Infobox nonhuman protein Name Horseradishperoxidase image 1w4yhrp.png width caption Horseradishperoxidase C1 PDB PDBe 1w4y ref cite pmid 15641789 ref Organism Armoracia rusticana TaxID 3704 Symbol Peroxidase C1A AltSymbols PRXC1A IUPHAR id ATC prefix ATC suffix ATC supplemental CAS number CAS supplemental DrugBank EntrezGene PDB GWU PDB supplemental http www.ebi.ac.uk pdbe searchResults.html?display both&term P00433 More structures RefSeqmRNA RefSeqProtein UniProt P00433 ECnumber 1.11.1.7 Chromosome EntrezChromosome GenLoc start GenLoc end The enzyme horseradishperoxidase HRP , found in horseradish , is used extensively in biochemistry applications primarily for its ability to amplify a weak signal and increase detectability of a target molecule. Applications Horseradishperoxidase is a 44,173.9 ... properties in rat sympathetic ganglia by using lanthanum ion and horseradishperoxidase as tracers journal ... ref Horseradishperoxidase is also commonly used in techniques such as ELISA and Immunohistochemistry due to its monomeric nature and the ease with which it produces coloure products. Peroxidase ... cleavage of hydrogen peroxide by an electron donor. Horseradishperoxidase is ideal in many respects ... neurons with the enzyme horseradishperoxidase has become a major tool. In its brief history, this method ... with HorseradishPeroxidase adapted from D. Purves and J.W. Lichtman, Principles of Neural Development ... title Horseradishperoxidase a modern view of a classic enzyme journal Phytochemistry journal ... ref Numerous substrates for the horseradishperoxidase enzyme have been described and commercialized ... by X ray crystallography in 1997 ref Crystal structure of horseradishperoxidase C at 2.15 A resolution ... ECL main Chemiluminescence Horseradishperoxidase catalyses the oxidation of luminol to 3 aminophthalate ... of BBI Enzymes, a manufacturer of HRP . MeshName Horseradishperoxidase Peroxidases DEFAULTSORT HorseradishPeroxidase Category EC 1.11.1 cs Avidin peroxid za de Meerrettichperoxidase pl Peroksydaza ... more details
and J. W. Lichtman Cell Marking with HorseradishPeroxidase , 1985. http 8e.devbio.com article.php?ch 13&id 139. ref Horseradishperoxidase HRP is widely used in research for immunohistochemistry labelling ...About the plant the book by Lemony Snicket Horseradish Bitter Truths You Can t Avoid Horseradish tree Moringa oleifera taxobox name Horseradish image Armoracia rusticana.jpg regnum Plantae unranked divisio ... Roots of the horseradish plant File Gardenology.org IMG 2788 rbgs11jan.jpg thumb Foliage of the horseradish plant Image Horseradish prepared.jpg thumb 160px right Prepared horseradishHorseradish Armoracia ... metres five feet tall and is mainly cultivated for its large white, tapered root . The intact horseradish ... to air and heat. History Horseradish has been cultivated since antiquity. According to Greek mythology , the Delphic Oracle told Apollo that the horseradish was worth its weight in gold. ref The Encyclopedia of Healing Foods By Michael T. Murray, Lara Pizzorno ref Horseradish was known in Egypt in 1500 BC. Dioscorides listed horseradish under Thlaspi or Persicon Cato the Elder Cato discusses the plant in his treatises on agriculture, and a mural in Pompeii shows the plant. Horseradish is probably ... Gerard showed it under Raphanus . ref J. W. Courter and A. M. Rhodes, Historical notes on horseradish .... ref name motherearthnews.com cite news first Barbara last Pleasant title Horseradish url .... ref name motherearthnews.com William Turner ornithologist William Turner mentions horseradish as Red ... ?id PfMCAAAAYAAJ isbn 1 4369 9965 0 ref Where the English name horseradish comes from is not certain ... Horseradish is perennial plant perennial in hardiness zones 2&ndash 9 and can be grown as an annual ... offshoots of the main root are replanted to produce next year s crop. Horseradish left undisturbed ... bin store grow.html title How To Grow Horseradish accessdate 2007 07 01 work ref ref name motherearthnews.com ... , the Small White Butterfly, are a common caterpillar pest in horseradish. The adults are white butterflies ... more details
electron donor is very dependent on the structure of the enzyme. For example, horseradishperoxidase can use a variety of organic compounds as electron donors and acceptors. Horseradishperoxidase has .... A majority of peroxidase protein sequences can be found in the PeroxiBase database. Applications Peroxidase can be used for treatment of industrial waste waters. For example, phenols, which are important pollutants, can be removed by enzyme catalyzed polymerization using horseradishperoxidase ...Pfam box Symbol peroxidase Name Peroxidase image GlutPeroxidase 1GP1.png width caption Glutathione Peroxidase 1 Pfam PF00141 InterPro IPR002016 SMART Prosite PDOC00394 SCOP 1hsr TCDB OPM family OPM protein PDB Peroxidases Enzyme Commission number EC number http www.chem.qmul.ac.uk iubmb enzyme EC1 11 1 1.11.1.x are a large family of enzyme s that typically catalyze a reaction of the form ROOR electron donor 2 e sup sup 2H sup sup ROH R OH For many of these enzymes the optimal Substrate biochemistry ... closed active site, for an enzyme such as cytochrome c peroxidase , the compounds that donate ... used as histology histological marker. Cytochrome c peroxidase is used as a soluble, easily purified model for cytochrome c oxidase . The glutathione peroxidase family consists of 8 known human isoforms ... containing homologues in rodents. Amyloid beta , when bound to heme, has been shown to have peroxidase activity. ref Cite journal title Amyloid beta peptide binds with heme to form a peroxidase Relationship ... investigations about the use of peroxidase in many manufacturing processes like adhesives, computer chips, car parts, and linings of drums and cans. See also Glutathione peroxidase Haloperoxidase Myeloperoxidase ... peroxidase Vanadium bromoperoxidase Lactoperoxidase References Reflist Enzymes Peroxidases Use dmy ... Peroxidasen es Peroxidasa fr Peroxydase io Peroxidazo it Perossidasi kk nl Peroxidase ja pl Peroksydazy pt Peroxidase sv Peroxidas zh ... more details
