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 glyoxylate oxidase EC number 1.2.3.5 CAS number 37251 03 9 IUBMB EC number 1 2 3 5 GO code 0047969 image width caption In enzymology , a glyoxylate oxidase EC number 1.2.3.5 is an enzyme that catalysis catalyzes the chemical reaction glyoxylate H sub 2 sub O O sub 2 sub math rightleftharpoons math oxalate H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are glyoxylate , water H sub 2 sub O , and oxygen O sub 2 sub , whereas its two product chemistry products are oxalate 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 glyoxylate oxygen oxidoreductase . This enzyme participates in glyoxylate and dicarboxylate metabolism . References reflist 1 cite journal author Kasai T, Suzuki I and Asai T date 1962 title Glyoxylic oxidase system in Acetobacter. journal Koso Kagaku Shimpojiumu volume 17 pages 77&ndash 81 1.2 enzyme stub Category EC 1.2.3 Category Enzymes of unknown structure it Gliossilato ossidasi ja ... more details
enzyme Name 3 hydroxyanthranilate oxidase EC number 1.10.3.5 CAS number 37256 53 4 IUBMB EC number 1 10 3 5 GO code 0047561 image width caption In enzymology , a 3 hydroxyanthranilate oxidase EC number 1.10.3.5 is an enzyme that catalysis catalyzes the chemical reaction 3 hydroxyanthranilate O sub 2 sub math rightleftharpoons math 6 imino 5 oxocyclohexa 1,3 dienecarboxylate H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are 3 hydroxyanthranilate and oxygen O sub 2 sub , whereas its two product chemistry products are 6 imino 5 oxocyclohexa 1,3 dienecarboxylate and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on diphenols and related substances as donor with oxygen as acceptor. The systematic name of this enzyme class is 3 hydroxyanthranilate oxygen oxidoreductase . This enzyme is also called 3 hydroxyanthranilic acid oxidase . References reflist 1 cite journal author Morgan LR Jr, Weimorts DM, Aubert CC date 1965 title Oxidation Of 3 hydroxyanthranilic acid by a soluble liver fraction from poikilothermic vertebrates journal Biochim. Biophys. Acta. volume 100 pages 393&ndash 402 pmid 14347936 Amino acid metabolism enzymes Category EC 1.10.3 Category Enzymes of unknown structure it 3 idrossiantranilato ossidasi ja 3 ... more details
enzyme Name glutathione oxidase EC number 1.8.3.3 CAS number 55467 56 6 IUBMB EC number 1 8 3 3 GO code 0047950 image width caption In enzymology , a glutathione oxidase EC number 1.8.3.3 is an enzyme that catalysis catalyzes the chemical reaction 2 glutathione O sub 2 sub math rightleftharpoons math glutathione disulfide H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are glutathione and oxygen O sub 2 sub , whereas its two product chemistry products are glutathione disulfide 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 glutathione oxygen oxidoreductase . This enzyme participates in glutathione metabolism . It employs one cofactor biochemistry cofactor , FAD . References reflist 1 cite journal author Kusakabe H, Kuninaka A and Yoshino H date 1982 title Purification and properties of a new enzyme, glutathione oxidase from Penicillium sp.K 6 5 journal Agric. Biol. Chem. volume 46 pages 2057&ndash 2067 1.8 enzyme stub Category EC 1.8.3 Category Flavin enzymes Category Enzymes of unknown structure it Glutatione ossidasi ja ... more details
enzyme Name Glucose oxidase EC number 1.1.3.4 CAS number 9001 37 0 IUBMB EC number 1 1 3 4 GO code 0046562 image 77 1gpe.gif width caption PDB Molecule of the Month pdb77 1 The glucose oxidase enzyme GOx EC number 1.1.3.4 is an Oxidoreductase oxido reductase that catalyses the oxidation of glucose to hydrogen peroxide and Glucono delta lactone D glucono lactone . In cells, it aids in breaking the sugar down into its metabolite s. Glucose oxidase is widely used for the determination of free glucose in body fluids diagnostic s , in vegetal raw material, and in the food industry. It also has many applications in biotechnology biotechnologies , typically enzyme