Articles tagged with Enzymatic Reactions
Researchers at Okinawa Institute of Science and Technology (OIST) have developed a system to study cellular reactions in a way that more closely reflects how molecules behave in a living cell. By mixing a polymer with protein, they created membraneless droplets that can mimic the molecular properties of how molecules move in the cell.
Researchers at Berkeley Lab have successfully engineered microbes to produce novel chemicals and developed a new technique for studying enzyme reactions in real-time. This breakthrough could lead to the production of sustainable fuels, pharmaceuticals, and renewable plastics.
Researchers at IOCB Prague have created a glowing DNA enzyme called Supernova, which catalyzes a chemiluminescent reaction. This breakthrough uses artificial evolution to identify light-producing deoxyribozymes in a vast library of DNA molecules, opening up new possibilities for point-of-care assays and high-throughput screens.
Researchers at Arizona State University explore alternative approaches to catalysis, a chemical process crucial for industrial applications. The study aims to develop synthetic catalysts that can improve on nature's designs, leading to the production of carbon-neutral fuels.
Researchers at DTU Health Tech have invented a one-pot assay, NISDA, for rapid detection of SARS-CoV-2 RNA without the need for enzyme-based methods. The assay detects low concentrations of RNA in 30 minutes and has shown high accuracy and sensitivity.
Researchers successfully mimic nano spatial compartments to create artificial mitochondria, capable of supplying ATP or other useful molecules to cells in damaged or diseased tissues. The artificial organelles are generated from Exosome fusion and can function as energy reserves in the damaged tissues.
Researchers discovered a massive enzyme complex in methanogenic archaea that directly transfers electrons from electron bifurcation to CO2 reduction, increasing efficiency. This finding may lead to sustainable biotechnological development and reduce greenhouse gas emissions.
Researchers found that a protein activator clamps down the active center of GTPase Ran, allowing efficient hydrolysis. This discovery may lead to the development of cancer drugs blocking this process.
A new method has enabled scientists to study the natural structure of large enzymes, revealing that they function differently than previously thought. This discovery could help better understand certain diseases, including Alzheimer's and those caused by viruses, and potentially lead to new treatment options.
Scientists at the Swiss Nanoscience Institute create miniature polymeric reaction containers, mimicking cellular compartments to study enzymatic reactions. The 'cell on a chip' technology provides precise control over enzyme combinations and transport, facilitating research into metabolic diseases and drug reactions.
Scientists develop nanocapsules loaded with enzymes that can enter cells and integrate into their signaling processes, amplifying natural reactions. The combination of nano-capsules increases cellular reactivity by 8-fold.
The innate immune system interprets cytosolic DNA as a sign of intracellular pathogens. However, cGAS is found in the nucleus and prevents autoimmune reactions by binding to chromatin, not DNA. This interaction fails to activate the innate immune system.
Researchers discovered that small highly branched polymers can mimic modern biological protein enzyme function, potentially aiding in the origins of life. These simple catalytic structures may have played a key role in jumpstarting life on early Earth.
Researchers at Uppsala University have resurrected billions-year-old enzymes and repurposed them to catalyse new chemical reactions. The study develops sustainable solutions in biotechnology and chemically degrades environmental toxins.
Scientists at Illinois have identified a novel enzymatic reaction that uses repurposed enzymes to produce high-yields of valuable chiral carbonyl compounds. This eco-friendly process merges biocatalysis with photocatalysis, offering potential applications in pharmaceutical and bioenergy fields.
Cold-adapted enzymes from low-temperature organisms exhibit distinctive properties that enable them to function in freezing conditions. However, they often stop functioning at around room temperature, until they start melting. Researchers have now explained this phenomenon through extensive computer simulations.
Scientists have discovered an enzyme that becomes catalytically active when exposed to blue light, enabling a wide range of biotechnological applications. The enzyme, found in Pseudomonas aeruginosa, uses a flavin-NADH complex to facilitate a new monooxygenase reaction.
University of Groningen researchers used nanopore technology to observe a single enzyme in four different folded states, which play an active role in the reaction mechanism. The study's findings have significant implications for enzyme engineering and the development of inhibitors.
Scientists develop a mathematical model that describes the chemical reactions responsible for amyloid fibril formation, revealing catalytic sites at interfaces and implications for laboratory data interpretation. The model has a simpler mathematical form than previous models, making it more accessible for future studies.
University of Wisconsin-Madison chemists create a novel method for synthesizing large ring-shaped molecules, the backbone of many pharmaceuticals, using foldamers that mimic enzymes' ability to bring molecular ends together and form rings.