enzyme Name Glutathione peroxidase EC number 1.11.1.9 CAS number 9013 66 5 IUBMB EC number 1 11 1 9 GO ... peroxidase 1. ref name pmid6852035 PDB 1GP1 cite journal author Epp O, Ladenstein R, Wendel A title The refined structure of the selenoenzyme glutathione peroxidase at 0.2 nm resolution journal ... 1033.1983.tb07429.x url ref Pfam box Symbol GSHPx Name Glutathione peroxidase image width caption ... 2f8a B 14 128 PDB3 1gp1 A 19 133 Glutathione peroxidase GPx EC number 1.11.1.9 is the general name of an enzyme family with peroxidase activity whose main biological role is to protect the organism from oxidative damage. The biochemical function of glutathione peroxidase is to reduce lipid Organic ... and substrate specificity. GPX1 Glutathione peroxidase 1 GPx1 is the most abundant version, found ... Glutathione peroxidase 4 GPx4 has a high preference for lipid hydroperoxides it is expressed in nearly every mammalian cell, though at much lower levels. GPX2 gene Glutathione peroxidase 2 is an intestinal and extracellular enzyme, while glutathione peroxidase 3 is extracellular, especially abundant ... url ref So far, eight different isoforms of glutathione peroxidase GPx1 8 have been identified in humans. class wikitable Gene Locus Enzyme GPX1 Chr. 3 p21.3 glutathione peroxidase 1 GPX2 gene GPX2 Chr. 14 q24.1 glutathione peroxidase 2 gastrointestinal GPX3 Chr. 5 q23 glutathione peroxidase 3 plasma GPX4 Chr. 19 p13.3 glutathione peroxidase 4 phospholipid hydroperoxidase GPX5 Chr. 6 p21.32 glutathione peroxidase 5 epididymal androgen related protein GPX6 Chr. 6 p21 glutathione peroxidase 6 olfactory GPX7 Chr. 1 p32 glutathione peroxidase 7 GPX8 Chr. 5 q11.2 glutathione peroxidase 8 putative Reaction An example reaction that glutathione peroxidase Catalyst catalyzes is 2GSH H sub 2 sub O sub .... As the integrity of the cellular and subcellular membranes depends heavily on glutathione peroxidase, the Antioxidant antioxidative protective system of glutathione peroxidase itself depends ... more details
enzyme Name NADPH peroxidase EC number 1.11.1.2 CAS number 9029 51 0 IUBMB EC number 1 11 1 2 GO code 0050137 image width caption In enzymology , a NADPH peroxidase EC number 1.11.1.2 is an enzyme that catalysis catalyzes the chemical reaction NADPH H sup sup H sub 2 sub O sub 2 sub math rightleftharpoons math NADP sup sup 2 H sub 2 sub O The 3 substrate biochemistry substrates of this enzyme are nicotinamide adenine dinucleotide phosphate NADPH , hydrogen ion H sup sup , and hydrogen peroxide H sub 2 sub O sub 2 sub , whereas its two product chemistry products are nicotinamide adenine dinucleotide phosphate NADP sup sup and water H sub 2 sub O . This enzyme belongs to the family of oxidoreductase s, specifically those acting on a peroxide as acceptor peroxidases . The systematic name of this enzyme class is NADPH hydrogen peroxide oxidoreductase . Other names in common use include TPNH peroxidase , NADP peroxidase , nicotinamide adenine dinucleotide phosphate peroxidase , TPN peroxidase , triphosphopyridine nucleotide peroxidase , and NADPH2 peroxidase . References reflist 1 cite journal author CONN EE, KRAEMER LM, LIU PN, VENNESLAND B date 1952 title The aerobic oxidation of reduced triphosphopyridine nucleotide by a wheat germ enzyme system journal J. Biol. Chem. volume 194 pages 143&ndash 51 pmid 14927602 issue 1 1.11 enzyme stub Category EC 1.11.1 Category NADPH dependent enzymes Category Enzymes of unknown structure it NADPH perossidasi ja NADPH ... more details
enzyme Name iodide peroxidase EC number 1.11.1.8 IUBMB EC number 1 11 1 8 CAS number 9031 28 1 GO code 0004447 image width caption protein Name thyroid peroxidase caption image width HGNCid 12015 Symbol TPO AltSymbols EntrezGene 7173 OMIM 606765 RefSeq NM 175722 UniProt P07202 PDB ECnumber 1.11.1.8 Chromosome 2 Arm Band LocusSupplementaryData pter p24 Thyroid peroxidase or thyroperoxidase TPO is an enzyme expressed mainly in the thyroid that liberates iodine for addition onto tyrosine residues on thyroglobulin for the production of thyroxine T sub 4 sub or triiodothyronine T sub 3 sub , thyroid hormones . ref name pmid16098474 cite journal author Ruf J, Carayon P title Structural and functional aspects of thyroid peroxidase journal Arch. Biochem. Biophys. volume 445 issue 2 pages 269 77 year 2006 month January pmid 16098474 doi 10.1016 j.abb.2005.06.023 url ref In humans, thyroperoxidase ..., Umeki K, Hirai K, Nakayama T, Ohtaki S title Human thyroid peroxidase complete cDNA and protein sequence ... Thyroid hormone synthesis.png thumb 300px Thyroid hormone synthesis , with thyroid peroxidase performing ... via pendrin , after which thyroid peroxidase oxidize s iodide to atomic iodine I or iodinium ... Kessler J, Obinger C, Eales G title Factors influencing the study of peroxidase generated iodine ... by thyroid peroxidase occur on the outer apical membrane surface and are mediated by hydrogen peroxide ... 