assays for biochemistry including ... sheet of Glucose Oxidase , Interchim ref It is often extracted from Aspergillus Aspergillus niger ... and furanose form being negligible. The glucose oxidase binds specifically to D glucopyranose .... ref name GOxTechData Glucose oxidase catalyst catalyze s the oxidation of D glucose into Glucono ... O sub 2 sub . Applications Glucose oxidase is widely used, coupled to peroxidase reaction that vizualizes ... Julio Raba and Horacio A. Mottola title Glucose Oxidase as an Analytical Reagent journal Critical ... white to prevent browning. Glucose oxidase is found in honey and acts as a natural preservative. GOx ... oxidase, enzymes extracted from other molds besides P. notatum ref name pmid14915954 cite journal author KEILIN D, HARTREE EF title Specificity of glucose oxidase notatin journal Biochem. J. volume 50 ... known as glucose oxidase. ref name JulioRaba Early experiments showed that notatin exhibits in vitro ... marco enzyme electrode chapter3 chapter3 page1.htm Glucose Oxidase A much used and much loved enzyme in biosensors at University of Paisley MeshName Glucose Oxidase Alcohol oxidoreductases DEFAULTSORT Glucose Oxidase Category EC 1.1.3 de Glucose Oxidase es Glucosa oxidasa fr Glucose oxydase id Glukosa oksidase it Glucosio ossidasi ja pl Oksydaza glukozowa pt Glicose oxidase ... more details
Ubiquinol oxidases EC 1.10.3. are enzymes in the bacteria l electron transport chain that oxidise coenzyme Q ubiquinol into ubiquinone and reduce oxygen to water. These enzymes are one set of the many alternative terminal oxidases in the branched prokaryotic electron transport chain. ref cite journal author Garc a Horsman JA, Barquera B, Rumbley J, Ma J, Gennis RB title The superfamily of heme copper respiratory oxidases journal J. Bacteriol. volume 176 issue 18 pages 5587 600 year 1994 pmid 8083153 pmc 196760 ref The overall structure of the E. coli ubiquinol oxidase is similar to that of the mammalian Cytochrome c oxidase , with the addition of a polar ubiquinol binding site embedded in the membrane. ref cite journal author Abramson J title The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site journal Nat. Struct. Biol. volume 7 issue 10 pages 910 7 year 2000 pmid 11017202 doi 10.1038 82824 author separator , author2 Riistama S author3 Larsson G display authors 3 last4 Riistama first4 Sirpa last5 Larsson first5 Gisela last6 Jasaitis first6 Audrius last7 Svensson Ek first7 Margareta last8 Laakkonen first8 Liisa last9 Puustinen first9 Anne ref See also Oxidative phosphorylation Microbial metabolism References reflist Electron transport chain Cellular respiration Category Cellular respiration Category Metabolism Category EC 1.10.3 1.10 enzyme stub metabolism stub pt Ubiquinol oxidase ... more details
enzyme Name 4 hydroxymandelate oxidase EC number 1.1.3.19 CAS number 60976 30 9 IUBMB EC number 1 1 3 19 GO code 0047579 image width caption In enzymology , a 4 hydroxymandelate oxidase EC number 1.1.3.19 is an enzyme that catalysis catalyzes the chemical reaction S 2 hydroxy 2 4 hydroxyphenyl acetate O sub 2 sub math rightleftharpoons math 4 hydroxybenzaldehyde CO sub 2 sub H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are S 2 hydroxy 2 4 hydroxyphenyl acetate and oxygen O sub 2 sub , whereas its 3 product chemistry products are 4 hydroxybenzaldehyde , 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 CH OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is S 2 hydroxy 2 4 hydroxyphenyl acetate oxygen 1 oxidoreductase . This enzyme is also called L 4 hydroxymandelate oxidase decarboxylating . It has 2 cofactor biochemistry cofactors FAD , and Manganese . References reflist 1 cite journal author Bhat SG, Vaidyanathan CS date 1976 title Purification and properties of L 4 hydroxymandelate oxidase from Pseudomonas convexa journal Eur. J. Biochem. volume 68 pages 323&ndash 31 pmid 976259 doi 10.1111 j.1432 1033.1976.tb10818.x issue 2 1.1 enzyme stub Category EC 1.1.3 Category Flavin enzymes Category Manganese enzymes Category Enzymes of unknown structure it 4 idrossimandelato ossidasi ja 4 ... more details
