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 fr Oxydase io Oxidazo nl Oxidase ja pl Oksydazy pt Oxidase sv Oxidaser uk ... more details
Wikify date January 2012 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
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
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 which 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 polyphenol s that is the cause of browning chemical process fruit browning . The amino acid tyrosine ... 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 ... ref See also catechol oxidase References Reflist DEFAULTSORT Polyphenol Oxidase Category ... 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
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 2004. p. 3.3.2 3.3.2.13 ref . These both catalyze the transport of electrons from donor compounds ... dihydrochloride acts as an artificial electron donor for the enzyme oxidase. The oxidized reagent ... and Wilkins 2000. p. 363 7 ref . Classification Strains may be either oxidase positive OX or oxidase negative OX . OX OX normally means that the bacterium contains cytochrome c oxidase and can ... and Moraxella genera, which are both oxidase positive, Gram negative diplococci . 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 ... that the bacterium does not contain cytochrome c oxidase and, therefore, either cannot utilize oxygen ... 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 eu Oxidasaren proba uk ... 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
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 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 1.10 enzyme stub Diphenol family oxidoreductases it Catecolo ossidasi ja ... 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 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 , a form ... oxidoreductase xanthine oxidase in mammalian corneal epithelium journal Acta Histochem volume 106 issue ... 33 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 ... sub 2 sub Xanthine oxidase can also act on certain other purines, pterins, and aldehydes. For example ... on the Reductive Half Reaction of Xanthine Oxidase Substrate Orientation and Mechanism journal Journal ... significance Xanthine oxidase is a superoxide producing enzyme found normally in serum and the lungs ... intphys iphy3700 vitCHemila92.pdf ref During severe liver damage, xanthine oxidase is released ... 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 ... genetic disorder where the lack of xanthine oxidase leads to high concentration of xanthine in blood ... xanthinuria has been traced directly to mutations of the XDH gene which mediates xanthine oxidase activity ... sites of xanthine oxidase and aldehyde oxidase , a related enzyme with some overlapping activities ... ref Inhibition of xanthine oxidase has been proposed as a mechanism for improving cardiovascular health. ref name pmid17052251 cite journal author Dawson J, Walters M title Uric acid and xanthine oxidase ... 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 ... b505789m url issn ref A G473D mutation impairs dimerization and catalysis in human sulfite oxidase ... mutation impairs dimerization and catalysis in human sulfite oxidase journal Biochemistry volume ... reflist Further reading refbegin 2 Kisker, C. Sulfite oxidase , Messerschimdt, A. Huber, R. Poulos ... 160 in intramolecular electron transfer in human sulfite oxidase. journal Biochemistry volume 42 issue ... 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 indole 3 acetaldehyde oxidase EC number 1.2.3.7 CAS number 66082 22 2 IUBMB EC number 1 2 3 7 GO code 0050302 image width caption In enzymology , an indole 3 acetaldehyde oxidase EC number 1.2.3.7 is an enzyme that catalysis catalyzes the chemical reaction indol 3 yl acetaldehyde H sub 2 sub O O sub 2 sub math rightleftharpoons math indol 3 yl acetate H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are indol 3 yl acetaldehyde , water H sub 2 sub O , and oxygen O sub 2 sub , whereas its two product chemistry products are indol 3 yl acetate 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 indol 3 yl acetaldehyde oxygen oxidoreductase . Other names in common use include indoleacetaldehyde oxidase , IAAld oxidase , AO1 , and indole 3 acetaldehyde oxygen oxidoreductase . This enzyme participates in tryptophan metabolism . It has 3 cofactor biochemistry cofactors FAD , Heme , and Molybdenum . References reflist 1 cite journal author Bower PJ, Brown HM and Purves WK date 1978 title Cucumber seedling indoleacetaldehyde oxidase journal Plant Physiol. volume 61 issue 1 pages 107&ndash 110 doi 10.1104 pp.61.1.107 cite journal author Miyata S, Suzuki Y, Kamisaka S and Masuda Y date 1981 title Indole 3 acetaldehyde oxidase of pea seedlings journal Physiol. Plant. volume 51 issue 4 pages 402&ndash 406 doi 10.1111 j.1399 3054.1981.tb05577.x cite journal author Rajagopal R date 1971 title Metabolism of indole 3 acetaldehyde. III. Some characteristics of the aldehyde oxidase of Avena coleoptiles journal Physiol. Plant. volume 24 issue 2 pages 272&ndash 281 doi 10.1111 ... date 1996 title Purification and Properties of Flavin and Molybdenum Containing Aldehyde Oxidase from ... issue 4 cite journal author T date 1998 title Higher activity of an aldehyde oxidase in the auxin ... 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 1.5 enzyme stub ... 