{"id":1431,"date":"2018-01-25T09:00:56","date_gmt":"2018-01-25T08:00:56","guid":{"rendered":"http:\/\/ibb.uab.cat\/?p=1431"},"modified":"2018-01-25T09:07:23","modified_gmt":"2018-01-25T08:07:23","slug":"dr-david-reverter-structural-mechanism-for-the-temperature-dependent-activation-of-the-hyperthermophilic-pf2001-esterase","status":"publish","type":"post","link":"https:\/\/ibb.uab.cat\/index.php\/2018\/01\/25\/dr-david-reverter-structural-mechanism-for-the-temperature-dependent-activation-of-the-hyperthermophilic-pf2001-esterase\/","title":{"rendered":"Dr. David Reverter: Structural Mechanism for the Temperature-Dependent Activation of the Hyperthermophilic Pf2001 Esterase"},"content":{"rendered":"<h2><span style=\"font-size: 12pt;\"><a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0969212617304033?via%3Dihub\"><img loading=\"lazy\" class=\"alignleft wp-image-1432\" src=\"http:\/\/ibb.uab.cat\/wp-content\/uploads\/25-1-2018.jpg\" alt=\"\" width=\"298\" height=\"298\" \/><\/a><a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0969212617304033?via%3Dihub\">https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0969212617304033?via%3Dihub<\/a><\/span><\/h2>\n<h2 class=\"section-title\">Summary<\/h2>\n<div id=\"abssec0010\">\n<p id=\"abspara0010\" style=\"text-align: justify;\"><a title=\"Learn more about Lipase\" href=\"https:\/\/www.sciencedirect.com\/topics\/biochemistry-genetics-and-molecular-biology\/lipase\">Lipases<\/a>\u00a0and\u00a0<a title=\"Learn more about Esterase\" href=\"https:\/\/www.sciencedirect.com\/topics\/biochemistry-genetics-and-molecular-biology\/esterase\">esterases<\/a>\u00a0constitute a group of enzymes\u00a0that catalyze the hydrolysis or synthesis of ester bonds. A major biotechnological interest corresponds to thermophilic esterases, due to their intrinsic stability at high temperatures. The Pf2001 esterase from\u00a0<em>Pyrococcus furiosus<\/em>\u00a0reaches its optimal activity between 70\u00b0C and 80\u00b0C. The crystal structure of the Pf2001 esterase shows two different conformations: monomer and dimer. The structures reveal important rearrangements in the \u201ccap\u201d subdomain between monomer and dimer, by the formation of an extensive intertwined helical interface. Moreover, the dimer interface is essential for the formation of the hydrophobic channel for substrate selectivity, as confirmed by\u00a0<a title=\"Learn more about Mutagenesis\" href=\"https:\/\/www.sciencedirect.com\/topics\/biochemistry-genetics-and-molecular-biology\/mutagenesis\">mutagenesis<\/a>\u00a0and kinetic analysis. We also provide evidence for dimer formation at high temperatures, a process that correlates with its enzymatic activation. Thus, we propose a temperature-dependent activation mechanism of the Pf2001 esterase via dimerization that is necessary for the substrate channel formation in the\u00a0<a title=\"Learn more about Active site\" href=\"https:\/\/www.sciencedirect.com\/topics\/biochemistry-genetics-and-molecular-biology\/active-site\">active-site<\/a>\u00a0cleft.<\/p>\n<\/div>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n","protected":false},"excerpt":{"rendered":"<p>https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0969212617304033?via%3Dihub Summary Lipases\u00a0and\u00a0esterases\u00a0constitute a group of enzymes\u00a0that catalyze the hydrolysis or synthesis of ester bonds. A major biotechnological interest corresponds to thermophilic esterases, due to their intrinsic stability at high temperatures. The Pf2001 esterase from\u00a0Pyrococcus furiosus\u00a0reaches its optimal activity between 70\u00b0C and 80\u00b0C. The crystal structure of the Pf2001 esterase shows two different conformations: monomer [&hellip;]<\/p>\n","protected":false},"author":65,"featured_media":1434,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":[],"categories":[4],"tags":[],"_links":{"self":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/1431"}],"collection":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/users\/65"}],"replies":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/comments?post=1431"}],"version-history":[{"count":2,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/1431\/revisions"}],"predecessor-version":[{"id":1435,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/posts\/1431\/revisions\/1435"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/media\/1434"}],"wp:attachment":[{"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/media?parent=1431"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/categories?post=1431"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/ibb.uab.cat\/index.php\/wp-json\/wp\/v2\/tags?post=1431"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}