enzyme Name hexose oxidase EC number 1.1.3.5 CAS number 9028 75 5 IUBMB EC number 1 1 3 5 GO code 0047979 image width caption In enzymology , a hexose oxidase EC number 1.1.3.5 is an enzyme that catalysis catalyzes the chemical reaction D glucose O sub 2 sub math rightleftharpoons math D glucono 1,5 lactone H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are D glucose and oxygen O sub 2 sub , whereas its two product chemistry products are D glucono 1,5 lactone 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 hexose oxygen 1 oxidoreductase . This enzyme participates in pentose phosphate pathway . It employs one cofactor biochemistry cofactor , copper . References reflist 1 cite journal author BEAN RC, HASSID WZ date 1956 title Carbohydrate oxidase from A red alga, Iridophycus flaccidum journal J. Biol. Chem. volume 218 pages 425&ndash 36 pmid 13278350 issue 1 cite journal author BEAN RC, PORTER GG, STEINBERG BM date 1961 title Carbohydrate metabolism of citrus fruits. II. Oxidation of sugars by an aerodehydrogenase from young orange fruits journal J. Biol. Chem. volume 236 pages 1235&ndash 40 pmid 13688220 cite journal author Sullivan JD Jr, Ikawa M date 1973 title Purification and characterization of hexose oxidase from the red alga Chondrus crispus journal Biochim. Biophys. Acta. volume 309 pages 11&ndash 22 pmid 4708670 issue 1 1.1 enzyme stub Category EC 1.1.3 Category Copper enzymes Category Enzymes of unknown structure it Esoso ossidasi ja ... more details
enzyme Name pyridoxal oxidase EC number 1.2.3.8 CAS number 76415 81 1 IUBMB EC number 1 2 3 8 GO code 0004732 image width caption In enzymology , a pyridoxal oxidase EC number 1.2.3.8 is an enzyme that catalysis catalyzes the chemical reaction pyridoxal H sub 2 sub O O sub 2 sub math rightleftharpoons math 4 pyridoxate ? The 3 substrate biochemistry substrates of this enzyme are pyridoxal , water H sub 2 sub O , and oxygen O sub 2 sub , whereas its product chemistry product is 4 pyridoxate . 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 pyridoxal oxygen 4 oxidoreductase . This enzyme participates in vitamin B6 vitamin B sub 6 sub metabolism . It employs one cofactor biochemistry cofactor , molybdenum . References reflist 1 cite journal author Hanly EW date 1980 title Preliminary characterization and physical properties of pyridoxal oxidase activity from Drosophila melanogaster journal Mol. Gen. Genet. volume 180 issue 2 pages 455 462 doi 10.1007 BF00425862 cite journal author Warner CK, Watts DT and Finnerty V date 1980 title Molybdenum hydroxylases in Drosophila. I. Preliminary studies of pyridoxal oxidase journal Mol. Gen. Genet. volume 180 issue 2 pages 449 453 doi 10.1007 BF00425861 1.2 enzyme stub Category EC 1.2.3 Category Molybdenum enzymes Category Enzymes of unknown structure it Piridossale ossidasi ja ... more details
enzyme Name putrescine oxidase EC number 1.4.3.10 CAS number 9076 87 3 IUBMB EC number 1 4 3 10 GO code 0050232 image width caption In enzymology , a putrescine oxidase EC number 1.4.3.10 is an enzyme that catalysis catalyzes the chemical reaction putrescine O sub 2 sub H sub 2 sub O math rightleftharpoons math 4 aminobutanal NH sub 3 sub H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are putrescine , oxygen O sub 2 sub , and water H sub 2 sub O , whereas its 3 product chemistry products are 4 aminobutanal , ammonia NH sub 3 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 CH NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is putrescine oxygen oxidoreductase deaminating . This enzyme participates in urea cycle and metabolism of amino groups . It employs one cofactor biochemistry cofactor , FAD . References reflist 1 cite journal author DeSa RJ date 1972 title Putrescine oxidase from Micrococcus rubens. Purification and properties of the enzyme journal J. Biol. Chem. volume 247 pages 5527&ndash 34 pmid 4341347 issue 17 cite journal author Yamada H date 1971 title Putrescine oxidase Micrococcus rubens journal Methods Enzymol. volume 17B pages 726&ndash 730 1.4 enzyme stub Category EC 1.4.3 Category Flavin enzymes Category Enzymes of unknown structure it Putrescina ossidasi ja ... more details
