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| {{Pfam_box
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| | Symbol = peroxidase
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| | Name = Peroxidase
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| | image =
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| | width =
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| | caption =
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| | Pfam= PF00141
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| | InterPro= IPR002016
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| | SMART=
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| | Prosite = PDOC00394
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| | SCOP = 1hsr
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| | TCDB =
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| | OPM family=
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| | OPM protein=
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| | CDD = cd00314
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| | PDB=
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| {{PDB3|1qgj}}B:46-293 {{PDB3|1sch}}A:40-280 {{PDB3|1qo4}}A:48-297
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| {{PDB3|1pa2}}A:48-297 {{PDB3|1fhf}}B:44-293 {{PDB3|1h5i}}A:48-299
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| {{PDB3|1atj}}B:48-299 {{PDB3|4atj}}B:48-299 {{PDB3|1gwt}}A:48-299
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| {{PDB3|1gwo}}A:48-299 {{PDB3|1gx2}}B:48-299 {{PDB3|1h5c}}A:48-299
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| {{PDB3|1h5a}}A:48-299 {{PDB3|1h58}}A:48-299 {{PDB3|3atj}}A:48-299
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| {{PDB3|7atj}}A:48-299 {{PDB3|1h5e}}A:48-299 {{PDB3|1gw2}}A:48-299
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| {{PDB3|1h55}}A:48-299 {{PDB3|1h57}}A:48-299 {{PDB3|1w4y}}A:48-299
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| {{PDB3|1h5f}}A:48-299 {{PDB3|1kzm}}A:48-299 {{PDB3|2atj}}B:48-299
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| {{PDB3|1hch}}A:48-299 {{PDB3|1h5d}}A:48-299 {{PDB3|1w4w}}A:48-299
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| {{PDB3|6atj}}A:48-299 {{PDB3|1h5m}}A:48-299 {{PDB3|1h5l}}A:48-299
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| {{PDB3|1gwu}}A:48-299 {{PDB3|1h5h}}A:48-299 {{PDB3|1h5j}}A:48-299
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| {{PDB3|1h5k}}A:48-299 {{PDB3|1h5g}}A:48-299 {{PDB3|1bgp}} :1-118
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| {{PDB3|1iyn}}A:15-243 {{PDB3|1apx}}B:19-227 {{PDB3|1oag}}A:19-227
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| {{PDB3|1v0h}}X:19-227 {{PDB3|1oaf}}A:19-227 {{PDB3|1cpf}} :89-321
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| {{PDB3|1s6v}}C:89-321 {{PDB3|2pcc}}A:89-321 {{PDB3|1z53}}A:89-321
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| {{PDB3|1u74}}A:89-321 {{PDB3|1cmt}} :89-321 {{PDB3|2cep}} :89-321
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| {{PDB3|2b0z}}A:89-321 {{PDB3|1beq}} :89-321 {{PDB3|1ccj}} :89-321
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| {{PDB3|2b10}}C:89-321 {{PDB3|1aef}} :89-321 {{PDB3|1ccg}} :89-321
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| {{PDB3|1cca}} :89-321 {{PDB3|3ccp}} :89-321 {{PDB3|1aem}} :89-321
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| {{PDB3|1aeg}} :89-321 {{PDB3|1dj5}}A:89-321 {{PDB3|7ccp}} :89-321
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| {{PDB3|6ccp}} :89-321 {{PDB3|1cmu}} :89-321 {{PDB3|1u75}}C:89-321
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| {{PDB3|1cmp}} :89-321 {{PDB3|4ccx}} :89-321 {{PDB3|1aej}} :89-321
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| {{PDB3|1aet}} :89-321 {{PDB3|1dj1}}A:89-321 {{PDB3|1s73}}A:89-321
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| {{PDB3|1aeq}} :89-321 {{PDB3|1bem}} :89-321 {{PDB3|2b12}}A:89-321
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| {{PDB3|1bep}} :89-321 {{PDB3|1bej}} :89-321 {{PDB3|1kok}}A:89-321
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| {{PDB3|2b11}}C:89-321 {{PDB3|1a2g}} :89-321 {{PDB3|2pcb}}C:89-321
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| {{PDB3|1ac8}} :89-321 {{PDB3|1ac4}} :89-321 {{PDB3|1ccp}} :89-321
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| {{PDB3|1stq}}A:89-321 {{PDB3|1ml2}}A:89-321 {{PDB3|1mkr}}A:89-321
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| {{PDB3|1cpg}} :89-321 {{PDB3|1mkq}}A:89-321 {{PDB3|1jdr}}A:89-321
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| {{PDB3|1kxm}}A:89-321 {{PDB3|1kxn}}A:89-321 {{PDB3|1cpd}} :89-321
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| {{PDB3|1a2f}} :89-321 {{PDB3|1cmq}} :89-321 {{PDB3|1dcc}} :89-321