Associate Professor Selin Kara aims to develop a fully green and sustainable production process for chemicals using natural enzymatic reactions. She plans to use bio-catalysis and photobiocatalysis in miniaturized bioreactors to create high-value products with minimal environmental impact.
Researchers used quantum light to track enzyme reactions in real-time without disrupting enzymatic activity, providing a potential breakthrough for biomedical applications. The technique combines quantum physics and biology to improve sensitivity and resolution.
A new study on an enzyme crucial for photosynthesis has uncovered a structural understanding of how light activates chlorophyll synthesis. The researchers discovered how the enzyme captures light and channels it to drive a biological reaction, paving the way for bioengineering artificial light-activated enzymes.
A German-Australian team of researchers has successfully converted carbon dioxide into ethanol and propanol using metallic nanoparticles, also known as nanozymes. This breakthrough is based on the principle of enzyme cascade reactions, where complex molecules are produced from comparatively simple raw materials.
Fungi's genes encode enzymes that use simple building blocks to build complex molecules through a decade-long collaborative research effort, revealing a surprising Diels-Alder reaction. This discovery opens paths for improving chemical reactions and harnessing the enzyme to create new compounds with biological activities.
The INTERfaces project, funded by the EU's Horizon 2020 programme, aims to replicate natural bioprocesses for use in the chemical industry. Researchers will mimic nature's metabolism to produce pure and sustainable chemical products.
Researchers from the Salk Institute have discovered how a specific enzyme called chalcone isomerase enables plants to manufacture essential compounds, such as flavonoids, through a unique catalytic process. This knowledge could inform the development of new medicines and improved crops.
A Thai research team has created a novel approach for simultaneously detecting and detoxifying harmful phenol compounds in one step. The innovative technique leverages natural enzymatic reactions to convert toxic chemicals into luciferin, a bioluminescent compound produced by fireflies.
Researchers at EPFL have successfully synthesized a manganese-hydrogenase by incorporating a manganese complex into an iron-hydrogenase. The resulting semi-synthetic enzyme is active for the native reaction of iron-hydrogenase, marking a significant breakthrough in metalloenzyme design.
Researchers developed BridgIT, a tool that annotates proteins for 93% of enzymatic reactions, filling gaps in metabolic networks. The tool correctly predicts enzymes for 211 out of 234 non-orphan reactions and 334 out of 379 hypothetical reactions.
Researchers from NTU and SUTD report an asymmetric reaction using a cationic catalyst, converting racemic substrates to asymmetric products via an S_N2X mechanism. The study also reveals an uncommon chemical interaction, halogen bonding, present between the participating molecules.
Chemists at the University of Münster have developed a new synthesis method for producing fluorinated piperidines, a breakthrough that could lead to more efficient pharmaceutical production. The new method involves two consecutive steps in one vessel and uses easily accessible starting molecules.
The study investigated the effect of viscosity on enzymatic reactions in a simulated intracellular environment. Scientists found that sucrose limited enzyme mobility more efficiently than glycerol, affecting reaction rates and mechanisms. The approach to constructing metabolic chains inside luminescent bacteria cells was proposed.
A synthetic organelle created in a lab modelled membraneless organelles found to drive efficient sugar processing by balancing substrate and enzyme interactions. Researchers at Georgia Institute of Technology used this setup to explore cellular biochemistry, discovering unexpected nuances in organelle chemistry.
Researchers have developed a synthetic enzyme that reduces sulfite to sulfide, a notoriously complex multistep chemical reaction. The new enzyme's design focused on functionality rather than structure, accounting for previously thought secondary interactions that proved crucial to its activity.
Researchers at Technical University of Munich have developed an enzymatic process to produce methionine from gaseous CO2, replacing the current petrochemical-based method. The new process requires just two enzymes and has a yield of 40 percent, compared to photosynthesis which uses 14 enzymes with only a 20 percent yield.
Researchers created an artificial enzyme that catalyzes a Diels-Alder reaction on the surfaces of living human cells, achieving up to a 50% yield. This breakthrough could lead to the development of therapeutic drugs targeted to specific organs and cells, reducing side effects.
Researchers at Princeton University have found a way to make a naturally occurring enzyme take on a new role, enabling the catalysis of non-natural reactions. This breakthrough could lead to the development of new enzymatic reactions and potentially more cost-effective chemical catalysis.
Researchers have successfully used E.coli bacteria to oxidize C-H bonds in benzene to generate phenol by activating a genetically inserted cytochrome P450BM3 enzyme with a decoy molecule. This novel approach enables whole-cell biotransformation without harsh conditions or genetic modification.
Researchers at the University of Nottingham have created a self-sustaining circuit of reactions that produces chemicals more efficiently through a looped set of reactions using enzymes in flow. This method reduces environmental waste, is self-sustaining, and produces higher-quality end products.
