XO is a way to determine if liver damage has happened. ref citation needed ref As well, because xanthine oxidase is a metabolic pathway for uric acid formation, the xanthine oxidase inhibitor allopurinol is used in the treatment of gout . Since xanthine oxidase is involved in the metabolism of 6 mercaptopurine ... , in conjunction. Xanthinuria is a rare genetic disorder where the lack of xanthine oxidase ... gene which mediates xanthine oxidase activity. 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 ... 20type title OMIM Xanthinuria type II ref Inhibition of xanthine oxidase has been proposed as a mechanism ... more details
enzyme Name Choline oxidase EC number 1.1.3.17 CAS number 9028 67 5 IUBMB EC number 1 1 3 17 GO code image width caption In enzymology , a choline oxidase EC number 1.1.3.17 is an enzyme that catalysis catalyzes the chemical reaction choline O sub 2 sub math rightleftharpoons math betaine aldehyde H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are choline and oxygen O sub 2 sub , whereas its two product chemistry products are betaine aldehyde and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the CH OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is choline oxygen 1 oxidoreductase . This enzyme participates in glycine , serine , and threonine metabolism. It employs one cofactor biochemistry cofactor , FAD . References reflist 1 cite journal author Ikuta S, Imamura S, Misaki H, Horiuti Y date Tokyo title Purification and characterization of choline oxidase from Arthrobacter globiformis journal J. volume Biochem. pages 1741&ndash 9 pmid 599154 issue 6 cite journal author Rozwadowski KL, Khachatourians GG, Selvaraj G date 1991 title Choline oxidase, a catabolic enzyme in Arthrobacter pascens, facilitates adaptation to osmotic stress in Escherichia coli journal J. Bacteriol. volume 173 pages 472&ndash 8 pmid 1987142 issue 2 pmc 207035 cite journal author Rand T, Halkier T, Hansen OC date 2003 title Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis journal Biochemistry. volume 42 pages 7188&ndash 94 pmid 12795615 doi 10.1021 bi0274266 issue 23 cite journal author Gadda G, Powell NL, Menon P date 2004 title The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase journal Arch. Biochem ... journal author Fan F, Gadda G date 2005 title On the catalytic mechanism of choline oxidase journal ... more details
enzyme Name nitroethane oxidase EC number 1.7.3.1 CAS number 9029 36 1 IUBMB EC number 1 7 3 1 GO code 0050141 image width caption In enzymology , a nitroalkane oxidase EC number 1.7.3.1 is an enzyme that catalysis catalyzes the chemical reaction a nitroalkane H sub 2 sub O O sub 2 sub math rightleftharpoons math an aldehyde or ketone nitrite H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are nitroalkane , water H sub 2 sub O , and oxygen O sub 2 sub , whereas its 4 product chemistry products are aldehyde , ketone , nitrite , and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on other nitrogenous compounds as donors with oxygen as acceptor. The systematic name of this enzyme class is nitroalkane oxygen oxidoreductase . Other names in common use include nitroethane oxidase , NAO , and nitroethane oxygen oxidoreductase . This enzyme participates in nitrogen metabolism . References reflist 1 cite journal author LITTLE HN date 1951 title Oxidation of nitroethane by extracts from Neurospora journal J. Biol. Chem. volume 193 pages 347&ndash 58 pmid 14907722 issue 1 cite journal author Kido T, Hashizume K, Soda K date 1978 title Purification and properties of nitroalkane oxidase from Fusarium oxysporum journal J. Bacteriol. volume 133 pages 53&ndash 8 pmid 22538 issue 1 pmc 221975 cite journal author Daubner SC, Gadda G, Valley MP, Fitzpatrick PF date 2002 title Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a new member of the acyl CoA dehydrogenase superfamily journal Proc. Natl. Acad. Sci. U. S. A. volume 99 pages 2702&ndash 7 pmid 11867731 doi 10.1073 pnas.052527799 issue 5 pmc 122411 cite journal author Fitzpatrick PF, Orville AM, Nagpal A, Valley MP date 2005 title Nitroalkane oxidase, a carbanion forming flavoprotein homologous to acyl CoA dehydrogenase ... the kinetic competency of the cationic imine intermediate in nitroalkane oxidase journal ... more details
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