Tag: enzyme

X-Rays Shed Light on Possible New Treatments for TB

X-Rays Shed Light on Possible New Treatments for TB

SCIENTIFIC ACHIEVEMENT

X-ray diffraction data, collected at the Advanced Light Source (ALS) and other Department of Energy light sources, revealed the crystal structure of CMX410, a new compound that targets a key enzyme (Pks13) in the cell membrane of the bacterium responsible for tuberculosis (TB).

SIGNIFICANCE AND IMPACT

CMX410 is a promising new candidate to treat TB, including multidrug-resistant strains.

New treatments needed to tackle an old foe

TB is a deadly infectious disease caused by the bacterium Mycobacterium tuberculosis (Mtb). According to the World Health Organization, an estimated 10.8 million people contracted TB globally in 2023, and 1.25 million died from the disease. While antibiotics are effective for drug-sensitive TB cases, multidrug-resistant Mtb strains can evade common drug therapies.

Drug-resistant cases require a regimen that is often more expensive, toxic, and time-intensive. Patients are required to take six or more medications daily for up to 20 months. New approaches are urgently needed to shorten the course of drug interventions and address widespread multidrug-resistant strains.

A multi-institutional study led by researchers at Texas A&M University and the Calibr-Skaggs Institute for Innovative Medicine sought to find new treatments to address multidrug-resistant TB. The team screened a library of 406 compounds that belong to an active class of molecules [i.e., sulfur fluoride exchange (SuFEx)] to evaluate their efficacy against Mtb. The team developed one promising compound into CMX410, which targets Pks13, an enzyme essential for microbial cell wall biosynthesis.

Read more on the ALS website

Image: A cross-section of the crystal structure for the enzyme Pks13 (the surface colored pink and blue by hydrophobicity) as it interacts with CMX410 (shown as stick-like structure), a new drug candidate for TB

Credit: ALS

Dynamic protein nanotubes for advanced applications

Dynamic protein nanotubes for advanced applications

A collaborative research team from Jagiellonian University in Poland and the universities of Leeds, York, and Durham in the UK have made a significant nanotech breakthrough by developing dynamic, pentamer-based protein nanotubes. The study, published in ACS Nano, reveals how an engineered enzyme can assemble into various hollow spherical and cylindrical structures in response to stimuli.

By leveraging the power of electron microscopy and mathematical modeling, the research led by the Azuma group at Malopolska Centre of Biotechnology (MCB) JU has unlocked the ability of a modified enzyme, called lumazine synthase, to form versatile and adaptive nanostructures. The protein shows an extraordinary capacity to morph between hollow spherical shapes and elongated, fiber-like nanotubes, all in response to salt contents in solution. Unlike conventional nanotubes that rely on hexameric or other subunit arrangements, these newly discovered assemblies consist entirely of pentamers. 
Thanks to the state-of-the-art Titan Krios G3i cryo-electron microscope, housed at the National Synchrotron Radiation Centre SOLARIS JU and the Polish high-performance computing infrastructure PLGrid (HPC Centers: ACK Cyfronet AGH), scientists have mapped the structures of these innovative nanocage complexes with remarkable precision.

This pioneering research provides invaluable insights into the molecular mechanics and geometric principles of protein assembly. The findings offer a fresh blueprint for designing nanoarchitectures with customizable shapes and functions, potentially revolutionizing fields such as drug delivery, catalysis, and the creation of advanced nanomaterials.

This discovery is thrilling, as it allows us to see and comprehend the various ways pentamers bind within these nanocages – says Dr. Łukasz Koziej, a leading researcher of the study.
Dr. Yusuke Azuma adds, This work is a promising step forward to pave the way for developing new biomimetic devices and materials with bespoke properties, marking a significant advancement in the field of nanotechnology.

Read more on SOLARIS website


Image: Electron microscopic structures of ball- and tube-shaped assemblies made from an engineered enzyme, lumazine synthase. Unlike many other cases found before, these structures are built entirely with pentameric (pentagonal) units. By simply changing the amount of salt in the solution, they can switch between forming balls or tubes.