University of Groningen biotechnologists successfully redesigned aspartase enzyme using computational method, producing kilograms of pure building blocks for pharmaceuticals and other bioactive compounds.
A University of British Columbia bioengineer has created platelets with extra powers to aid in the coagulation process, potentially rescuing blood from massive bleeding. The modified platelets showed improved clotting times and stronger clots in various blood samples.
A new study from the University of Bristol and the University of Waikato reveals how enzymes 'choreograph' their atomic movements to work optimally at specific temperatures. This finding provides insights into enzyme structure and function, which can inform the design of better biocatalysts for industrial processes.
Researchers developed an enzymatic cycling method using pyruvate kinase to quantify pyruvate and phosphoenolpyruvate. The method uses the reversibility of the reaction in the presence of ATP and IDP, with a limit of detection estimated at 12 nM PEP.
A team of scientists at Princeton University has successfully created a protein that can catalyze biological reactions, functioning as a genuine enzyme. The artificial protein, Syn-F4, was designed entirely from scratch and can sustain life in E. coli bacteria by replacing the natural enzyme Fes.
Researchers found that bacteria navigate randomly but are biased towards nutrient sources, unlike enzymes which move towards areas with less substrate. The study used super-resolution microscopy and discovered run-and-tumble dynamics in enzyme motion.
A newly developed technique has allowed researchers to study the reactions of hydrogenases, enzymes that catalyze hydrogen production from algae and bacteria. The study reveals that the iron atoms in these enzymes briefly form a hydride before releasing molecular hydrogen.
Researchers have developed enzymes that can perform complex chemical reactions with improved selectivity and efficiency. These catalysts show promise for building molecules with important biological activity and reducing waste in the process. The discovery opens up new practices for chemists to create more powerful tools.
Researchers report that sugar phosphorylation and uridine synthesis occur spontaneously in microdroplets without enzymes or ATP. This discovery suggests prebiotic formation of biologically relevant molecules could have occurred in these environments.
Researchers at DGIST have synthesized metal-reactive oxygen species that react with nitrile, a triple-bonded carbon and nitrogen compound. This discovery could lead to the development of anti-cancer prodrugs.
Scientists at the University of Basel created bio-catalytic capsules capable of producing glucose-6-phosphate, a key metabolite involved in carbohydrate degradation and energy storage. The nanocapsules, measuring less than 200 nanometers, can be taken up by cells and may pave the way for new disease treatments.
Scientists from the University of Freiburg successfully elucidated the three-dimensional structure of phytoene desaturase, a crucial enzyme in carotene production. This breakthrough offers insights into herbicide binding and reaction mechanisms, which may lead to new agents for crop protection and Golden Rice development.
A new SBOL repository has been created to optimize metabolic processes and facilitate design of useful synthetic biological systems. The repository contains thousands of chemical compounds, enzyme classes, and metabolic reactions from nearly 4000 organisms.
Scientists from the University of Wisconsin-Madison solved the structure of an enzyme that attacks toluene, a chemical derived from wood and oil. The study reveals a less reactive form of iron-oxygen intermediate that avoids side reactions, offering insights for synthetic chemists.
A light-sensing protein from a microbe has enabled new technologies for biomedical applications, including drug discovery and understanding human vision. The protein's dynamic structure is crucial for bacterial response to stimuli and also necessary for other proteins, such as rhodopsin pigment.
A team of researchers at UD has discovered a new function for an enzyme involved in bacterial metabolism. They found that the enzyme plays a major role when generating sugars from non-sugar substrates and facilitates 'back-flow' even when sugar is being consumed.
Princeton researchers have discovered a method to expand enzyme reactivity through light activation, allowing access to high selectivities. They successfully catalyzed non-natural reactions, including dehalogenation reactions, by irradiating enzymes with light.
Researchers at the Max-Planck-Institute developed a novel pathway for effective carbon fixation, using a new CO2-fixing enzyme nearly 20 times faster than nature's most prevalent enzyme. This breakthrough enables the efficient capture of CO2 and its conversion into valuable products.
Researchers from Ruhr-University Bochum have successfully combined enzyme and chemical catalysts using a gel matrix to overcome the challenge of different reaction conditions. This approach enables more efficient and cost-effective synthesis of polyphenols, with potential applications in cancer therapies.
Researchers at Berkeley Lab developed a hybrid enzyme capable of churning out 2,550 product molecules per hour, comparable to biological counterparts. The study represents a major advance for artificial metalloenzymes, which promise to open up a world of beneficial molecular products not currently possible with natural enzymes.