View source for 2wd4

==ASCORBATE PEROXIDASE AS A HEME OXYGENASE: W41A VARIANT PRODUCT WITH T-BUTYL PEROXIDE==
<StructureSection load='2wd4' size='340' side='right' caption='[[2wd4]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wd4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WD4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WD4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TBV:3-[2-[[3-(2-CARBOXYETHYL)-5-[[3-ETHENYL-4-METHYL-5-[(2-METHYLPROPAN-2-YL)OXY]-1H-PYRROL-2-YL]METHYL]-4-METHYL-1H-PYRROL-2-YL]METHYL]-5-[(Z)-(4-ETHENYL-3-METHYL-5-OXO-PYRROL-2-YLIDENE)METHYL]-4-METHYL-1H-PYRROL-3-YL]PROPANOIC+ACID'>TBV</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cl4|2cl4]], [[2ghe|2ghe]], [[2vnx|2vnx]], [[2ggn|2ggn]], [[2ghd|2ghd]], [[1oag|1oag]], [[2vcn|2vcn]], [[2ghc|2ghc]], [[1oaf|1oaf]], [[2vnz|2vnz]], [[2vcf|2vcf]], [[2vo2|2vo2]], [[2vcs|2vcs]], [[2ghh|2ghh]], [[2ghk|2ghk]], [[1v0h|1v0h]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-ascorbate_peroxidase L-ascorbate peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.11 1.11.1.11] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wd4 OCA], [http://pdbe.org/2wd4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wd4 RCSB], [http://www.ebi.ac.uk/pdbsum/2wd4 PDBsum]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wd/2wd4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2wd4 ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
The heme peroxidases and heme oxygenase enzymes share a common heme prosthetic group but catalyse fundamentally different reactions, the first being H2O2-dependent oxidation of substrate using an oxidised Compound I intermediate, the second O2-dependent degradation of heme. It has been proposed that these enzymes utilise a common reaction intermediate, a ferric hydroperoxide species, that sits at a crossroads in the mechanism and beyond which there are two mutually exclusive mechanistic pathways. Here, we present evidence to support this proposal in a heme peroxidase. Hence, we describe kinetic data for a variant of ascorbate peroxidase (W41A) which reacts slowly with t-butylhydroperoxide and does not form the usual peroxidase Compound I intermediate; instead, structural data show that a product is formed in which the heme has been cleaved at the alpha-meso position, analogous to the heme oxygenase mechanism. We interpret this to mean that the Compound I (peroxidase) pathway is shut down, so that instead the reaction intermediate diverts through the alternative (heme oxygenase) route. A mechanism for formation of the product is proposed and discussed in the light of what is known about the heme oxygenase reaction mechanism.

Evidence for Heme Oxygenase Activity in a Heme Peroxidase.,Raven E, Badyal S, Eaton G, Mistry S, Pipirou Z, Basran J, Metcalfe C, Gumiero A, Handa S, Moody P Biochemistry. 2009 Mar 23. PMID:19309109<ref>PMID:19309109</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2wd4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ascorbate peroxidase|Ascorbate peroxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Glycine hispida]]
[[Category: L-ascorbate peroxidase]]
[[Category: Badyal, S K]]
[[Category: Gumiero, A]]
[[Category: Metcalfe, C L]]
[[Category: Moody, P C.E]]
[[Category: Raven, E L]]
[[Category: Heme peroxidase]]
[[Category: Oxidoreductase]]
[[Category: Peroxide scavenge]]
[[Category: Tert-butyl peroxide]]