{"id":63411,"date":"2025-08-29T12:13:13","date_gmt":"2025-08-29T15:13:13","guid":{"rendered":"https:\/\/cnpem.br\/?p=63411"},"modified":"2025-09-01T13:22:12","modified_gmt":"2025-09-01T16:22:12","slug":"international-collaboration-reveals-a-new-role-for-water-in-enzymes-a-novel-water-mediated-catalytic-architecture-is-discovered-in-ce20-family-enzymes","status":"publish","type":"post","link":"https:\/\/cnpem.br\/en\/international-collaboration-reveals-a-new-role-for-water-in-enzymes-a-novel-water-mediated-catalytic-architecture-is-discovered-in-ce20-family-enzymes\/","title":{"rendered":"International collaboration reveals a new role for water in enzymes. A novel water-mediated catalytic architecture is discovered in CE20 family enzymes"},"content":{"rendered":"

Researchers from the Brazilian Center for Research in Energy and Materials (CNPEM) and the University of Greifswald (Germany) described an unprecedented architecture in the functioning of enzymes involved in the modification of complex sugars<\/p><\/blockquote>\n

\"\"

Active site of the studied enzyme, with catalytic residues in orange and the water molecule that completes it through hydrogen bonds (dashed) represented as a red sphere. Other amino acid residues that complete the interdomain interface and the active site are also represented in pink and light bl<\/p><\/div>\n

 <\/p>\n

The work was published on July 31, 2025 in the journal Nature Communications and expands fundamental knowledge about how enzymes act in the conversion of polysaccharides \u2014 an essential step for industrial processes ranging from food processing to biofuel production.<\/p>\n

What was discovered<\/strong><\/p>\n

The enzymes studied belong to the CE20 family, a group of biocatalysts that can remove small chemical parts (esters) attached to larger sugars. This modification alters the physical properties of these molecules and facilitates the access of other enzymes that will act on them in subsequent stages, making the degradation process more efficient.<\/p>\n

In general, this type of enzyme works thanks to a catalytic triad \u2014 three amino acids that work together to speed up the chemical reaction. But, when analyzing two CE20 enzymes, researchers found something surprising: one of the classic components was missing. In its place was a perfectly organized water molecule, which took on the role that would normally be played by an amino acid.<\/p>\n

This new architecture, named the \u201cwater-mediated catalytic triad\u201d, was confirmed in additional experiments, which showed that the water molecule is not just a solvent, but an active and indispensable element of the reaction.<\/p>\n

 <\/p>\n

\"\"

Crystallographic structure representation of the proteins elucidated in the study. The different domains are highlighted and identified in green, light blue, and dark blue. In pink, the new auxiliary domain described in this study. In orange, the catalytic residues..<\/p><\/div>\n

 <\/p>\n

Cutting-edge infrastructure in Brazil<\/strong><\/p>\n

The enzymes\u2019 detailed characterization was only possible thanks to different open research facilities at CNPEM:<\/p>\n

– the Manac\u00e1 beamline, at the Sirius\/LNLS particle accelerator, used to collect high-resolution X-ray diffraction data;<\/p>\n

– the Robolab, at the Brazilian Biosciences National Laboratory (LNBio), which automates molecular biology and crystallization experiments;<\/p>\n

– and the macromolecule biophysics platform at the Brazilian Biorenewables National Laboratory (LNBR), essential for functional studies of proteins.<\/p>\n

In Manac\u00e1, for example, the crystals were frozen in liquid nitrogen at 100 K (approximately -173 \u00b0C) and analyzed with the Pilatus 2M detector. Approximately 3,600 images were collected per crystal, with high precision, revealing the role of the water molecule in the active structure of the enzyme.<\/p>\n

Scientific and technological impact<\/p>\n

For biochemist Michael Lammers, from the University of Greifswald, the result significantly expands our understanding of enzyme catalysis:<\/p>\n

“Our results show that water is not just a solvent, but can actively participate in the reaction. It is a previously unknown mechanism that substantially expands our understanding of enzymes.\u201d<\/p>\n

In addition to fundamental relevance, the discovery could boost industrial applications by guiding the development of more efficient and sustainable biocatalysts, useful both for the production of second-generation biofuels and for the food and biotechnology industries.<\/p>\n

Pl\u00ednio Vieira, researcher from the Brazilian Biorenewables National Laboratory at CNPEM, adds that \u201cthe most striking thing about this work was realizing how the diversity of perspectives enriches science\u201d. \u201cThe exchange of perspectives and ways of thinking provided immense learning about how collaboration can accelerate discoveries and open up paths that, alone, we might not have noticed. It was precisely this exchange that led us to see beyond the obvious and understand that the enzyme acted in a different way, mediated by a water molecule. It’s a detail that changes the way we understand the common mechanism of this class of proteins\u201d, he says.<\/p>\n