6 propyl 2 thiouracil and 1 mehtyl 2 mercaptoimidazole on human thyroid iodine peroxidase journal ... jcem 43 1 152 url ref Clinical significance Thyroid peroxidase is a frequent epitope of autoantibody autoantibodies in autoimmune thyroid disease, with such antibodies being called anti thyroid peroxidase ... response to the thyroid in humans thyroid peroxidase the common autoantigenic denominator journal ... V, Lefranc MP, P raldi Roux S title The human anti thyroid peroxidase autoantibody repertoire in Graves ... External links MeshName Thyroid Peroxidase med stub Peroxidases Thyroid hormone metabolism enzymes ... more details
Ascorbate peroxidases or APX1 are enzymes that detoxify peroxides such as hydrogen peroxide using ascorbate as a substrate. The reaction they catalyse is the transfer of electrons from ascorbate to a peroxide, producing dehydroascorbate and water as products. ref cite journal author Raven EL title Peroxidase catalyzed oxidation of ascorbate. Structural, spectroscopic and mechanistic correlations in ascorbate peroxidase journal Subcell. Biochem. volume 35 issue pages 317 49 year 2000 pmid 11192727 doi 10.1007 0 306 46828 X 10 series Subcellular Biochemistry isbn 0 306 46399 7 ref Ascorbate Hydrogen peroxide Dehydroascorbate Water C sub 6 sub H sub 8 sub O sub 6 sub H sub 2 sub O sub 2 sub C sub 6 sub H sub 6 sub O sub 6 sub 2 H sub 2 sub O APX is an integral component of the glutathione ascorbate cycle . ref name Noctor cite journal author Noctor G, Foyer CH title ASCORBATE AND GLUTATHIONE Keeping Active Oxygen Under Control journal Annu Rev Plant Physiol Plant Mol Biol volume 49 pages 249 279 year 1998 month Jun pmid 15012235 doi 10.1146 annurev.arplant.49.1.249 ref These enzymes are commonly hemoproteins and the haem cofactor is the site of the oxidation reduction reaction shown above. ref cite journal author Raven EL, Lad L, Sharp KH, Mewies M, Moody PC title Defining substrate specificity and catalytic mechanism in ascorbate peroxidase journal Biochem. Soc. Symp. volume issue 71 pages 27 38 year 2004 pmid 15777010 ref References reflist External links http us.expasy.org enzyme 1.11.1.11 EC 1.11.1.11 http www.brenda.uni koeln.de php result flat.php4?ecno 1.11.1.11&organism L ascorbate peroxidase EC Number 1.11.1.11 Category Antioxidants enzyme stub ja pt Ascorbato peroxidase sr Askorbatna peroksidaza ... more details
enzyme Name NADH peroxidase EC number 1.11.1.1 CAS number 9032 24 0 IUBMB EC number 1 11 1 1 GO code 0016692 image Structure of NADH Peroxidase from Enterococcus faecalis.png width 296px caption The structure of NADH peroxidase from Enterococcus faecalis. Adapted from PDB 2NPX . In enzymology , a NADH peroxidase EC number 1.11.1.1 is an enzyme that catalysis catalyzes the chemical reaction NADH H sup ... function of NADH peroxidase is to inactivate H sub 2 sub O sub 2 sub generated within the cell, for example ... M, Hartke A title Comparative study of the physiological roles of three peroxidases NADH peroxidase, Alkyl hydroperoxide reductase and Thiol peroxidase in oxidative stress response, survival ... hydrogen peroxide oxidoreductase . Other names in common use include DPNH peroxidase , NAD peroxidase , diphosphopyridine nucleotide peroxidase , NADH peroxidase , nicotinamide adenine dinucleotide peroxidase , and NADH2 peroxidase . Structure The crystal structure of NADH peroxidase resembles glutathione ... site and catalysis of NADH peroxidase journal Eur. J. Biochem. volume 211 issue 1 2 pages 221 6 year 1993 month January pmid 8425532 doi 10.1111 j.1432 1033.1993.tb19889.x ref His10 of the NADH peroxidase ... peroxidase journal Meth. Enzymol. volume 353 issue pages 44 54 year 2002 pmid 12078517 doi 10.1016 ... thumb 300px Alignment of NADH, FAD and Cysteine 42 in NADH Peroxidase, Adapted from PDB 2NPX Image Four ... essential for active site functionality in NADH Peroxidase, Adapted from PDB 2NPX Reaction mechanism The NADH peroxidase from Enterococcus faecalis is unique in that it utilizes the Cys42 thiol sulfenic ... peroxidase R303M mutant correlation with the crystal structure journal Biochemistry volume 39 issue ... of the wild type peroxidase involves 1 NADH reduction of E FAD, Cys42 SOH to EH sub 2 sub FAD ... D, Poole LB, Claiborne A title Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals ... EJ, Parsonage D, Claiborne A title The active site histidine 10 of enterococcal NADH peroxidase ... more details