Enzyme discovered from Brazilian biodiversity can revolutionize bio-refineries

Enzyme discovered from Brazilian biodiversity can revolutionize bio-refineries

Unprecedented enzyme class prospected in Brazilian soil can increase biorefinery efficiency and accelerate the sustainable production of energy and chemicals

A new enzyme class discovered in Brazilian soil represents one of the main advances in recent decades in the field of sustainable production of energy and chemicals. This enzyme is capable of accelerating the cellulose breakdown, a critical process in the production of bioenergy and biochemicals. This discovery, published in the journal Nature, was led by researchers from CNPEM (Brazilian Center for Research in Energy and Materials, in Campinas) in a partnership with researchers from INRAE (French National Research Institute for Agriculture, Food and Environment, at Aix Marseille University) and Technical University of Denmark (DTU).

This enzyme was identified from the genetic material of a microbial community found in biomass residues collected in Brazilian soils. Its novel mechanism of action, combined with the ability to generate its own co-substrate, makes it a powerful tool for plant biomass deconstruction.

“This discovery changes the paradigm of cellulose degradation in nature and has the potential to revolutionize biorefineries”, says CNPEM researcher Mario Murakami, responsible for leading the studies. “With CelOCE, we can envision new routes for bioenergy, biochemicals and biomaterials production from plant biomass, contributing to a bio-based, low-carbon and circular economy.”

CelOCE (Cellulose Oxidative Cleaving Enzyme) improves efficiency in breaking down biomass into glucose, an essential step to convert this raw material into bioenergy and biochemicals. This research spanned from bioprospection in nature to an industrially relevant scale, with validation at the CNPEM pilot plant.

Data under industrial conditions have shown that, when used together with enzymes already used in the industry, CelOCE increased the amount of glucose released by up to 21% from agro-industrial residues. This means higher productivity and less waste in the industrial process.

According to ANP (Brazilian National Agency for Petroleum, Natural Gas and Biofuels) data, Brazil produced 43 billion ethanol liters in 2023. With this discovery, production can increase by billions of liters, using agro-industrial residues such as sugarcane bagasse, corn straw, wood and other crops, without needing to expand planting areas. However, the exact volume of this increase cannot yet be determined, as it depends on the amount of residues that will be used for ethanol production.

The research was carried out by a multidisciplinary team of scientists from CNPEM and international institutions from countries such as France and Denmark. According to CNPEM’s General Director, Antonio José Roque da Silva, the combination of advanced techniques available at the Center, including X-ray crystallography at Sirius, Brazil’s particle accelerator, and genetic engineering with CRISPR-Cas9, was essential to unravel  CelOCE’s unprecedented mechanism. “This work exemplifies the potential opened up by the integration and synergy between CNPEM’s different scientific competencies”, highlights the institution’s General Director.

Read more on CNPEM website

The World’s Most Efficient PET-Degrading Enzyme 

The World’s Most Efficient PET-Degrading Enzyme 

Polyethylene terephthalate (PET), which is used in drinking bottles, fibers, and many other applications, is one of a few plastics that can be broken down to its constituent monomers by naturally occurring enzymes. This study developed a landscape profiling method to identify and characterize the potential of microbial enzymes to degrade these plastics. Two enzymes were engineered with sequential mutagenesis and exhibited excellent performance relative to benchmarks, especially under the harsh conditions that are ideal for use in recycling applications..