enzyme Name Dihydrobenzophenanthridine oxidase EC number 1.5.3.12 IUBMB EC number 1 5 3 12 CAS number 114051 83 1 GO code 0047132 image width caption Dihydrobenzophenanthridine oxidase DHBP oxidase is an enzyme . In the IUBMB Enzyme Nomenclature, Dihydrobenzophenanthridine oxidase is EC number 1.5.3.12 . Dihydrobenzophenanthridine oxidase EC 1.5.3.12 produces oxidized forms of benzophenanthridine alkaloids In Bloodroot Sanguinaria Canadensis EC 1.5.3.12 produces sanguinarine from dihydrosanguinarine , and chelirubine from dihydrochelirubine . In Eschscholzia californica California poppy , EC 1.5.3.12 produces macarpine from dihydromacarpine . External links http www.chem.qmul.ac.uk iubmb enzyme EC1 5 3 12.html EC 1.5.3.12 International Union of Biochemistry and Molecular Biology, Recommendations on Biochemical & Organic Nomenclature, Symbols & Terminology etc., http www.chem.qmul.ac.uk iubmb web interface. http www.chem.qmul.ac.uk iubmb enzyme reaction alkaloid macarpine.html Chelirubine, Macarpine, and Sanguinarine Biosynthesis ibid. cite journal author Ignatov A, Clark WG, Cline SD, Psenak M, Krueger J, Coscia CJ title Elicitation of dihydrobenzophenanthridine oxidase in Sanguinaria canadensis cell cultures journal Phytochemistry journal Phytochemistry volume 43 issue 6 pages 1141 4 year 1996 pmid 8987906 doi 10.1016 S0031 9422 96 00540 7 cite journal author Park SU, Yu M, Facchini PJ title Antisense RNA mediated suppression of benzophenanthridine alkaloid biosynthesis in transgenic cell cultures of California poppy journal Plant Physiol. volume 128 issue 2 pages 696 706 year 2002 pmid 11842172 doi 10.1104 pp.010741 url http www.plantphysiol.org cgi content abstract 128 2 696 pmc 148930 cite journal author Rho D, Chauret N, Laberge N, Archambault J title Growth characteristics of Sanguinaria canadensis L. cell suspensions and immobilized cultures for production of benzophenanthridine alkaloids journal Appl. Microbiol. Biotechnol. volume 36 issue 5 pages 611 7 year ... 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
PBB geneid 4015 Lysyl oxidase also known as protein lysine 6 oxidase is a protein that, in humans, is encoded by the LOX gene . ref name entrez cite web title Entrez Gene LOX lysyl oxidase url http www.ncbi.nlm.nih.gov ... KI title Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3 ... and cancer cancerous . Function Lysyl oxidase is an extracellular copper enzyme that catalyzes formation ... Lysyl oxidases a novel multifunctional amine oxidase family journal Prog. Nucleic Acid Res. Mol. Biol ... These aldehydes are highly reactive, and undergo spontaneous chemical reactions with other lysyl oxidase ... K, Fujimoto D title Collagen cross linking lysyl oxidase dependent synthesis of pyridinoline in vitro ... 1 url ref The importance of lysyl oxidase derived cross linking was established from animal studies in which lysyl oxidase was inhibited either by nutritional copper deficiency or by supplementation of diets with aminopropionitrile BAPN , an inhibitor of lysyl oxidase. ref name pmid12135629 cite ... KR, Froines JR title In vitro and in vivo inhibition of lysyl oxidase by aminopropionitriles journal ... AJ title Lysyl oxidase is essential for hypoxia induced metastasis journal Nature volume 440 ... name pmid17079439 cite journal author Erler JT, Giaccia AJ title Lysyl oxidase mediates hypoxic control ... induced lysyl oxidase is a critical mediator of bone marrow cell recruitment to form the premetastatic ... oxidase as a potential therapeutic target journal Drug News Perspect. volume 21 issue 4 pages 218 ... citations cite journal author Csiszar K title Lysyl oxidases a novel multifunctional amine oxidase ... doi 10.1016 S0079 6603 01 70012 8 cite journal author Kagan HM, Li W title Lysyl oxidase properties ... DM, Twomey TA, Macauley SP, et al. title Characterization of the human lysyl oxidase gene locus journal ... oxidase and assignment of the gene to chromosome 5 extensive sequence homology with the murine ... author Murawaki Y, Kusakabe Y, Hirayama C title Serum lysyl oxidase activity in chronic liver disease ... more details