Eosinophil peroxidase is a haloperoxidase enzyme that in humans is encoded by the EPX gene . ref name ... and characterization of a chromosomal gene for human eosinophil peroxidase journal J. Biol. Chem. volume ... eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family journal J ... jem.169.5.1757 url ref The enzyme is a heterodimeric 71 77 kD peroxidase consisting of a heavier glycosylated ... sub O sub 2 sub formed by the eosinophil , and either chloride or bromide ions, eosinophil peroxidase ... bacteria . Eosinophil peroxidase is a haloperoxidase that preferentially uses bromide over chloride ... 26129 36 year 2005 pmid 15894800 doi 10.1074 jbc.M503027200 ref Eosinophil peroxidase is also partly ... peroxidase have been implicated in the inflammatory pathology of several disease states, including ... of eosinophil peroxidase journal Biochem. J. volume 358 issue Pt 1 pages 233 9 year 2001 month ... C, et al. title Hereditary eosinophil peroxidase deficiency immunochemical and spectroscopic studies ... peroxidase. Evidence for the existence of a peroxidase multigene family journal J. Exp. Med. volume ... Granule Toxins Mediated by Eosinophil Peroxidase journal J. Biol. Chem. volume 283 issue 42 ... Dalen CJ, Winterbourn CC, Kettle AJ title Mechanism of nitrite oxidation by eosinophil peroxidase ... Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase journal ... peroxidase and IL 4 receptor alpha chain in Japanese cedar pollinosis journal J. Allergy Clin ... in the eosinophil peroxidase gene with allergic rhinitis in the Czech population journal Int. Arch ... polymorphisms in the eosinophil peroxidase gene with Japanese cedar pollinosis journal Int. Arch ... K, Kanda N, Ueda T, et al. title The eosinophil peroxidase gene forms a cluster with the genes for myeloperoxidase ..., Vita F, Shankar S, et al. title Human Eosinophil Peroxidase Induces Surface Alteration, Killing, and Lysis ... peroxidase. The ester with Asp 93 is only partially formed in vivo journal J. Biol. Chem. volume ... more details
enzyme Name manganese peroxidase EC number 1.11.1.13 CAS number 114995 15 2 IUBMB EC number 1 11 1 13 GO code 0016689 image width caption In enzymology , a manganese peroxidase EC number 1.11.1.13 is an enzyme that catalysis catalyzes the chemical reaction 2 Mn II 2 H sup sup H sub 2 sub O sub 2 sub math rightleftharpoons math 2 Mn III 2 H sub 2 sub O The 3 substrate biochemistry substrates of this enzyme are Mn II , hydrogen ion H sup sup , and hydrogen peroxide H sub 2 sub O sub 2 sub , whereas its two product chemistry products are Mn III and water H sub 2 sub O . This enzyme belongs to the family of oxidoreductase s, to be specific those acting on a peroxide as acceptor peroxidases . The systematic name of this enzyme class is Mn II hydrogen peroxide oxidoreductase . Other names in common use include peroxidase M2 , and Mn dependent NADH oxidizing peroxidase . It employs one cofactor biochemistry cofactor , heme . This enzyme needs Ca sup 2 sup for activity. White rot fungi secrete this enzyme to aid lignin degradation. Structural studies As of late 2007, 6 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1MN1 , PDB link 1MN2 , PDB link 1YYD , PDB link 1YYG , PDB link 1YZP , and PDB link 1YZR . References reflist 1 cite journal author Glenn JK, Akileswaran L, Gold MH year 1986 title Mn II oxidation is the principal function of the extracellular Mn peroxidase from Phanerochaete chrysosporium journal Arch. Biochem. Biophys. volume 251 pages 688&ndash 96 pmid 3800395 doi 10.1016 0003 9861 86 90378 4 issue 2 cite journal author Paszczynski A, Huynh VB, Crawford R year 1986 title Comparison of ligninase I and peroxidase M2 from the white rot fungus Phanerochaete chrysosporium journal Arch. Biochem. Biophys. volume 244 pages 750&ndash 65 pmid 3080953 doi 10.1016 0003 9861 86 90644 2 issue 2 cite journal author Wariishi H, Akileswaran L and Gold MH year 1988 title Manganese peroxidase from the basidiomycete ... more details
enzyme Name diarylpropane peroxidase EC number 1.11.1.14 CAS number 93792 13 3 IUBMB EC number 1 11 1 14 GO code 0016690 image width caption Lignin is highly resistant to biodegradation and only higher fungi are capable of degrading the polymer via an oxidative process. This process has been studied extensively in the past twenty years, but the actual mechanism has not yet been fully elucidated. The complicated structure of the lignin polymer and major difficulties in analysis are responsible for the relatively slow progress Lignin is found to be degraded by an enzyme lignin peroxidases produced by some fungi like Phanerochaete chrysosporium . The mechanism by which lignin peroxidase Lip interacts with the lignin polymer which involves Veratryl alcohol Valc , a secondary metabolite of white rot fungi, acts as a cofactor for the enzyme In enzymology , a lignin peroxidase EC number 1.11.1.14 is an enzyme that catalysis catalyzes the chemical reaction 1,2 bis 3,4 dimethoxyphenyl propane 1,3 diol H sub 2 sub O sub 2 sub math rightleftharpoons math 3,4 dimethoxybenzaldehyde 1 3,4 dimethoxyphenyl ethane 1,2 diol H sub 2 sub O Thus, the two substrate biochemistry substrates of this enzyme are 1,2 bis 3,4 dimethoxyphenyl propane 1,3 diol and hydrogen peroxide H sub 2 sub O sub 2 sub , whereas its 3 product chemistry products are 3,4 dimethoxybenzaldehyde , 1 3,4 dimethoxyphenyl ethane 1,2 ... , ligninase I , diarylpropane peroxidase , LiP , diarylpropane oxygen,hydrogen peroxide oxidoreductase ... Hans E. Schoemaker and Klaus Piontek title On the interaction of lignin peroxidase with lignin, journal ... I and peroxidase M2 from the white rot fungus Phanerochaete chrysosporium journal Arch. Biochem. Biophys ... substrate interaction sites in lignin peroxidase revealed by site directed mutagenesis journal Biochemistry ... author Wariishi H, Marquez L, Dunford HB, Gold MH year 1990 title Lignin peroxidase compounds II and III ... title Role of molecular oxygen in lignin peroxidase reactions journal Arch. Biochem. Biophys. volume ... more details