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 oxalate oxidase EC number 1.2.3.4 CAS number 9031 79 2 IUBMB EC number 1 2 3 4 GO code 0050162 image width caption In enzymology , an oxalate oxidase EC number 1.2.3.4 is an enzyme that catalysis catalyzes the chemical reaction oxalate O sub 2 sub 2 H sup sup math rightleftharpoons math 2 CO sub 2 sub H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are oxalate , oxygen O sub 2 sub , and hydrogen ion H sup sup , whereas its two product chemistry products are carbon dioxide CO sub 2 sub 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 oxalate oxygen oxidoreductase . Other names in common use include aero oxalo dehydrogenase , and oxalic acid oxidase . This enzyme participates in glyoxylate and dicarboxylate metabolism . It has 2 cofactor biochemistry cofactors FAD , and Manganese . Structural studies As of late 2007, 4 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1FI2 , PDB link 2ET1 , PDB link 2ET7 , and PDB link 2ETE . References reflist 1 cite journal author DATTA PK, MEEUSE BJ date 1955 title Moss oxalic acid oxidase a flavoprotein journal Biochim. Biophys. Acta. volume 17 pages 602&ndash 3 pmid 13250021 doi 10.1016 0006 3002 55 90436 4 issue 4 cite journal author Kotsira VP, Clonis YD date 1997 title Oxalate oxidase from barley roots purification to homogeneity and study of some molecular, catalytic, and binding properties journal Arch. Biochem. Biophys. volume 340 pages 239&ndash 49 pmid 9143327 doi 10.1006 abbi.1997.9896 issue 2 cite journal author Requena L, Bornemann S date 1999 title Barley Hordeum vulgare oxalate oxidase is a manganese containing enzyme journal Biochem. J. 343 Pt volume 1 pages 185&ndash 90 pmid 10493928 pmc 1220540 issue Pt 1 1.2 enzyme ... more details
enzyme Name pyruvate oxidase EC number 1.2.3.3 CAS number 9001 96 1 IUBMB EC number 1 2 3 3 GO code 0047112 image width caption In enzymology , a pyruvate oxidase EC number 1.2.3.3 is an enzyme that catalysis catalyzes the chemical reaction pyruvate phosphate O sub 2 sub math rightleftharpoons math acetyl phosphate CO sub 2 sub H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are pyruvate , phosphate , and oxygen O sub 2 sub , whereas its 3 product chemistry products are acetyl phosphate , carbon dioxide CO sub 2 sub , 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 pyruvate oxygen 2 oxidoreductase phosphorylating . Other names in common use include pyruvic oxidase , and phosphate dependent pyruvate oxidase . This enzyme participates in pyruvate metabolism . It has 2 cofactor biochemistry cofactors FAD , and Thiamin diphosphate . Structural studies As of late 2007, 12 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1POW , PDB link 1POX , PDB link 1V5E , PDB link 1V5F , PDB link 1V5G , PDB link 1Y9D , PDB link 2DJI , PDB link 2EZ4 , PDB link 2EZ8 , PDB link 2EZ9 , PDB link 2EZT , and PDB link 2EZU . References reflist 1 cite journal author Williams FR, Hager LP date 1966 title Crystalline flavin pyruvate oxidase from Escherichia coli. I Isolation and properties of the flavoprotein journal Arch. Biochem. Biophys. volume 116 pages 168&ndash 76 pmid 5336022 doi 10.1016 0003 9861 66 90025 7 issue 1 cite journal author Tittmann K, Wille G, Golbik R, Weidner A, Ghisla S, Hubner G date 2005 title Radical phosphate transfer mechanism for the thiamin diphosphate and FAD dependent pyruvate oxidase from Lactobacillus plantarum Kinetic coupling of intercofactor electron transfer with phosphate ... 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 membrane of phagosome . Subunits It is made up of six subunits. These subunits are a Rho guanosine triphosphatase GTPase , usually Rac1 or Rac2 Rac stands for Rho related C3 botulinum toxin substrate Five phox units. Phox stands for phagocytic oxidase . gp91 PHOX contains heme Nox2 p22phox p40phox p47phox p67phox Function image superoxide.svg thumb right 150px Lewis structure Lewis electron configuration of superoxide. Under normal circumstances, the complex is latent in neutrophils and is activated ... oxidase is a major cause of atherosclerosis, and NADPH oxidase inhibitors may reverse atherosclerosis ... in artery walls in the intima . NADPH oxidase produces ROSs. These ROSs activate an enzyme that makes ... by NADPH oxidase inhibitors, and by antioxidants. An imbalance in favor of ROS produces atherosclerosis. In vitro studies have found that the NADPH oxidase inhibitors apocynin and diphenyleneiodonium ... 1116 ref Mutations in the NADPH oxidase subunit genes cause several Chronic granulomatous disease ... a part of the complex. One study suggests a role for NADPH oxidase in ketamine induced loss of neuronal ... spiking interneurons is mediated by NADPH oxidase journal Science volume 318 issue 5856 pages 1645 ... , and the results may point at the NADPH oxidase as a possible player in the pathophysiology of the disease ... disease, a disease in which there is a defect in NADPH oxidase therefore, the phagocyte is unable ... 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 ... of Nox2 Oxidase Activity Ameliorates Influenza A Virus Induced Lung Inflammation journal PLoS Pathog ... pmid 21304882 pmc 3033375 ref References reflist 2 External links MeshName NADPH Oxidase EC number ... more details
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