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<wx:section level="1" title="Sulfiredossina" id="wxsec1"><h1 class="pagetitle" id="wx1">Sulfiredossina</h1>

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<p id="wx6"> Questa voce di <a href="/wit/Enzimi" title="Enzimi" wx:linktype="known" wx:pagename="Enzimi" wx:page_id="1740" id="wx7">enzimi</a> è solo un <a href="/wit/Aiuto:Abbozzo" title="Aiuto:Abbozzo" wx:linktype="known" wx:pagename="Aiuto:Abbozzo" id="wx8">abbozzo</a>: <b id="wx9"><a href="http://wit/wit/index.php?title=Sulfiredossina&amp;action=edit" class="external text" wx:linktype="external" rel="nofollow" id="wx10">contribuisci</a></b> a migliorarla secondo le <a href="/wit/Aiuto:Manuale_di_stile" title="Aiuto:Manuale di stile" wx:linktype="known" wx:pagename="Aiuto:Manuale_di_stile" id="wx11">convenzioni di Wikipedia</a>.</p>
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<div style="-moz-border-radius-topleft:.9em; background:#C2C3FF; border:1px solid #88A; width:100%; text-align:center; margin-bottom:.5em;" id="wx13"><b id="wx14">sulfiredossina</b></div>

<div class="wx_image" wx:align="center" id="wx15"><a href="/wit/Immagine:Noenzyimage.png" title="" wx:linktype="image" wx:pagename="Immagine:Noenzyimage.png" wx:page_id="1836985" id="wx16"><img src="/wit/Immagine:Noenzyimage.png" alt="" width="150" id="wx17"/></a></div>

<div style="background:#E2F3EF; border-top:2px solid #C2C3FF" id="wx18"><b id="wx19">Altri nomi</b></div>

<p id="wx20">Srx1; sulfiredossina; perossiredossina-(<i id="wx21">S</i>-idrossi-<i id="wx22">S</i>-ossocisteina) reduttasi</p>

<div style="background:#E2F3EF; border-top:2px solid #C2C3FF" id="wx23"><b id="wx24">Banche dati</b></div>

<p id="wx25"><a href="http://brenda.bc.uni-koeln.de/php/result_flat.php4?ecno=1.8.98.2" class="external text" wx:linktype="external" rel="nofollow" id="wx26">BRENDA</a> <a href="http://www.expasy.ch/cgi-bin/nicezyme.pl?1.8.98.2" class="external text" wx:linktype="external" rel="nofollow" id="wx27">EXPASY</a> <a href="http://xpdb.nist.gov/enzyme_thermodynamics/enzyme_compose_query.pl?EC=1.8.98.2" class="external text" wx:linktype="external" rel="nofollow" id="wx28">GTD</a> <a href="http://www.genome.ad.jp/dbget-bin/www_bget?ec:1.8.98.2" class="external text" wx:linktype="external" rel="nofollow" id="wx29">KEGG</a> <a href="http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/enzymes/GetPage.pl?ec_number=1.8.98.2" class="external text" wx:linktype="external" rel="nofollow" id="wx30">PDB</a></p>

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<p id="wx39">La <b id="wx40">sulfiredossina</b> è un <a href="/wit/Enzima" title="Enzima" wx:linktype="known" wx:pagename="Enzima" wx:page_id="21081" id="wx41">enzima</a> appartenente alla classe delle <a href="/wit/Ossidoreduttasi" title="Ossidoreduttasi" wx:linktype="known" wx:pagename="Ossidoreduttasi" wx:page_id="416919" id="wx42">ossidoreduttasi</a>, che catalizza la seguente <a href="/wit/Reazione_chimica" title="Reazione chimica" wx:linktype="known" wx:pagename="Reazione_chimica" wx:page_id="51512" id="wx43">reazione</a>:</p>