Research Background and Objectives

PET (polyethylene terephthalate) is a representative general-purpose plastic widely used in various fields such as PET bottles, clothing, seat belts, takeout cups, and car mats. While most PET waste is separately collected and mechanically recycled into intermediate products, the recycled materials often degrade in quality, ultimately leading to incineration or landfill disposal. As a method to address this issue, chemical recycling technology has been developed to break down the PET polymer bonds using chemical catalysts and return them to the original raw materials. However, it has not been a perfect alternative due to the limitations of applying the method, which is caused by high temperature and high-pressure conditions. Therefore, the scientific community has turned to biological/biocatalytic recycling to solve these problems through enzymes. With complex bonding structures, enzymes react selectively with PET at low temperatures and in water solvent conditions to produce pure reactants. Thus, they are excellent at converting contaminated raw materials. There has been a fierce competition worldwide to develop PET-degrading enzymes using advanced technologies in various fields such as synthetic biology, computational chemistry, and AI-driven protein design. 

Research Approach

The research team attempted to experimentally determine the fitness landscape of various enzyme protein sequences. Since conducting experiments on all sequences was physically impossible, it was necessary to use a statistical sampling method through a landscape. To construct a landscape of the Polyesterase-Lipase-Cutinase Family, a neighborhood analysis module was devised to control the network’s rigidity using distance histogram data for each protein sequence. This analysis generated a two-dimensional semantic network. Based on this semantic network, the research team proposed an innovative approach to experimentally measure the fitness for PET degradation activity and thermal stability using hierarchization and cluster sampling. Also, to improve the selected enzymes, the team attempted a unique strategy of applying cross-template engineering to reflect natural diversity and fitness information in a rational design based on the protein’s 3D structural information. 

Results and Discussion

The new approach identified the most promising enzymes, Mipa-P and Kubu-P, among 158 nodes, which showed a superior PET-degradation rate and durability compared to other benchmarks. Cross-template engineering created heat-resistant variants MipaM19 (Mipa-PM19) and KubuM12 (Kubu-PM12) with melting temperatures exceeding 92 and 99°C, respectively. Surprisingly, Kubu-M12 withstood the condition of a minimum enzyme dosage of 0.58 g/mg and high PET loading of 20% and 30%, degrading more than 90% of the PET substrate within 8 hours. It showed overwhelming performance compared to other engineered benchmark enzymes. Moreover, Kubu-M12 withstood 99% ethylene glycol solvent and produced 30 mM level bis(2-hydroxyethyl) and terephthalic acid. For the first time in the world, the enzymatic catalytic glycolysis reaction was achieved at a significant level. 

Read more on PAL website

New enzyme-embedded plastic degrades rapidly

New enzyme-embedded plastic degrades rapidly

Scientists have developed a biosourced plastic embedded with an enzyme that ensures rapid biodegradation and compostability, overcoming the hurdles of currently used plastics. They used the ESRF to solve the structure of the enzyme. The results are published in Nature.

Plastic production reached a staggering 400 million tons in 2022, with packaging and single-use items making up a significant portion. The resulting waste often ends up in landfills, incinerators, or the environment, contributing to the growing crisis of plastic pollution.

Due to this situation, there is a burgeoning interest in biodegradable and compostable plastics as more sustainable alternatives. Polylactide (PLA) is the most widely used biosourced polymer, however, PLA degrades very slowly in home compost and soil.

Now scientists led by the company Carbios and the Toulouse Biotechnology Institute (TBI), in France, have developed a PLA-based plastic embedded with a specially optimized enzyme that ensures rapid biodegradation and compostability at room temperature through a scalable industrial process.

hey optimised the process used to achieve an engineered enzyme able to withstand the 170°C temperature required to introduce it in molten state PLA during the plastic production process. The new enzyme-embedded material, containing just 0.02% enzyme by weight, fully disintegrated under home compost conditions within 20–24 weeks, meeting all home composting standards. It also helped produce more biomethane, another source of waste recovery.

Part of this research required the structure determination of the enzyme, which the scientists acquired using the ESRF structural biology beamlines. This is the second Nature publication led by Carbios with data from the ESRF. Alain Marty, Chief Scientific Officer of Carbios, explains the long-term collaboration with the ESRF: “Since the early days of Carbios, TBI (Toulouse Biotechnology Institute), IPBS (The Institute of Pharmacology and Structural Biology) and Carbios have collaborated with the ESRF as synchrotron radiation plays an important role in this research. In particular, in this article diffraction data helped us unveil the structure of the enzyme to understand better the relation between the structure of the enzyme and its function. The resulting enzyme engineering work leads to an efficient enzyme that allows the plastic to self-biodegrade at room temperature.”