enzyme Name Aminocyclopropanecarboxylate oxidase EC number 1.14.17.4 CAS number IUBMB EC number 1 14 17 4 GO code image width caption In enzymology , an aminocyclopropanecarboxylate oxidase EC number 1.14.17.4 is an enzyme that catalysis catalyzes the chemical reaction 1 aminocyclopropane 1 carboxylate ascorbate O sub 2 sub math rightleftharpoons math ethylene cyanide dehydroascorbate CO sub 2 sub 2 H sub 2 sub O The 3 substrate biochemistry substrates of this enzyme are 1 aminocyclopropane 1 carboxylate , ascorbate , and oxygen O sub 2 sub , whereas its 5 product chemistry products are ethylene , cyanide , dehydroascorbate , carbon dioxide CO sub 2 sub , and water H sub 2 sub O . This enzyme belongs to the family of oxidoreductase s, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced ascorbate as one donor, and incorporation of one ato of oxygen into the other donor. The systematic name of this enzyme class is 1 aminocyclopropane 1 carboxylate oxygenase ethylene forming . Other names in common use include ACC oxidase , and ethylene forming enzyme . Structural studies As of late 2007, two tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1W9Y and PDB link 1WA6 . References reflist 1 cite journal author Zhang Z, Schofield CJ, Baldwin JE, Thomas P, John P date Pt 1 title Expression, purification and characterization of 1 aminocyclopropane 1 carboxylate oxidase from tomato in Escherichia coli journal Biochem. J. volume 307 pages 77&ndash 85 pmid 7717997 pmc 1136747 issue Pt 1 cite journal ... studies on the iron II binding site of 1 aminocyclopropane 1 carboxylate oxidase journal ... 1 carboxylic acid oxidase journal Arch. Biochem. Biophys. volume 385 pages 179&ndash 85 pmid ... JP date 2001 title Steady state kinetics of substrate binding and iron release in tomato ACC oxidase ... more details
enzyme Name alcohol oxidase EC number 1.1.3.13 CAS number 9073 63 6 IUBMB EC number 1 1 3 13 GO code 0047639 image width caption In enzymology , an alcohol oxidase EC number 1.1.3.13 is an enzyme that catalysis catalyzes the chemical reaction a primary alcohol O sub 2 sub math rightleftharpoons math an aldehyde H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are primary alcohol and oxygen O sub 2 sub , whereas its two product chemistry products are 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 alcohol oxygen oxidoreductase . This enzyme is also called ethanol oxidase . It employs one cofactor biochemistry cofactor , FAD . 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 1AHU , PDB link 1AHV , PDB link 1AHZ , PDB link 1VAO , PDB link 1W1J , PDB link 1W1K , PDB link 1W1L , PDB link 1W1M , and PDB link 2VAO . References reflist 1 cite journal author Janssen FW, Ruelius HW date 1968 title Alcohol oxidase, a flavoprotein from several Basidiomycetes species Crystallization by fractional precipitation with polyethylene glycol journal Biochim. Biophys. Acta. volume 151 pages 330&ndash 42 pmid 5636370 issue 2 cite journal author Nishida A, Ishihara T and Hiroi T date 1987 title Studies on enzymes related to lignan biodegradation journal Baiomasu Henkan Keikaku Kenkyu volume Hokoku pages 38&ndash 59 cite journal author Suye S date 1997 title Purification and properties of alcohol oxidase from Candida methanosorbosa M 2003 journal Curr. Microbiol. volume 34 pages 374&ndash 7 pmid 9142745 doi 10.1007 s002849900198 issue 6 1.1 enzyme stub Category EC 1.1.3 Category Flavin enzymes Category Enzymes of known structure it Alcol ossidasi ja ... more details