Collaboration instead of competition<\/strong><\/p>\n

The study arose from a meeting between research groups from Germany and Brazil, who realized they were investigating similar questions. Instead of competing for publishing primacy, they decided to join forces. For Mario Murakami, director of the Brazilian Biorenewables National Laboratory (LNBR\/CNPEM) and leader of the work in Brazil, this is one of the great legacies of the project:<\/p>\n

“It’s impressive to see how a situation that could easily have generated competition ended up resulting in such a robust article. The willingness of Professor Uwe Bornscheuer and Michael Lammers to join forces, rather than prioritizing rapid publication, made all the difference. This<\/p>\n

open collaboration not only strengthened the scientific output, but also left a lasting example of what science can achieve when we choose to build together.\u201d<\/p>\n

Institutional support<\/strong><\/p>\n

The project was funded by the Deutsche Forschungsgemeinschaft (DFG \u2013 German Research Foundation), within the scope of the POMPU research unit, and the S\u00e3o Paulo Research Foundation (FAPESP) in Brazil. The research also connects to the recently approved Transregio\/CRC CONCENTRATE collaborative consortium.<\/p>\n

________________________________________________________________________ Read the article in Nature Communications<\/p>\n

 <\/p>\n

About LNBR<\/h2>

The Brazilian Biorenewables National Laboratory (LNBR) works to address scientific challenges that are strategic for Brazil in order to promote energy transition and develop a sustainable bioeconomy. Its interdisciplinary competencies in bioprospecting, synthetic biology, biocatalysis, bioprocesses and sustainability are integrated into the development of technologies founded on renewable sources, domestic production chains and Brazilian biodiversity. Its infrastructure on the cutting edge of multi-omics, synthetic biology, precision fermenting, and scaling-up of bioprocesses is open to the scientific community in order to strengthen the national bioeconomy ecosystem and partnerships with the productive sector. The biotechnology platforms developed by LNBR, which are made available for research and innovation, are intended to boost Brazil\u2019s autonomy and competitiveness in the production of biofuels, chemicals and materials. LNBR is part of the Brazilian Center for Research in Energy and Materials (CNPEM) in Campinas, S\u00e3o Paulo, a private, non-profit organization overseen by the Ministry of Science, Technology and Innovation (MCTI).<\/p>

https:\/\/lnbr.cnpem.br\/<\/a><\/p><\/div><\/span><\/p>\n

About CNPEM<\/h2>

The Brazilian Center for Research in Energy and Materials (CNPEM) is home to a state-of-the-art, multi-user and multidisciplinary scientific environment and works on different fronts within the Brazilian National System for Science, Technology and Innovation. A social organization overseen by the Ministry of Science, Technology and Innovation (MCTI), CNPEM is driven by research that impacts the areas of health, energy, renewable materials, and sustainability. It is responsible for Sirius, the largest assembly of scientific equipment constructed in the country, and is currently constructing Project Orion, a laboratory complex for advanced pathogen research. Highly specialized science and engineering teams, sophisticated infrastructure open to the scientific community, strategic lines of investigation, innovative projects involving the productive sector, and training for researchers and students are the pillars of this institution that is unique in Brazil and able to serve as a bridge between knowledge and innovation. CNPEM\u2019s research and development activities are carried out through its four National Laboratories: Synchrotron Light (LNLS), Biosciences (LNBio), Nanotechnology (LNNano), Biorenewables (LNBR), as well as its Technology Unit (DAT) and the Ilum School of Science \u2014 an undergraduate program in Science and Technology supported by the Ministry of Education (MEC).<\/p>

https:\/\/cnpem.br\/en\/<\/a><\/p><\/div><\/span><\/p>\n","protected":false},"excerpt":{"rendered":"

Researchers from the Brazilian Center for Research in Energy and Materials (CNPEM) and the University of Greifswald (Germany) described an unprecedented architecture in the functioning of enzymes involved in the…<\/p>\n","protected":false},"author":42,"featured_media":63414,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"_jetpack_newsletter_access":"","_jetpack_dont_email_post_to_subs":false,"_jetpack_newsletter_tier_id":0,"_jetpack_memberships_contains_paywalled_content":false,"_jetpack_memberships_contains_paid_content":false,"footnotes":"","_links_to":"","_links_to_target":""},"categories":[1458,1479,1461,1510],"tags":[],"class_list":["post-63411","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-releases-cnpem-en-2","category-releases-lnbr-en","category-noticia-home-en-en","category-noticia-home-en-en-2","category-1458","category-1479","category-1461","category-1510","description-off"],"acf":[],"yoast_head":"\nInternational collaboration reveals a new role for water in enzymes. 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