Read more on ESRF website

Image: The encapsulated enzyme CARBIOS Active, in granule form, when integrated directly into PLA-based packaging or products at the production phase, enables compostability at room temperature.

Credit: Carbios.

Towards prevention of diabetes linked substance produced by human gut microbiota 

Towards prevention of diabetes linked substance produced by human gut microbiota 

The team at the Novo Nordisk Foundation funded life science beamline MicroMAX welcomed the first users in December 2023. In the experiment the users investigated an enzyme that may be found in some bacteria of human gut microbiota and may have a role in the development of diabetes and other diseases.

An enzyme called urocanate reductase may be present in the bacteria that are found in the human gut. The enzyme breaks down urocanic acid, a natural constituent of skin and other tissues of the body, into the metabolite imidazole propionate. The metabolite has been linked to diabetes and other diseases.

The user team from Lund University used MicroMAX to investigate the molecular structure of the enzyme.

“A possible therapeutic strategy is to inhibit the enzyme and prevent the imidazole propionate production. The high-resolution atomic structure is needed to design inhibitor molecules that could occupy the active site of the enzyme,” says Raminta Venskutonyte, one of the researchers who conducted the study.

The experiment was conducted using X-ray diffraction at room temperature on a crystal prepared from a purified enzyme. One of the features of MicroMAX is that the experimental setup can handle even small amounts of samples, so-called microcrystals. It is important as it lets the researchers study samples that cannot be made to form large crystals and extend investigations into new areas.

“We aim to carry out time-resolved studies using microcrystals of urocanate reductase to further clarify its enzymatic mechanism. We are also looking forward to using MicroMAX in other projects involving medically interesting proteins, which only yield microcrystals,” concludes Raminta Venskutonyte.

Read more om the MAX IV website

Image: Raminta Venskutonyte in the experiment hutch at beamline MicroMAX

Stanford study shows how modifying enzymes’ electric fields boosts their speed

Stanford study shows how modifying enzymes’ electric fields boosts their speed

A seemingly subtle swap of metals—substituting a zinc ion with a cobalt ion—and a mutation ramps up the overall electric field strength at the active site of an enzyme, Stanford scientists find. The result is a predictably modified enzyme that works an astonishing 50 times faster than its unmodified analog.

Stanford researchers have demonstrated a way to dramatically speed up the reaction rate of an enzyme, a finding that could pave the way to designing ultra-fast synthetic enzymes for a range of industrial and medical uses.

Honed over billions of years of evolution, biological enzymes are marvels of chemistry. These specialized proteins serve as catalysts for accelerating chemical reactions essential to life as well as processes used in the food, pharmaceutical, and cosmetic industries.    

Ever since enzymes’ discovery nearly two centuries ago, scientists have sought ways to make them even faster. Most fabricated enzymes, though, have failed to match the lofty efficiency standards of nature-made varieties. And even where some successes have been realized through directed evolution, a protein engineering method that mirrors nature’s trial-and-error approach, these successes so far have been by chance, not because of a deeper understanding of how enzymes work or could be modified to work more swiftly.

Now, in a new study, researchers at Stanford’s School of Humanities and Sciences and SLAC National Accelerator Laboratory have debuted a modified enzyme that works an astonishing 50 times faster than its unmodified analog. The findings derive from pioneering research at the university regarding electric fields generated at “active sites,” the pocketlike places where revved up chemical reactions occur. Based on this concept, the researchers tweaked the chemistry of the active site, boosting its electric field strength and specificity to deliver the zippy results.  