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| {{PDB3|5ccp}} :89-321 {{PDB3|1ccb}} :89-321 {{PDB3|1bj9}} :89-321
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| {{PDB3|1aa4}} :89-321 {{PDB3|1dsg}}A:89-321 {{PDB3|1zbz}}A:89-321
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| {{PDB3|1aes}} :89-321 {{PDB3|4ccp}} :89-321 {{PDB3|1aen}} :89-321
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| {{PDB3|1cpe}} :89-321 {{PDB3|1aed}} :89-321 {{PDB3|1mk8}}A:89-321
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| {{PDB3|1bes}} :89-321 {{PDB3|1dsp}}A:89-321 {{PDB3|1aee}} :89-321
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| {{PDB3|2cyp}} :89-321 {{PDB3|1ebe}}A:89-321 {{PDB3|2ccp}} :89-321
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| {{PDB3|1jci}}A:89-321 {{PDB3|1ccl}} :89-321 {{PDB3|1zby}}A:89-321
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| {{PDB3|1ds4}}A:89-321 {{PDB3|1cce}} :89-321 {{PDB3|1krj}}A:89-321
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| {{PDB3|1sbm}}A:89-321 {{PDB3|1aeu}} :89-321 {{PDB3|1aeb}} :89-321
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| {{PDB3|1aek}} :89-321 {{PDB3|3ccx}} :89-321 {{PDB3|1ccc}} :89-321
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| {{PDB3|1sog}}A:89-321 {{PDB3|1aeo}} :89-321 {{PDB3|1bva}}A:89-321
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| {{PDB3|1cck}} :89-321 {{PDB3|1dso}}A:89-321 {{PDB3|1dse}}A:89-321
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| {{PDB3|1cci}} :89-321 {{PDB3|1ryc}} :89-321 {{PDB3|1cyf}} :89-321
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| {{PDB3|1bek}} :89-321 {{PDB3|1aeh}} :89-321 {{PDB3|1aev}} :89-321
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| {{PDB3|1ub2}}A:62-394 {{PDB3|2ccd}}A:76-400 {{PDB3|2cca}}A:76-400
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| {{PDB3|1sfz}}A:76-400 {{PDB3|1sj2}}A:76-400 {{PDB3|1mwv}}B:80-408
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| {{PDB3|1x7u}}B:80-408 {{PDB3|1itk}}B:64-391 {{PDB3|1lga}}A:48-285
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| {{PDB3|1llp}} :48-285 {{PDB3|1b80}}A:48-285 {{PDB3|1b82}}B:48-285
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| {{PDB3|1b85}}B:48-285 {{PDB3|1qpa}}B:49-286 {{PDB3|2boq}}A:50-280
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| {{PDB3|1a20}} :50-280 {{PDB3|1qjr}}A:51-287 {{PDB3|1bqw}} :51-287
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| {{PDB3|1ary}} :49-285 {{PDB3|1arp}} :49-285 {{PDB3|1arv}} :49-285
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| {{PDB3|1aru}} :49-285 {{PDB3|1arx}} :49-285 {{PDB3|1arw}} :49-285
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| {{PDB3|1gza}} :49-285 {{PDB3|1ck6}}A:49-285 {{PDB3|1hsr}} :49-285
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| {{PDB3|1gzb}} :49-285 {{PDB3|1c8i}}A:49-285 {{PDB3|1lyc}}A:48-284
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| {{PDB3|1ly9}}A:48-284 {{PDB3|1lyk}}A:48-284 {{PDB3|1ly8}}B:48-284
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| {{PDB3|1h3j}}A:48-284 {{PDB3|1yzp}}A:41-282 {{PDB3|1yzr}}A:41-282
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| {{PDB3|1mn2}} :41-282 {{PDB3|1mnp}} :41-282 {{PDB3|1yyd}}A:41-282
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| {{PDB3|1mn1}} :41-282 {{PDB3|1yyg}}A:41-282 {{PDB3|1u2j}}A:422-726
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| {{PDB3|1u2l}}B:422-726 {{PDB3|1u2k}}A:422-726
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| }}
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| '''Haem peroxidases''' (or '''heme peroxidases''') are [[haem]]-containing enzymes that use [[hydrogen peroxide]] as the electron acceptor to catalyse a number of oxidative reactions. Most haem peroxidases follow the reaction scheme:
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| : Fe<sup>3+</sup> + H<sub>2</sub>O<sub>2</sub> <math>\rightleftharpoons</math> [Fe<sup>4+</sup>=O]R' (Compound I) + H<sub>2</sub>O
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| : [Fe<sup>4+</sup><math>\rightleftharpoons</math>O]R' + substrate --> [Fe<sup>4+</sup>=O]R (Compound II) + oxidised substrate | |
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| : [Fe<sup>4+</sup><math>\rightleftharpoons</math>O]R + substrate --> Fe<sup>3+</sup> + H<sub>2</sub>O + oxidised substrate
