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Molecular simulations reveal how an enzyme’s shape guides molecular recognition

Researchers from Shibaura Institute of Technology used molecular simulations to investigate how an enzyme's shape affects molecular recognition and ligand retention. They found that enzyme shape influences ligand retention, with 75.6% of trajectories in the closed group retaining ligands compared to 55.1% in the open group.

SourceShibaura Institute of Technology·JournalACS Omega·TypeComputational simulation/modeling·DateSep 29, 2026

New AI method revolutionizes the design of enzymes

Researchers have developed a new AI method called Riff-Diff to construct artificial biocatalysts, resulting in enzymes that are significantly faster, more stable and versatile. The technology allows for precise design of protein structures around active centres, making enzyme design more accessible to the wider biotechnology community.

SourceGraz University of Technology·JournalNature·TypeComputational simulation/modeling·DateJan 22, 2026

Finding the enzymatic needle in the database haystack

A Kobe University team developed a technique to classify thousands of enzymes, allowing for rapid evaluation and identification of highly active and versatile enzymes. The approach enabled the discovery of an enzyme with up to 10 times higher productivity than industry standards.

SourceKobe University·JournalACS Catalysis·TypeExperimental study·DateJun 26, 2025

Enzymes from scratch

Scientists at UC Santa Barbara and UCSF have developed a new method to design enzymes from scratch, enabling the creation of highly efficient and selective catalysts. The new approach allows for the combination of desirable properties into novel enzymes for various applications, including drug development and materials design.

An enzyme in training camp

Researchers at Max Planck Institute developed a new, efficient metabolic pathway to convert acetyl-CoA into pyruvate, enabling effective CO2 utilization. The 'lactyl-CoA mutase' enzyme can produce valuable products like 3-hydroxypropionate for sustainable plastics.

SourceMax-Planck-Gesellschaft·JournalNature Communications·TypeExperimental study·DateNov 29, 2024

Through the looking glass: A cross-chiral reaction challenges our definition of life

Researchers demonstrate the first cross-chiral exponential amplification of an RNA enzyme, potentially leading to the development of cross-chiral therapeutics and biotechnologies. The discovery suggests that a bioengineer can create a new form of biochemical evolution by using both left- and right-handed molecules.

SourceSalk Institute·JournalProceedings of the National Academy of Sciences·TypeExperimental study·DateOct 22, 2024

Reprogramming wood-degrading mushroom enzymes for the biorecycling of plastic

Researchers successfully designed and engineered novel enzyme systems that can degrade various types of plastics. By replacing the binding module with different modules, they created chimera LPMOs capable of recognizing and breaking down different types of plastics, including biosourced polyhydroxyalkanoate.

New additive process can make better — and greener — high-value chemicals

Researchers at the University of Illinois developed an eco-friendly method to precisely mix fluorine into olefins using natural enzymes and light, offering a more efficient strategy for creating high-value chemicals with potential applications in agriculture, pharmaceuticals, renewable fuels and more.

Synthetic droplets cause a stir in the primordial soup

Scientists from OIST created synthetic droplets to mimic biological processes, finding that pH gradients facilitate Marangoni effect and enabling droplets to detect and migrate towards each other. This study sheds light on the movement of simplest forms of life in primordial soup billions of years ago.

SourceOkinawa Institute of Science and Technology (OIST) Graduate University·JournalJournal of the American Chemical Society·TypeExperimental study·DateApr 25, 2024

Team creates synthetic enzymes to unravel molecular mysteries

A team of researchers developed synthetic enzymes that can control the behavior of the signaling protein Vg1, which plays a key role in vertebrate embryonic development. The study uses zebrafish to investigate how Vg1 is formed and found that it must undergo additional processing before it can be activated.

SourceUniversity of Texas at Dallas·JournalProceedings of the National Academy of Sciences·TypeExperimental study·DateNov 9, 2023

BSC scientists create artificial protein capable of degrading microplastics in bottles

Researchers from BSC and CSIC have developed an artificial protein capable of degrading PET micro- and nanoplastics with efficiency between 5 and 10 times higher than current PETases. The protein can be used as filters to purify or recycle plastics, offering a potential solution to environmental pollution.

SourceBarcelona Supercomputing Center·JournalNature Catalysis·TypeComputational simulation/modeling·DateOct 23, 2023

Evolutionary history of detoxifying enzymes reconstructed

Scientists have reconstructed the evolutionary history of flavin-containing monooxygenases (FMOs), a class of detoxifying enzymes present in all lifeforms. The study reveals that a single ancestral gene diverged into two distinct functions, with one gene triggering a different breakdown reaction.

SourceUniversity of Groningen·JournalNature Communications·TypeComputational simulation/modeling·DateFeb 27, 2023

Artificial intelligence conjures proteins that speed up chemical reactions

Researchers used machine-learning algorithms to design new light-emitting enzymes called luciferases that can efficiently recognize specific chemicals and emit light. This breakthrough could lead to custom enzymes for a wide range of applications in biotechnology, medicine, environmental remediation, and manufacturing.

SourceUniversity of Washington School of Medicine/UW Medicine·JournalNature·TypeComputational simulation/modeling·DateFeb 22, 2023

Protecting biocatalysts from oxygen

Researchers discovered a new enzyme with molecular protection against oxygen, increasing its resistance by genetic modification. This breakthrough aims to improve protein dynamics and control inorganic centre reactivity for carbon-neutral hydrogen production.

SourceRuhr-University Bochum·JournalACS Catalysis·TypeExperimental study·DateJan 11, 2023

Experimental drug to treat liver cancer shows evidence of activity with manageable side effects

A new experimental drug has shown promising results in treating liver cancer, with two patients experiencing a partial response to the treatment. The drug, NMS-01940153E, targets an enzyme that plays a critical role in cell division and growth, and its side effects are manageable.

SourceEuropean Organisation for Research and Treatment of Cancer·TypeRandomized controlled/clinical trial·DateOct 27, 2022

Process to customize molecules does double duty

Researchers at Rice University have developed a chemical process that can add two distinct functional groups to single alkenes, a breakthrough in drug design and materials science. The process uses manganese catalysts and photocalysts to enable radical ligand transfer, allowing for the creation of unique molecules.

SourceRice University·JournalJournal of the American Chemical Society·TypeExperimental study·DateJun 22, 2022

Optimized binding cavity

Researchers developed a designer enzyme with an unnatural aniline side chain, increasing its activity by a factor of 90. Directed evolution led to variants with higher conversion rates, showing the potential for this method in producing highly effective enzymes.

SourceWiley·JournalAngewandte Chemie International Edition·DateFeb 1, 2019

The enzyme designers

The study reveals that a slight change in the substrate can practically stop an enzyme reaction. Computational design of a new variant was successfully produced and tested, demonstrating the method's accuracy and potential for future research.

SourceTechnical University of Munich (TUM)·JournalNature Communications·DateApr 17, 2018

Catalyst mystery unlocked

A team of researchers has developed a computational model that challenges entrenched ideas about enzyme catalysis, proposing a method for designing custom-designed enzymes. The 'lock and key' model is replaced by an electrical attraction theory, suggesting a perfect physical fit between catalyst and substrate is not necessary.

SourceUniversity of Southern California·JournalProceedings of the National Academy of Sciences·DateAug 18, 2008

Birth of an enzyme

Researchers designed an enzyme for a specific reaction using computational design, but the synthetic enzyme was less efficient than naturally occurring ones. However, by allowing the enzyme to undergo 'evolution in a test tube,' they were able to improve its efficiency 200-fold and increase reaction rates by a million-fold.