Read more on Stanford University website

Image: X-ray crystallography was used to investigate and compare the 3D crystal structures of the unmodified enzyme containing an ion of zinc (Zn) (pictured left) and the modified enzyme with a cobalt (Co) ion in place of zinc (pictured right).

Undermining the foundations of bacterial resistance

Undermining the foundations of bacterial resistance

Scientists from the University of Guelph have used the Canadian Light Source (CLS) at the University of Saskatchewan to better understand how several infectious bacteria, including E. coli., build a protective sugar-based barrier that helps cloak their cells.

Published in the Journal of Biological Chemistry, the Guelph research provides the very early steps toward new treatments for E. coli and a whole range of bacteria. Their particular focus is on strains of E. coli that cause urinary tract and bloodstream infections, particularly those that are antibiotic resistant.

The research is looking to understand the enzyme that many infectious bacteria use to build the foundations of their protective capsule. The capsule helps shield the bacterium from attack by the human immune system and exists in many clinically distinct variants.

Making vaccines or drugs that targets the capsule itself directly is impractical as such treatments would target only a few bacteria. Instead, the Guelph team is focused on a key enzyme that builds the capsule foundation. This foundation could serve as a common point of attack, allowing a single treatment for several key pathogens infecting humans and livestock.

“We are interested in the machinery that builds the bacterium’s protective layer,” said Dr. Chris Whitfield, Professor Emeritus in the Department of Molecular and Cellular Biology. “By understanding and targeting the machinery, we can render the pathogen unable to survive in the host”.

Read more on the Canadian Light Source website

Image : Matthew Kimber, Chris Whitfield, and enzyme

Natural substances show promise against coronavirus


Natural substances show promise against coronavirus

X-ray screening identifies compounds blocking a major corona enzyme

Three natural compounds present in foods like green tea, olive oil and red wine are promising candidates for the development of drugs against the coronavirus. In a comprehensive screening of a large library of natural substances at DESY’s X-ray source PETRA III the compounds bound to a central enzyme vital for the replication of the coronavirus. All three compounds are already used as active substances in existing drugs, as the team headed by Christian Betzel from the University of Hamburg and Alke Meents from DESY reports in the journal Communications Biology. However, if and when a corona drug can be developed on the basis of these compounds remains to be investigated.

“We tested 500 substances from the Karachi Library of Natural Compounds if they bind to the papain-like protease of the novel coronavirus, which is one of the main targets for an antiviral drug,” explains the study’s main author Vasundara Srinivasan from the University of Hamburg. “A compound that binds to the enzyme at the right place can stop it from working.”

The papain-like protease (PLpro) is a vital enzyme for virus replication: When a cell is hijacked by the coronavirus, it is forced to produce building blocks for new virus particles. These proteins are manufactured as a long string. PLpro then acts like a molecular pair of scissors, cutting the proteins from the string. If this process is blocked, the proteins cannot assemble new virus particles.

Read more on the DESY website

Image: The paper’s main author Vasundara Srinivasan at an X-ray set-up to test protein crystals in the lab.

Credit: University of Hamburg, Susanna Gevorgyan

How a soil microbe could rev up artificial photosynthesis

How a soil microbe could rev up artificial photosynthesis

Researchers discover that a spot of molecular glue and a timely twist help a bacterial enzyme convert carbon dioxide into carbon compounds 20 times faster than plant enzymes do during photosynthesis. The results stand to accelerate progress toward converting carbon dioxide into a variety of products.

Plants rely on a process called carbon fixation – turning carbon dioxide from the air into carbon-rich biomolecules ­– for their very existence. That’s the whole point of photosynthesis, and a cornerstone of the vast interlocking system that cycles carbon through plants, animals, microbes and the atmosphere to sustain life on Earth. 

But the carbon fixing champs are not plants, but soil bacteria. Some bacterial enzymes carry out a key step in carbon fixation 20 times faster than plant enzymes do, and figuring out how they do this could help scientists develop forms of artificial photosynthesis to convert the greenhouse gas into fuels, fertilizers, antibiotics and other products.