enzyme Name chloride peroxidase EC number 1.11.1.10 CAS number 9055 20 3 IUBMB EC number 1 11 1 10 GO code 0016691 image width caption Chloride peroxidase EC number 1.11.1.10 is an enzyme that catalysis catalyzes the chemical reaction 2 RH 2 Cl H sub 2 sub O sub 2 sub math rightleftharpoons math 2 RCl 2 H sub 2 sub O The 3 substrate biochemistry substrates of this enzyme are a hydrogen containing molecule RH , chloride ion, and hydrogen peroxide , whereas its two product chemistry products are a corresponding chloride compound and water . This enzyme belongs to the family of oxidoreductase s, specifically those acting on a peroxide as acceptor peroxidases . The systematic name of this enzyme class is chloride hydrogen peroxide oxidoreductase . This enzyme is also called chloroperoxidase . It employs one cofactor biochemistry cofactor which may be either heme or vanadia. Chloroperoxidases are heme or vanadium containing enzymes that exhibits peroxidase, catalase and cytochrome P450 like activities in addition to catalyzing halogenation reactions ref name PUB00005255 cite journal doi 10.1016 S0969 2126 01 00274 X author Poulos TL, Sundaramoorthy M, Terner J title The crystal structure of chloroperoxidase a heme peroxidase cytochrome P450 functional hybrid journal Structure volume 3 issue 12 pages 1367 1377 year 1995 pmid 8747463 ref . Despite functional similarities with other heme enzymes, CPO folds into a novel tertiary structure dominated by eight helical segments. The catalytic base, required to cleave the peroxide O O bond, is glutamic acid rather than histidine as in other peroxidases. Structural studies As of late 2007, 30 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1A7U , PDB link 1A88 , PDB link 1A8Q , PDB link 1A8S , PDB link 1A8U , PDB link 1BRT , PDB link 1CPO , PDB link 1IDQ , PDB ... LP, Hollenberg PF, Rand Meir T, Chiang R, Doubek D date 1975 title Chemistry of peroxidase intermediates ... more details
Orphan date December 2010 Pfam box Symbol peroxidase Name Peroxidase image width caption Pfam PF00141 InterPro IPR002016 SMART Prosite PDOC00394 SCOP 1hsr TCDB OPM family OPM protein CDD cd00314 PDB PDB3 1qgj B 46 293 PDB3 1sch A 40 280 PDB3 1qo4 A 48 297 PDB3 1pa2 A 48 297 PDB3 1fhf B 44 293 PDB3 1h5i A 48 299 PDB3 1atj B 48 299 PDB3 4atj B 48 299 PDB3 1gwt A 48 299 PDB3 1gwo A 48 299 PDB3 1gx2 B 48 299 PDB3 1h5c A 48 299 PDB3 1h5a A 48 299 PDB3 1h58 A 48 299 PDB3 3atj A 48 299 PDB3 7atj A 48 299 PDB3 1h5e A 48 299 PDB3 1gw2 A 48 299 PDB3 1h55 A 48 299 PDB3 1h57 A 48 299 PDB3 1w4y A 48 299 PDB3 1h5f A 48 299 PDB3 1kzm A 48 299 PDB3 2atj B 48 299 PDB3 1hch A 48 299 PDB3 1h5d A 48 299 PDB3 1w4w A 48 299 PDB3 6atj A 48 299 PDB3 1h5m A 48 299 PDB3 1h5l A 48 299 PDB3 1gwu A 48 299 PDB3 1h5h A 48 299 PDB3 1h5j A 48 299 PDB3 1h5k A 48 299 PDB3 1h5g A 48 299 PDB3 1bgp 1 118 PDB3 1iyn A 15 243 PDB3 1apx B 19 227 PDB3 1oag A 19 227 PDB3 1v0h X 19 227 PDB3 1oaf A 19 227 PDB3 1cpf 89 321 PDB3 1s6v C 89 321 PDB3 2pcc A 89 321 PDB3 1z53 A 89 321 PDB3 1u74 A 89 321 PDB3 1cmt 89 321 PDB3 2cep 89 321 ... Poulos TL, Li H title Structural variation in heme enzymes a comparative analysis of peroxidase and P450 ..., includes yeast cytochrome c peroxidase CCP , a soluble protein found in the mitochondrial electron transport chain, where it probably protects against toxic peroxides ascorbate peroxidase ... plants ref name PUB00005930 cite journal author Dalton DA title Ascorbate peroxidase journal volume 2 issue pages 139 153 year 1991 ref and bacterial catalase peroxidases, exhibiting both peroxidase and catalase activities. It is thought that catalase peroxidase provides protection to cells under oxidative ... are gene duplicated members of the plant peroxidase superfamily journal Biochim. Biophys. Acta ... group is embedded. Another family of haem peroxidases is the DyP type peroxidase family . ref ... DEFAULTSORT Haem Peroxidase Category Protein domains Category EC 1.11.1 Category Hemoproteins ... more details
enzyme Name phospholipid hydroperoxide glutathione peroxidase EC number 1.11.1.12 CAS number 97089 70 8 IUBMB EC number 1 11 1 12 GO code 0047066 image width caption In enzymology , a phospholipid hydroperoxide glutathione peroxidase EC number 1.11.1.12 is an enzyme that catalysis catalyzes the chemical reaction 2 glutathione a lipid hydroperoxide math rightleftharpoons math glutathione disulfide lipid 2 H sub 2 sub O Thus, the two substrate biochemistry substrates of this enzyme are glutathione and lipid hydroperoxide , whereas its 3 product chemistry products are glutathione disulfide , lipid , and water H sub 2 sub O . This enzyme belongs to the family of oxidoreductase s, to be specific those acting on a peroxide as acceptor peroxidases . The systematic name of this enzyme class is glutathione lipid hydroperoxide oxidoreductase . Other names in common use include peroxidation inhibiting protein , PHGPX , peroxidation inhibiting protein peroxidase, glutathione , phospholipid hydroperoxide reducing , phospholipid hydroperoxide glutathione peroxidase , hydroperoxide glutathione peroxidase , or glutathione peroxidase 4 GPX4 . This enzyme participates in glutathione metabolism . 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 2GS3 and PDB link 2OBI . References reflist 1 cite journal author Ursini F, Maiorino M, Gregolin C date 1985 title The selenoenzyme phospholipid hydroperoxide glutathione peroxidase journal Biochim. Biophys. Acta. volume 839 pages 62&ndash 70 pmid 3978121 issue 1 1.11 enzyme stub Category EC 1.11.1 Category Enzymes of known structure it Fosfolipide idroperossido glutatione perossidasi ja ... more details