<dl id="wx44">
<dd id="wx45"><a href="/wit/Perossiredossina" class="new" title="Perossiredossina" wx:linktype="unknown" wx:pagename="Perossiredossina" id="wx46">perossiredossina</a>
<p id="wx47">-(<i id="wx48">S</i>-idrossi-S-osso<a href="/wit/Cisteina" title="Cisteina" wx:linktype="known" wx:pagename="Cisteina" wx:page_id="50959" id="wx49">cisteina</a>) + <a href="/wit/ATP" title="ATP" wx:linktype="known" wx:pagename="ATP" wx:page_id="22914" id="wx50">ATP</a> + <b id="wx51">2</b> R-SH <wx:template id="wx_t3" pagename="Template:Unicode" page_id="87605"/><span class="Unicode" style="font-family: Code2000, TITUS Cyberbit Basic, Doulos SIL, Chrysanthi Unicode, Arial Unicode MS, Bitstream Cyberbit, Bitstream Vera, Gentium, GentiumAlt, Lucida Sans Unicode; font-family  :inherit;" id="wx52">⇄</span><wx:templateend start="wx_t3"/> perossiredossina-(<i id="wx53">S</i>-idrossicisteina) + ADP + <a href="/wit/Fosfato" title="Fosfato" wx:linktype="known" wx:pagename="Fosfato" wx:page_id="208036" id="wx54">fosfato</a> + R-S-S-R</p>
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<p id="wx55">Nel corso della <a href="/wit/Reazione_chimica" title="Reazione chimica" wx:linktype="known" wx:pagename="Reazione_chimica" wx:page_id="51512" id="wx56">reazione</a> della perossiredossina <wx:template id="wx_t4" pagename="Template:Enzima" page_id="680819"/><i id="wx57"><a href="/wit/Classificazione_EC" title="Classificazione EC" wx:linktype="known" wx:pagename="Classificazione_EC" wx:page_id="419349" id="wx58">numero EC</a> <a href="http://www.enzyme-database.org/query.php?ec=1.11.1.15*" class="external text" wx:linktype="external" rel="nofollow" id="wx59">1.11.1.15</a></i><wx:templateend start="wx_t4"/>, il suo residuo di cisteina è ossidato ad <a href="/wit/Acido_sulfenico" class="new" title="Acido sulfenico" wx:linktype="unknown" wx:pagename="Acido_sulfenico" id="wx60">acido sulfenico</a>, <i id="wx61">S</i>-idrossicisteina, e poi di nuovo ridotto a cisteina. Occasionalmente, il residuo <i id="wx62">S</i>-idrossicisteina è ulteriormente ossidato ad <a href="/wit/Acido_sulfinico" class="new" title="Acido sulfinico" wx:linktype="unknown" wx:pagename="Acido_sulfinico" id="wx63">acido sulfinico</a>, <i id="wx64">S</i>-idrossi-<i id="wx65">S</i>-ossocisteina, inattivando l'enzima. La reduttasi fornisce un meccanismo per la rigenerazione della forma attiva della perossiredossina, come la forma perossiredossina-(<i id="wx66">S</i>-idrossicisteina). Apparentemente, la reduttasi prima catalizza la <a href="/wit/Fosforilazione" title="Fosforilazione" wx:linktype="known" wx:pagename="Fosforilazione" wx:page_id="484699" id="wx67">fosforilazione</a> del gruppo -S(O)-OH, per mezzo di ATP, per produrre -S(O)-<i id="wx68">O</i>-<i id="wx69">P</i>, che è attaccato dalla perossiredossina tramite il residuo di cisteina, formando un ponte -S(O)-<i id="wx70">S</i>- tra i due enzimi. Successivamente rompe questo legame, lasciando la perossiredossina come acido sulfenico e la reduttasi come <a href="/wit/Tiolo" title="Tiolo" wx:linktype="known" wx:pagename="Tiolo" wx:page_id="571737" id="wx71">tiolo</a>.</p>

<a id="Bibliografia" name="Bibliografia"/>
<wx:section level="2" title="Bibliografia" id="wxsec2"><h2 id="wx72">Bibliografia</h2>