enzyme Name pyranose oxidase EC number 1.1.3.10 CAS number 37250 80 9 IUBMB EC number 1 1 3 10 GO code 0050233 image width caption In enzymology , a pyranose oxidase EC number 1.1.3.10 is an enzyme that catalysis catalyzes the chemical reaction D glucose O sub 2 sub math rightleftharpoons math 2 dehydro D glucose H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are D glucose and oxygen O sub 2 sub , whereas its two product chemistry products are 2 dehydro D glucose 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 pyranose oxygen 2 oxidoreductase . Other names in common use include glucose 2 oxidase , and pyranose 2 oxidase . This enzyme participates in pentose phosphate pathway . It employs one cofactor biochemistry cofactor , FAD . Structural studies As of late 2007, 8 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1TT0 , PDB link 1TZL , PDB link 2F5V , PDB link 2F6C , PDB link 2IGK , PDB link 2IGM , PDB link 2IGN , and PDB link 2IGO . References reflist 1 cite journal author Janssen FW, Ruelius HW date 1968 title Carbohydrate oxidase, a novel enzyme from Polyporus obtusus. II Specificity and characterization of reaction products journal Biochim. Biophys. Acta. volume 167 pages 501&ndash 10 pmid 5722278 issue 3 cite journal author Machida Y and Nakanishi T date 1984 title Purification and properties of pyranose oxidase from Coriolus versicolor journal Agric. Biol. Chem. volume 48 pages 2463&ndash 2470 cite journal author Neidleman SL, Amon WF, Jr and Geigert J date 1981 title Process for the production of fructose journal Chem. Abstr. volume 94 pages 20737 cite journal author Ruelius HW, Kerwin RM, Janssen FW date 1968 title Carbohydrate oxidase, a novel enzyme from Polyporus obtusus ... more details
orphan date February 2010 enzyme Name dihydrouracil oxidase EC number 1.3.3.7 CAS number 104327 11 9 IUBMB EC number 1 3 3 7 GO code 0047857 image width caption In enzymology , a dihydrouracil oxidase EC number 1.3.3.7 is an enzyme that catalysis catalyzes the chemical reaction 5,6 dihydrouracil O sub 2 sub math rightleftharpoons math uracil H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are 5,6 dihydrouracil and oxygen O sub 2 sub , whereas its two product chemistry products are uracil 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 5,6 dihydrouracil oxygen oxidoreductase . It employs one cofactor biochemistry cofactor , FMN . References reflist 1 cite journal author Owaki J, Uzura K, Minami Z and Kusai K year 1986 title Partial purification and characterization of dihydrouracil oxidase, a flavoprotein from Rhodotorula glutinis journal J. Ferment. Technol. volume 64 pages 205&ndash 210 doi 10.1016 0385 6380 86 90100 7 issue 3 Category EC 1.3.3 Category Flavin enzymes Category Enzymes of unknown structure 1.3 enzyme stub it Diidrouracil ossidasi ja ... more details
enzyme Name xylitol oxidase EC number 1.1.3.41 CAS number 177322 52 0 IUBMB EC number 1 1 3 41 GO code 0050582 image width caption In enzymology , a xylitol oxidase EC number 1.1.3.41 is an enzyme that catalysis catalyzes the chemical reaction xylitol O sub 2 sub math rightleftharpoons math xylose H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are xylitol and oxygen O sub 2 sub , whereas its two product chemistry products are xylose 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 xylitol oxygen oxidoreductase . References reflist 1 cite journal author Murooka Y date 2000 title Isolation, characterization, and molecular cloning of a thermostable xylitol oxidase from Streptomyces sp. IKD472 journal J. Biosci. Bioeng. volume 89 pages 350&ndash 60 pmid 16232758 doi 10.1016 S1389 1723 00 88958 6 last2 Omura first2 H last3 Okamoto first3 E last4 Furuya first4 Y last5 Yabuuchi first5 M last6 Fukahi first6 K last7 Murooka first7 Y issue 4 1.1 enzyme stub Category EC 1.1.3 Category Enzymes of unknown structure it Xilitolo ossidasi ja ... more details
