Aconitase: Diferenzas entre revisións

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{{entradución}}
{{encima
| Name = aconitatoAconitato hidratase
| EC_number = 4.2.1.3
| CAS_number = 9024-25-3
Liña 34:
 
== Función ==
InA contrastdiferenza withda themaioría majority ofdas [[ironproteína ferro-sulfursulfurada|proteínas proteinferro-sulfuradas]]s thatque functionfuncionan ascomo electrontransportadores carriersde electróns, theo [[iron-sulfur cluster de ferro-xofre]] ofda aconitase reactsreacciona directlydirectamente withco an[[substrato enzymeencimático|substrato]] substratedo encima. AconitaseA hasaconitase anten activeun ''cluster'' [Fe<sub>4</sub>S<sub>4</sub>]<sup>2+</sup> clusteractivo, whichque mayse convertpode toconverter aná inactiveforma [Fe<sub>3</sub>S<sub>4</sub>]<sup>+</sup> forminactiva. ThreeHai tres residuos de [[cysteinecisteína]] (Cys) residuesque havefuncionan beencomo shown to be ligands[[ligando]]s ofdo thecentro [Fe<sub>4</sub>S<sub>4</sub>] centre. InNo theestado active stateactivo, theo labileión [[iron]]ferro ionlábil ofdo the''cluster'' [Fe<sub>4</sub>S<sub>4</sub>] clusternon isestá notcoordinado coordinatedpola bycisteína Cyssenón butpor bymoléculas waterde moleculesauga.
 
TheSon homólogos da aconitase a [[iron-responsiveproteína element-bindingde proteinunión ao elemento de resposta ao ferro]] (IRE-BP) ande a [[3-Isopropylmalateisopropilmalato dehydratasedeshidratase|3-isopropylmalateisopropilmalato dehydratasedeshidratase]] (α-isopropylmalateisopropilmalato isomerase; {{número EC number|:4.2.1.33}}), anque enzymeé catalysingun theencima secondque stepcataliza ino thesegundo biosynthesispaso ofda biosíntese de [[leucineleucina]],. areOs known[[IRE|elementos aconitaseregulatorios homologues.do Iron regulatory elementsferro]] (IREs) constituteconstitúen aunha familyfamilia ofde [[ARN]]s de 28-nucleotide [[nucleótido]]s, non-coding codificantes, stemcon estruturas de [[talo-loopbucle]] structuresque thatregulan regulateo ironalmacenameto storagede ferro, a síntese de grupos [[hemehemo]] synthesise anda ironcaptación uptakede ferro. TheyTamén participan alsona participateunión indo [[ribosomeARNm]] binding and control theao [[mRNAribosoma]] turnovere (degradation)no control da degradación do ARNm. TheUnha specificproteína regulatorreguladora proteinespecífica, thea [[IRE-BP]], bindsúnese toaos IREs[[IRE]]s intanto bothnas rexións 5' andcoma nas 3' regions, butpero only toao RNAARN inna theforma apo form, withoutsen the Fe-So ''cluster'' de ferro-xofre. ExpressionA ofexpresión da IRE-BP inen cultured[[cultivo cellscelular|células hasen revealedcultivo]] thatrevelou theque a proteinproteína functionsfunciona either as an active aconitase, when cells are iron-replete, or as an active RNA-binding protein, when cells are iron-depleted. Mutant IRE-BPs, in which any or all of the three Cys residues involved in Fe-S formation are replaced by [[serine]], have no aconitase activity, but retain RNA-binding properties.
 
Aconitase is inhibited by [[Fluoroacetic acid|fluoroacetate]], therefore fluoroacetate is poisonous. The iron sulfur cluster is highly sensitive to oxidation by [[superoxide]].<ref name="pmid11912933">{{cite journal |pages=9–23 |doi=10.1016/S0076-6879(02)49317-2 |chapter=Aconitase: Sensitive target and measure of superoxide |title=Superoxide Dismutase |series=Methods in Enzymology |year=2002 |last1=Gardner |first1=Paul R. |isbn=978-0-12-182252-1 |volume=349}}</ref>