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| In this mechanism, the enzyme reacts with one equivalent of H<sub>2</sub>O<sub>2</sub> to give [Fe<sup>4+</sup>=O]R' (compound I). This is a two-electron oxidation/reduction reaction where H<sub>2</sub>O<sub>2</sub> is reduced to water and the enzyme is oxidised. One oxidising equivalent resides on iron, giving the oxyferryl<ref name="PUB00001259">{{cite journal |author=Nelson RE, Fessler LI, Takagi Y, Blumberg B, Keene DR, Olson PF, Parker CG, Fessler JH |title=Peroxidasin: a novel enzyme-matrix protein of Drosophila development |journal=EMBO J. |volume=13 |issue=15 |pages=3438–3447 |year=1994 |pmid=8062820 |pmc=395246}}</ref> intermediate, while in many peroxidases the porphyrin (R) is oxidised to the porphyrin pi-cation radical (R'). Compound I then oxidises an organic substrate to give a substrate radical.<ref name="PUB00005246">{{cite journal |author=Poulos TL, Li H |title=Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures |journal=Structure |volume=2 |issue=6 |pages=461–464 |year=1994 |pmid=7922023 |doi=10.1016/S0969-2126(00)00046-0}}</ref>
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| Haem peroxidases include two superfamilies: one found in bacteria, fungi, plants and [[Animal heme-dependent peroxidases|the second found in animals]]. The first one can be viewed as consisting of 3 major classes.<ref name="PUB00001075">{{cite journal |author=Welinder KG |title=Superfamily of plant, fungal and bacterial peroxidases |journal=Curr. Opin. Struct. Biol. |volume=2 |issue= 3| doi=10.1016/0959-440X(92)90230-5 |pages=388–393 |year=1992}}</ref> Class I, the intracellular peroxidases, 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 (AP), the main enzyme responsible for hydrogen peroxide removal in chloroplasts and cytosol of higher 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 stress.<ref name="PUB00000617">{{cite journal |author=Welinder KG |title=Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily |journal=Biochim. Biophys. Acta |volume=1080 |issue=3 |pages=215–220 |year=1991 |pmid=1954228}}</ref>
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| Class II consists of secretory fungal peroxidases: ligninases, or lignin peroxidases (LiPs), and manganese-dependent peroxidases (MnPs). These are monomeric glycoproteins involved in the degradation of lignin. In MnP, Mn<sup>2+</sup> serves as the reducing substrate.<ref name="PUB00001743">{{cite journal |author=Reddy CA, D Souza TM |title=Physiology and molecular biology of the lignin peroxidases of Phanerochaete chrysosporium |journal=FEMS Microbiol. Rev. |volume=13 |issue=2 |pages=137–152 |year=1994 |pmid=8167033}}</ref> Class II proteins contain four conserved disulphide bridges and two conserved calcium-binding sites.
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| Class III consists of the secretory plant peroxidases, which have multiple tissue-specific functions: e.g., removal of hydrogen peroxide from chloroplasts and cytosol; oxidation of toxic compounds; biosynthesis of the cell wall; defence responses towards wounding; indole-3-acetic acid (IAA) catabolism; ethylene biosynthesis; and so on.<ref name="PUB00005929">{{cite journal |author=Campa A |title=Biological roles of plant peroxidases: known and potential function |journal= |volume=2 |issue= |pages=25–50 |year=1991}}</ref> Class III proteins are also monomeric glycoproteins, containing four conserved disulphide bridges and two calcium ions, although the placement of the disulphides differs from class II enzymes.
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| The crystal structures of a number of these proteins show that they share the same architecture - two all-alpha domains between which the haem group is embedded.
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| Another family of haem peroxidases is the [[DyP-type peroxidase family]].<ref name="pmid17654545">{{cite journal | author = Zubieta C, Krishna SS, Kapoor M, Kozbial P, McMullan D, Axelrod HL, Miller MD, Abdubek P, Ambing E, Astakhova T, Carlton D, Chiu HJ, Clayton T, Deller MC, Duan L, Elsliger MA, Feuerhelm J, Grzechnik SK, Hale J, Hampton E, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kumar A, Marciano D, Morse AT, Nigoghossian E, Okach L, Oommachen S, Reyes R, Rife CL, Schimmel P, van den Bedem H, Weekes D, White A, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA | title = Crystal structures of two novel dye-decolorizing peroxidases reveal a beta-barrel fold with a conserved heme-binding motif | journal = Proteins | volume = 69 | issue = 2 | pages = 223–33 |date=November 2007 | pmid = 17654545 | doi = 10.1002/prot.21550 | url = }}</ref>
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| ==References==
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| {{reflist}}
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| {{InterPro content|IPR002016}}
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| {{DEFAULTSORT:Haem Peroxidase}}
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| [[Category:Protein domains]]
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| [[Category:EC 1.11.1|*]]
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| [[Category:Hemoproteins]]
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