enzyme Name cyclohexylamine oxidase EC number 1.4.3.12 CAS number 63116 97 2 IUBMB EC number 1 4 3 12 GO code 0018527 image width caption In enzymology , a cyclohexylamine oxidase EC number 1.4.3.12 is an enzyme that catalysis catalyzes the chemical reaction cyclohexylamine O sub 2 sub H sub 2 sub O math rightleftharpoons math cyclohexanone NH sub 3 sub H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are cyclohexylamine , oxygen O sub 2 sub , and water H sub 2 sub O , whereas its 3 product chemistry products are cyclohexanone , ammonia NH sub 3 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 CH NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is cyclohexylamine oxygen oxidoreductase deaminating . This enzyme participates in caprolactam degradation . It employs one cofactor biochemistry cofactor , FAD . References reflist 1 cite journal author Tokieda T, Niimura T, Takamura F, Yamaha T date Tokyo title Purification and some properties of cyclohexylamine oxidase from a Pseudomonas sp journal J. volume Biochem. pages 851&ndash 8 pmid 18451 issue 4 1.4 enzyme stub Category EC 1.4.3 Category Flavin enzymes Category Enzymes of unknown structure it Cicloesilammina ossidasi ja ... more details
enzyme Name dimethylglycine oxidase EC number 1.5.3.10 CAS number 74870 79 4 IUBMB EC number 1 5 3 10 GO code 0047866 image width caption In enzymology , a dimethylglycine oxidase EC number 1.5.3.10 is an enzyme that catalysis catalyzes the chemical reaction N,N dimethylglycine H sub 2 sub O O sub 2 sub math rightleftharpoons math sarcosine formaldehyde H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are N,N dimethylglycine , water H sub 2 sub O , and oxygen O sub 2 sub , whereas its 3 product chemistry products are sarcosine , formaldehyde , 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 N,N dimethylglycine oxygen oxidoreductase demethylating . It employs one cofactor biochemistry cofactor , FAD . Structural studies As of late 2007, 3 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB2 1PJ5 , PDB2 1PJ6 , and PDB2 1PJ7 . References reflist 1 cite journal author Mori N, Kawakami B, Tani Y and Yamada H date 1980 title Purification and properties of dimethylglycine oxidase from Cylindrocarpon didymum M 1 journal Agric. Biol. Chem. volume 44 pages 1383&ndash 1389 Category EC 1.5.3 Category Flavin enzymes Category Enzymes of known structure it Dimetilglicina ossidasi ja ... more details
enzyme Name ethanolamine oxidase EC number 1.4.3.8 CAS number 9013 00 7 IUBMB EC number 1 4 3 8 GO code 0047883 image width caption In enzymology , an ethanolamine oxidase EC number 1.4.3.8 is an enzyme that catalysis catalyzes the chemical reaction ethanolamine H sub 2 sub O O sub 2 sub math rightleftharpoons math glycolaldehyde NH sub 3 sub H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are ethanolamine , water H sub 2 sub O , and oxygen O sub 2 sub , whereas its 3 product chemistry products are glycolaldehyde , ammonia NH sub 3 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 CH NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is ethanolamine oxygen oxidoreductase deaminating . It has 2 cofactor biochemistry cofactors cobalt , and Cobamide . References reflist 1 cite journal author Narrod SA and Jakoby WB date 1964 title Metabolism of ethanolamine. An ethanolamine oxidase journal J. Biol. Chem. volume 239 pages 2189&ndash 2193 1.4 enzyme stub Category EC 1.4.3 Category Cobalt enzymes Category Cobamide enzymes Category Enzymes of unknown structure it Etanolammina ossidasi ja ... more details