enzyme Name cytochrome c peroxidase EC number 1.11.1.5 IUBMB EC number 1 11 1 5 CAS number 9029 53 2 GO code 0004130 image width caption Cytochrome c peroxidase , or CCP is a water soluble heme containing enzyme of the peroxidase family that takes reducing equivalents from cytochrome c cytochrome c and reduces hydrogen peroxide to water CCP H sub 2 sub O sub 2 sub 2 ferrocytochrome c 2H sup sup CCP 2H sub 2 sub O 2 ferricytochrome c Cytochrome c peroxidase can react with hydroperoxides other than hydrogen peroxide, but the reaction rate is much slower than with hydrogen peroxide. It was first isolated from baker s yeast by R. A. Altschul, Abrams, and Hogness in 1940, ref Altchul, A. M., Abrams, R., and Hogness, T. R. 1940 Cytochrome c peroxidase. J. Biol. Chem., 136, 777. ref though not to purity. The first purified preparation of yeast CCP dates to Takashi Yonetani and his preparation by ion exchange chromatography in the early 1960s. The X ray crystallography X ray structure was the work of Thomas Poulos and coworkers in the late 1970s. ref Poulos, T. L., Freer, S. T., Alden, R. A., Edwards, S. L., Skogland, U., Takio, K., Eriksson, B., Xuong, N., Yonetani, T., and Kraut, J. 1980 http www.jbc.org content 255 2 575.full.pdf The crystal structure of cytochrome c peroxidase. J. Biol. Chem. 255, 575 580. ref The yeast enzyme is a monomer of molecular weight 34,000, containing 293 amino acids, and contains as well a single noncovalently bound heme b . Unusual for proteins, this enzyme crystallizes when dialysis biochemistry dialysed against distilled water. More so, the enzyme ... step. Much like catalase , the reaction of cytochrome c peroxidase proceeds through a three ... of other peroxidase compound I species. Early on it was recognized to be an organic free radical ... faculty.ucsd.edu kraut projects.html Cytochrome c peroxidase , maintained by the http chem faculty.ucsd.edu ... entry for yeast cytochrome c peroxidase. Peroxidases DEFAULTSORT Cytochrome C Peroxidase Category EC ... more details
enzyme Name L ascorbate peroxidase EC number 1.11.1.11 CAS number 72906 87 7 IUBMB EC number 1 11 1 11 GO code 0016688 image width caption In enzymology , a L ascorbate peroxidase EC number 1.11.1.11 is an enzyme that catalysis catalyzes the chemical reaction L ascorbate H sub 2 sub O sub 2 sub math rightleftharpoons math dehydroascorbate 2 H sub 2 sub O Thus, the two substrate biochemistry substrates of this enzyme are L ascorbate and hydrogen peroxide H sub 2 sub O sub 2 sub , whereas its two product chemistry products are dehydroascorbate and water H sub 2 sub O . This enzyme belongs to the family of oxidoreductase s, specifically those acting on a peroxide as acceptor peroxidases . The systematic name of this enzyme class is L ascorbate hydrogen peroxide oxidoreductase . Other names in common use include L ascorbic acid peroxidase , L ascorbic acid specific peroxidase , ascorbate peroxidase , and ascorbic acid peroxidase . This enzyme participates in ascorbate and aldarate metabolism . 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 1APX , PDB link 1IYN , PDB link 1OAF , PDB link 1OAG , PDB link 1V0H , PDB link 2CL4 , PDB link 2GGN , PDB link 2GHC , PDB link 2GHD , PDB link 2GHE , PDB link 2GHH , and PDB link 2GHK . References reflist 1 cite journal author Shigeoka S, Nakano Y, Kitaoka S date 1980 title Purification and some properties of L ascorbic acid specific peroxidase in Euglena gracilis Z journal Arch. Biochem. Biophys. volume 201 pages 121&ndash 7 pmid 6772104 doi 10.1016 0003 9861 80 90495 6 issue 1 cite journal author Shigeoka S, Nakano Y, Kitaoka S date 1980 title Metabolism of hydrogen peroxide in Euglena gracilis Z by L ascorbic acid peroxidase journal Biochem. J. volume 186 pages 377&ndash 80 pmid 6768357 issue 1 pmc 1161541 1.11 enzyme stub Category EC 1.11.1 Category Enzymes of known structure it L ascorbato perossidasi sr L askorbatna ... more details
Infobox protein family Symbol Dyp perox Name Dyp type peroxidase family image PDB 2gvk EBI.jpg width caption crystal structure of a dye decolorizing peroxidase dyp from bacteroides thetaiotaomicron vpi 5482 at 1.6 a resolution Pfam PF04261 Pfam clan CL0032 InterPro IPR006314 SMART PROSITE MEROPS SCOP TCDB OPM family OPM protein CAZy CDD In molecular biology, the DyP type peroxidase family is a family of haem peroxidase enzymes . Haem peroxidase s were originally divided into two superfamilies, namely, the animal peroxidases and the plant peroxidases which are subdivided into class I, II and III , which include fungus fungal class II and bacteria bacterial peroxidases. The DyP for dye de colourising peroxidase family constitutes a novel class of haem peroxidase. Because these enzyme s were derived from fungal sources, the DyP family was thought to be structurally related to the class II secretory fungal peroxidases. However, the DyP family exhibits only low sequence biology sequence similarity to classical fungal peroxidases, such as LiP and MnP, and does not contain the conserved proximal and distal histidines and an essential arginine found in other plant peroxidase superfamily members. DyP protein s have several characteristics that distinguish them from all other peroxidases, including a particularly wide Enzyme substrate substrate specificity, a lack of homology to most other peroxidases, and the ability to function well under much lower pH conditions compared with the other plant peroxidases. ref name pmid17654545 cite journal author Zubieta C, Krishna SS, Kapoor M, Kozbial ... specificity, DyP degrades the typical peroxidase substrates, but also degrades hydroxyl free ... of heme binding in a novel dye decolorizing peroxidase, TyrA journal Proteins volume 69 issue ... Y, Muramatsu R, Ichiyanagi A, Sato T, Shoda M title DyP, a unique dye decolorizing peroxidase, represents a novel heme peroxidase family ASP171 replaces the distal histidine of classical peroxidases ... more details