<ul id="wx73">
<li id="wx74"><wx:template id="wx_t5" pagename="Template:Cita_pubblicazione" page_id="654720"/><cite style="font-style:normal" id="wx75">Woo, H.A., Jeong, W., Chang, T.S., Park, K.J., Park, S.J., Yang, J.S. and Rhee, S.G. (2005).  <i id="wx76">Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins</i> J. Biol. Chem. <b id="wx77">280</b>: 3125–3128. <a href="/wit/Entrez" title="Entrez" wx:linktype="known" wx:pagename="Entrez" wx:page_id="681159" id="wx78">Entrez PubMed</a> <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=pubmed&amp;dopt=Abstract&amp;list_uids=15590625" class="external text" wx:linktype="external" rel="nofollow" id="wx79">15590625</a>.</cite><wx:templateend start="wx_t5"/>
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<li id="wx80"><wx:template id="wx_t6" pagename="Template:Cita_pubblicazione" page_id="654720"/><cite style="font-style:normal" id="wx81">Chang, T.S., Jeong, W., Woo, H.A., Lee, S.M., Park, S. and Rhee, S.G. (2004).  <i id="wx82">Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine</i> J. Biol. Chem. <b id="wx83">279</b>: 50994–51001. <a href="/wit/Entrez" title="Entrez" wx:linktype="known" wx:pagename="Entrez" wx:page_id="681159" id="wx84">Entrez PubMed</a> <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=pubmed&amp;dopt=Abstract&amp;list_uids=15448164" class="external text" wx:linktype="external" rel="nofollow" id="wx85">15448164</a>.</cite><wx:templateend start="wx_t6"/>
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<li id="wx86"><wx:template id="wx_t7" pagename="Template:Cita_pubblicazione" page_id="654720"/><cite style="font-style:normal" id="wx87">Biteau, B., Labarre, J. and Toledano, M.B. (2003).  <i id="wx88">ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin</i> Nature <b id="wx89">425</b>: 980–984. <a href="/wit/Entrez" title="Entrez" wx:linktype="known" wx:pagename="Entrez" wx:page_id="681159" id="wx90">Entrez PubMed</a> <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=pubmed&amp;dopt=Abstract&amp;list_uids=14586471" class="external text" wx:linktype="external" rel="nofollow" id="wx91">14586471</a>.</cite><wx:templateend start="wx_t7"/>
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<div id="wx_categorylinks">
<a href="/wit/index.php?title=Speciale:Categories&amp;article=Sulfiredossina" title="Speciale:Categories" wx:linktype="known" wx:pagename="Speciale:Categories" id="wx92">Categorie</a>: <span dir="ltr" id="wx93"><a href="/wit/Categoria:Stub_enzimi" title="Categoria:Stub enzimi" wx:linktype="known" wx:pagename="Categoria:Stub_enzimi" wx:page_id="747485" id="wx94">Stub enzimi</a></span> | <span dir="ltr" id="wx95"><a href="/wit/Categoria:EC_1.8.98" title="Categoria:EC 1.8.98" wx:linktype="known" wx:pagename="Categoria:EC_1.8.98" wx:page_id="1545886" id="wx96">EC 1.8.98</a></span></div>
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<p id="wx97">enzimi</p>
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<p id="wx98">sulfiredossina</p>
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<p id="wx99">1.8.98.2</p>
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<p id="wx100">perossiredossina-(<i id="wx101">S</i>-idrossi-<i id="wx102">S</i>-ossocisteina):tiolo ossidoreduttasi [ATP-idrolizzante; perossiredossina-(<i id="wx103">S</i>-idrossicisteina)-formante]</p>
</wx:argument><wx:argument name="altri nomi">
<p id="wx104">Srx1; sulfiredossina; perossiredossina-(<i id="wx105">S</i>-idrossi-<i id="wx106">S</i>-ossocisteina) reduttasi</p>
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<p id="wx107">⇄</p>
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<p id="wx108">1.11.1.15</p>
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<p id="wx109">Woo, H.A., Jeong, W., Chang, T.S., Park, K.J., Park, S.J., Yang, J.S. and Rhee, S.G.</p>
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<p id="wx110">Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins</p>
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<p id="wx111">J. Biol. Chem.</p>
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<p id="wx113">2005</p>
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<a href="/wit/Entrez" title="Entrez" wx:linktype="known" wx:pagename="Entrez" wx:page_id="681159" id="wx115">Entrez PubMed</a> <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=pubmed&amp;dopt=Abstract&amp;list_uids=15590625" class="external text" wx:linktype="external" rel="nofollow" id="wx116">15590625</a>
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<p id="wx117">Chang, T.S., Jeong, W., Woo, H.A., Lee, S.M., Park, S. and Rhee, S.G.</p>
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<p id="wx118">Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine</p>
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<p id="wx119">J. Biol. Chem.</p>
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<p id="wx128">425</p>
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