enzyme Name prenylcysteine oxidase EC number 1.8.3.5 CAS number IUBMB EC number 1 8 3 5 GO code 0001735 image width caption In enzymology , a prenylcysteine oxidase EC number 1.8.3.5 is an enzyme that catalysis catalyzes the chemical reaction an S prenyl L cysteine O sub 2 sub H sub 2 sub O math rightleftharpoons math a prenal L cysteine H sub 2 sub O sub 2 sub The 3 substrate biochemistry substrates of this enzyme are S prenyl L cysteine , oxygen O sub 2 sub , and water H sub 2 sub O , whereas its 3 product chemistry products are prenal , L cysteine , 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 S prenyl L cysteine oxygen oxidoreductase . This enzyme is also called prenylcysteine lyase . References reflist 1 cite journal author Zhang L, Tschantz WR, Casey PJ date 1997 title Isolation and characterization of a prenylcysteine lyase from bovine brain journal J. Biol. Chem. volume 272 pages 23354&ndash 9 pmid 9287348 doi 10.1074 jbc.272.37.23354 issue 37 cite journal author Tschantz WR, Digits JA, Pyun HJ, Coates RM, Casey PJ date 2001 title Lysosomal prenylcysteine lyase is a FAD dependent thioether oxidase journal J. Biol. Chem. volume 276 pages 2321&ndash 4 pmid 11078725 doi 10.1074 jbc.C000616200 issue 4 1.8 enzyme stub Category EC 1.8.3 Category Enzymes of unknown structure it Prenilcisteina ossidasi ja ... more details
enzyme Name thiol oxidase EC number 1.8.3.2 CAS number 9029 39 4 IUBMB EC number 1 8 3 2 GO code 0016972 image width caption In enzymology , a thiol oxidase EC number 1.8.3.2 is an enzyme that catalysis catalyzes the chemical reaction 4 R C R SH O sub 2 sub math rightleftharpoons math 2 R C R S S R CR 2 H sub 2 sub O Thus, the two substrate biochemistry substrates of this enzyme are R C R SH and oxygen O sub 2 sub , whereas its two product chemistry products are R C R S S R CR and water H sub 2 sub O . 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 thiol oxygen oxidoreductase . This enzyme is also called sulfhydryl oxidase . References reflist 1 cite journal author AURBACH GD, JAKOBY WB date 1962 title The multiple functions of thiooxidase journal J. Biol. Chem. volume 237 pages 565&ndash 8 pmid 13863296 cite journal author NEUFELD HA, GREEN LF, LATTERELL FM, WEINTRAUB RL date 1958 title Thioxidase, a new sulfhydryl oxidizing enzyme from Piricularia oryzae and Polyporus versicolor journal J. Biol. Chem. volume 232 pages 1093&ndash 9 pmid 13549489 issue 2 1.8 enzyme stub Category EC 1.8.3 Category Enzymes of unknown structure it Tiolo ossidasi ja ... more details
enzyme Name cholesterol oxidase EC number 1.1.3.6 CAS number 9028 76 6 IUBMB EC number 1 1 3 6 GO code 0016995 image width caption Infobox protein family Symbol Chol subst bind Name Cholesterol oxidase substrate binding domain image PDB 1i19 EBI.jpg width caption crystal structure of cholesterol oxidase from b.sterolicum Pfam PF09129 Pfam clan CL0277 InterPro IPR015213 SMART PROSITE MEROPS SCOP 1i19 TCDB OPM family OPM protein CAZy CDD In enzymology , a cholesterol oxidase EC number 1.1.3.6 is an enzyme that catalysis catalyzes the chemical reaction cholesterol O sub 2 sub math rightleftharpoons math cholest 4 en 3 one H sub 2 sub O sub 2 sub Thus, the two substrate biochemistry substrates of this enzyme are cholesterol and oxygen O sub 2 sub , whereas its two product chemistry products are cholest 4 en 3 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 OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is cholesterol oxygen oxidoreductase . Other names in common use include cholesterol O2 oxidoreductase , 3beta hydroxy steroid oxidoreductase , and 3beta hydroxysteroid oxygen oxidoreductase . This enzyme participates in bile acid biosynthesis . The substrate binding protein domain domain found in some bacterial cholesterol oxidases is composed of an eight stranded mixed beta pleated sheet and six alpha helix alpha helices . This domain is positioned over the isoalloxazine ring system of the FAD Cofactor biochemistry cofactor bound by the FAD binding domain and forms the roof of the active site cavity, allowing for catalysis of redox oxidation and isomerisation of cholesterol to cholest 4 en 3 one. ref name pmid11397813 cite journal author Coulombe R, Yue KQ, Ghisla S, Vrielink A title Oxygen access to the active site of cholesterol oxidase through ... cite journal author Richmond W year 1973 title Preparation and properties of a cholesterol oxidase from ... more details
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