enzyme Name fatty acid peroxidase EC number 1.11.1.3 CAS number 9029 52 1 IUBMB EC number 1 11 1 3 GO code 0047888 image width caption In enzymology , a fatty acid peroxidase EC number 1.11.1.3 is an enzyme that catalysis catalyzes the chemical reaction palmitate 2 H sub 2 sub O sub 2 sub math rightleftharpoons math pentadecanal CO sub 2 sub 3 H sub 2 sub O Thus, the two substrate biochemistry substrates of this enzyme are palmitate and hydrogen peroxide H sub 2 sub O sub 2 sub , whereas its 3 product chemistry products are pentadecanal , 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 a peroxide as acceptor peroxidases . The systematic name of this enzyme class is hexadecanoate hydrogen peroxide oxidoreductase . This enzyme is also called long chain fatty acid peroxidase . References reflist 1 cite journal author MARTIN RO, STUMPF PK date 1959 title Fat metabolism in higher plants. XII. alpha Oxidation of long chain fatty acids journal J. Biol. Chem. volume 234 pages 2548&ndash 54 pmid 14421733 1.11 enzyme stub Category EC 1.11.1 Category Enzymes of unknown structure it Acido grasso perossidasi ja ... more details
improveref date July 2011 Infobox Book See Wikipedia WikiProject Novels or Wikipedia WikiProject Books name Horseradish Bitter Truths You Can t Avoid title orig translator image prefer 1st edition image caption author Lemony Snicket illustrator cover artist country United States language English language English series genre Fiction publisher HarperCollins release date April 24, 2007 United States U.S. br September 3, 2007 United Kingdom U.K. english release date media type Print Paperback pages 168 pp isbn 0 06 124006 0 dewey 818 .54 22 congress PS3558.A4636 H67 2007 oclc 123417401 preceded by followed by Horseradish Bitter Truths You Can t Avoid is a 2007 book written by Lemony Snicket . It is a wit and wisdom quotation book partly drawn from Snicket s famous A Series of Unfortunate Events . ref Lemony Snicket AuthorTracker April 24th In thirteen far reaching chapters from Family to Emotional Health, from A Life of Mystery to The Mystery of Life Horseradish puts the unhappy mind of Mr. Snicket at your fingertips. This compendium of wisdom drawn from his published works and his unpublishable remarks is the perfect gift for loved ones and enemies alike. ref Contents Following the tradition of Snicket s work, Horseradish has thirteen chapters, each with a certain theme. The book is prefaced with an introduction that outlines these themes. Introduction The bulk of the introduction follows the story of a man and a woman who live in a small grass hut in a village surrounded by a horseradish field. They generally live a routine life, and, as they have no taste for the horseradish, spend most of their time hunting to prepare raisin stuffed snail s to provide for their meals. One night, the woman asks her husband if there is more to life than doing the same thing for years. Her husband replies that the woman s mother once told him about a wise man who would probably know. The woman visits her mother, who says that she heard about the wise man from the woman s third grade t ... more details
Infobox protein family Symbol CCP MauG Name Di haem cytochrome c peroxidase image PDB 1eb7 EBI.jpg width caption crystal structure of the di haem cytochrome c peroxidase from pseudomonas aeruginosa Pfam PF03150 Pfam clan CL0318 InterPro IPR004852 SMART PROSITE MEROPS SCOP 1eb7 TCDB OPM family OPM protein CAZy CDD In molecular biology, the di haem cytochrome c peroxidase family is a group of distinct cytochrome c peroxidase cytochrome c peroxidases CCPs that contain two haem groups. Similar to other cytochrome c peroxidases, they reduce hydrogen peroxide to water using c type haem as an oxidizable Enzyme substrate substrate . However, since they possess two, instead of one, haem prosthetic groups , this family of bacteria bacterial CCPs reduce hydrogen peroxide without the need to generate semi stable free radical s. The two haem groups have significantly different redox potentials. The high potential 320 mV haem feeds electron s from electron shuttle protein s to the low potential 330 mV haem, where peroxide is Redox reduced indeed, the low potential site is known as the peroxidatic site . ref name pmid8591033 cite journal author Fulop V, Ridout CJ, Greenwood C, Hajdu J title Crystal structure of the di haem cytochrome c peroxidase from Pseudomonas aeruginosa journal Structure volume 3 issue 11 pages 1225 33 year 1995 month November pmid 8591033 doi url ref The CCP protein itself is structured into two domains, each containing one c type haem group, with a calcium binding site at the domain interface. This family also includes MauG proteins, whose similarity to di haem CCP was previously recognised. ref name pmid9202457 cite journal author Gak ER, Tsygankov YD, Chistoserdov AY title Organization of methylamine utilization genes mau in Methylobacillus flagellatum KT and analysis of mau mutants journal Microbiology Reading, Engl. volume 143 issue 6 pages 1827 35 year 1997 month June pmid 9202457 doi url ref References reflist InterPro content IPR004852 Category Protein ... more details
