{"id":885,"date":"2026-07-27T09:50:00","date_gmt":"2026-07-27T00:50:00","guid":{"rendered":"https:\/\/onepress.co.kr\/index.php\/briefing\/2026-07-27-condenzymes-catalysis-en\/"},"modified":"2026-07-27T09:50:00","modified_gmt":"2026-07-27T00:50:00","slug":"2026-07-27-condenzymes-catalysis-en","status":"publish","type":"briefing","link":"https:\/\/onepress.co.kr\/index.php\/briefing\/2026-07-27-condenzymes-catalysis-en\/","title":{"rendered":"Liquid-like cell droplets became catalysts without enzymes"},"content":{"rendered":"<p><strong>2026-07-27 09:50 KST<\/strong><\/p>\n<p>A study showing that proteins without catalytic function can accelerate chemistry after condensing into liquid-like droplets has been published after peer review in Molecular Cell.<\/p>\n<p>The result suggests that membraneless biomolecular condensates can do more than gather molecules: the condensed state itself can become a catalyst the authors call a condenzyme.<\/p>\n<h2>What produced the reaction<\/h2>\n<p>The team built condensates from intrinsically disordered proteins with no fixed three-dimensional structure or enzyme active site. Electric fields at the interface and changes in water properties created a reaction environment that promoted hydrolysis of esters, ATP, nucleic-acid-like substrates and peptides.<\/p>\n<h2>Droplet composition determined function<\/h2>\n<p>Not every condensate acted as the same catalyst. Changing protein sequence and charge pattern altered interfacial fields, water activity and reaction rate. The researchers showed that sequence design could tune these electrochemical properties.<\/p>\n<figure class=\"wp-block-image size-full\"><img decoding=\"async\" src=\"https:\/\/onepress.co.kr\/wp-content\/uploads\/2026\/07\/condenzymes-catalysis-en.png\" alt=\"Produced molecular view of water and ATP-like molecules reacting at a biomolecular-condensate interface\" loading=\"lazy\" \/><figcaption class=\"op-briefing-image-caption\">Produced explanatory image: it visualizes catalysis at a condensate interface and is not an actual microscopy image.<\/figcaption><\/figure>\n<h2>Effects appeared in living bacteria<\/h2>\n<p>Synthetic condensates introduced into E. coli changed ATP and transcription patterns and activated gene circuits dependent on products made by condensate-catalyzed hydrolysis. This demonstrates that the chemistry can affect a living cellular system.<\/p>\n<h2>Human disease and treatment remain unknown<\/h2>\n<p>The core experiments use purified proteins and engineered bacteria. It is not yet known which reactions natural condensates such as nucleoli or stress granules control in human cells. Links to cancer or neurodegeneration are hypotheses for follow-up, not treatment results.<\/p>\n<h2>The precise scope of novelty<\/h2>\n<p>Preprint versions were public in 2024 and 2025. The new event is final peer-reviewed publication on July 24, 2026. The next test is direct causal measurement of reaction rates and functions in natural condensates.<\/p>\n<h2>Official Primary Sources<\/h2>\n<p><a href=\"https:\/\/engineering.washu.edu\/news\/2026\/Biomolecular-condensates-reveal-surprising-activity-as-catalysts.html\" target=\"_blank\" rel=\"noopener noreferrer\">Washington University: Molecular Cell publication and experiment summary<\/a><\/p>\n<p><a href=\"https:\/\/doi.org\/10.1016\/j.molcel.2026.07.008\" target=\"_blank\" rel=\"noopener noreferrer\">Molecular Cell: final peer-reviewed paper DOI<\/a><\/p>\n<p><a href=\"https:\/\/www.biorxiv.org\/content\/10.1101\/2024.07.06.602359v3\" target=\"_blank\" rel=\"noopener noreferrer\">bioRxiv: authors\u2019 detailed methods and experimental results<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Intrinsically disordered proteins with no catalytic active site promoted hydrolysis of ATP, nucleic-acid-like substrates and other molecules after forming liquid-like condensates. The peer-reviewed result is based mainly on purified proteins and synthetic bacterial systems.<\/p>\n","protected":false},"featured_media":0,"template":"","meta":[],"class_list":["post-885","briefing","type-briefing","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/onepress.co.kr\/index.php\/wp-json\/wp\/v2\/briefing\/885","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/onepress.co.kr\/index.php\/wp-json\/wp\/v2\/briefing"}],"about":[{"href":"https:\/\/onepress.co.kr\/index.php\/wp-json\/wp\/v2\/types\/briefing"}],"wp:attachment":[{"href":"https:\/\/onepress.co.kr\/index.php\/wp-json\/wp\/v2\/media?parent=885"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}