A histochemical tracer is a compound used to reveal the location of cell biology cell s and track neuron neuronal projections. A neuronal tracer may be retrograde, anterograde, or work in both directions. A retrograde tracer is taken up in the terminal of the neuron and transported to the cell body, whereas an anterograde tracer moves away from the cell body of the neuron. List Diamidino yellow Fast blue Horseradish peroxidase retrograde Cholera toxin Cholera toxin B ref Kreier Felix et al 2006 ref Pseudorabies Pseudorabies virus ref Kreier Felix et al 2006 ref Hydroxystilbamidine retrograde Texas Red Fluorescein isothiocyanate Footnotes Reflist 2 References Kreier Felix Kap Yolanda S Mettenleiter Thomas C van Heijningen Caroline van der Vliet Jan Kalsbeek Andries Sauerwein Hans P Fliers Eric Romijn Johannes A Buijs Ruud M 2006 . Tracing from fat tissue, liver, and pancreas a neuroanatomical framework for the role of the brain in type 2 diabetes , Endocrinology , 147 3 1140 7. Category Histology ... more details
ECL may stand for ECL programming language , an extensible programming language developed at Harvard ECL, data centric programming language for Big Data , a declarative, data centric programming language used for data intensive supercomputing Exit Control List , which lists people prohibited from exiting Pakistan Eastern Counties Football League Eastern Counties League , a football league in East Anglia, England Ecolab , a sanitation supply company whose NYSE ticker symbol is ECL Ecole centrale de Lille , a graduate engineering school in Lille, France Ecole centrale de Lyon , a graduate engineering school in Lyon, France Educational Community License , an open source license issued to academic institutions for otherwise copyrighted material Embeddable Common Lisp , an implementation of the Lisp programming language Emitter coupled logic , an electronic logic family Electrochemiluminescence , a kind of luminescence produced during electrochemical reactions in solutions Enterochromaffin like cell , a gastric cell Chemoluminescence ECL Enzymatic Chemiluminescence , a technique used commonly in biochemistry Horseradish peroxidase Enhanced chemiluminescence ECL Enhanced Chemoluminescence UEFA Champions League European Champions League , top club football competition in Europe Eastern Colored League one of the several Negro Leagues that were established during the early twentieth century in the United States when professional baseball was segregated disambig de ECL fr ECL it ECL ja ECL sr ECL ... more details
Hrp or HRP may refer to Hard Rock Park , a former amusement park now called the Freestyle Music Park Haute Randonn e Pyr n enne , a high level long distance trail in the Pyrenees Mountains Human resources planning Hybrid Roleplay , a popular Warcraft III map based on the similar DoBRP The Harvard Review of Philosophy , a journal of philosophy. Organizations Halifax Regional Police , a law enforcement agency operating in the Halifax Regional Municipality, Nova Scotia, Canada Happiness Realization Party , a Japanese political party Haryana Republican Party , a political party in the Indian state of Haryana Human Rights Party disambiguation Human Rights Party , various political groups Science and Technology Anti spam techniques HELO EHLO checking HELO Randomization Prevention , a technique to detect and reject spambot email messages. Horseradish peroxidase , an enzyme famed for its ability to amplify a weak biochemical signal HRP Rescuer , an American 1940s tandem rotor helicopter The Piasecki H 21 Piasecki Rescuer pre 1962 US Navy designation a successor helicopter developed from the HRP Rescuer Humanoid Robotics Project disambig de HRP fr HRP ... more details
Biotinylated dextran amines BDA are organic compounds used as anterograde tracing anterograde and Retrograde tracing retrograde Histochemical tracer neuroanatomical tracers . They can be used for labeling the source as well as the point of termination of Neuron neural connections and therefore to study neural pathway s. BDA is delivered into the nervous system by iontophoresis iontophoretic or pressure injection and visualized with an avidin biotinylated Horseradish peroxidase procedure, followed by a standard or metal enhanced 3,3 Diaminobenzidine diaminobenzidine DAB reaction. Samples can then be analyzed by optical microscopy as well as by electron microscopy . High molecular weight BDA 10 kDa yields sensitive and detailed labeling of axons and terminals, while low molecular weight BDA 3 kDa yields sensitive and detailed retrograde labeling of neuronal cell bodies ref name Reiner 2000 cite journal author Reiner A, Veenman CL, Medina L, Jiao Y, Del Mar N, Honig MG title Pathway tracing using biotinylated dextran amines journal J Neurosci Methods volume 103 issue 1 pages 23 37 year 2000 doi 10.1016 S0165 0270 00 00293 4 pmid 11074093 ref . References Reflist 2 DEFAULTSORT Biotinylated Dextran Amine Amine stub Category Amines Category Article Feedback 5 ... more details
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