Now a team of researchers from the Department of Energy’s SLAC National Accelerator Laboratory, Stanford University, Max Planck Institute for Terrestrial Microbiology in Germany, DOE’s Joint Genome Institute (JGI) and the University of Concepción in Chile has discovered how a bacterial enzyme – a molecular machine that facilitates chemical reactions – revs up to perform this feat.

Rather than grabbing carbon dioxide molecules and attaching them to biomolecules one at a time, they found, this enzyme consists of pairs of molecules that work in sync, like the hands of a juggler who simultaneously tosses and catches balls, to get the job done faster. One member of each enzyme pair opens wide to catch a set of reaction ingredients while the other closes over its captured ingredients and carries out the carbon-fixing reaction; then, they switch roles in a continual cycle.  

Read more on the SLAC website

Capybara gut holds valuable enzymes for biotechnology

Capybara gut holds valuable enzymes for biotechnology

Study elucidates unprecedented processes of herbivore metabolism involved in the efficient degradation of plant fibers

A group of researchers from the Brazilian Biorenewables National Laboratory (LNBR), Brazilian Center for Research in Energy and Materials (CNPEM), an organization supervised by the Brazilian Ministry of Science, Technology and Innovations (MCTI), has published in the journal Nature Communications a study that explores some of the most modern resources of current science to reveal unprecedented and valuable details of the capybara’s digestive process.

The capybara, the largest rodent on the planet, is known for its ability to degrade very efficiently the biomass it consumes, but the details of the animal’s microbiota metabolism that contribute to this characteristic have not yet been elucidated. Researcher Mario Murakami recalls that, in Brazil, this animal is used to eating sugarcane. “Since Brazilian biodiversity is an invaluable source of biotechnological solutions, our hypothesis was that the microorganisms inhabiting capybaras’ intestines have, throughout evolution, developed highly effective molecular strategies for the degradation and use of this biomass of great industrial and economic importance. And that was demonstrated in our study.”

“Population and molecular inventory” of the gut microbiome

The meticulous and unprecedented work started with a complete survey of the bacteria present in the capybara’s intestine, in addition to the expressed genes and metabolites produced from plant fibers. To understand the processes of depolymerization of lignocellulosic fibers and the efficient transformation of sugars into energy, a vast combination of techniques, methodologies and resources, including synchrotron light at the MX2 and SAXS1 beamlines of the Brazilian Synchrotron Light Laboratory (LNLS), was required, from the population scale of microorganisms to the atomic and molecular level of enzymes.

Read more the the LNLS website

Developing pain medication with fewer side effects

Developing pain medication with fewer side effects

Opiates like morphine and codeine provide many patients with relief: from the ache felt after mild surgery to chronic pain experienced by cancer patients. However, this type of medication can cause multiple side effects and can lead to physical dependency with long-term use. Improving pain medication would help millions of people to have a better quality of life.

Dr. Ken Ng, a professor at the University of Windsor and adjunct professor at the University of Calgary (UCalgary), and Sam Carr, a PhD student from UCalgary, have been working with Dr. Peter Facchini’s group at UCalgary to better understand how natural opiates are produced. The team has narrowed their focus on one enzyme in the last stage of opiate assembly, a process that occurs naturally in the poppy plant.

“Imagine this sort of like an assembly line,” Carr said. “There are a lot of different steps in this specific pathway, and each enzyme contributes a different step from the starting product to the finished drug.”

Read more on the Canadian Light Source (CLS) website

Image: Structure of the enzyme studied, a molecule of codeine, and a seed capsule from an opium poppy.

Credit: Sam Carr.

Surprising behavior of a fatty acid enzyme with potential biofuel applications

Surprising behavior of a fatty acid enzyme with potential biofuel applications

Derived from microscopic algae, the rare, light-driven enzyme converts fatty acids into starting ingredients for solvents and fuels.

Although many organisms capture and respond to sunlight, it’s rare to find enzymes – proteins that promote chemical reactions in living things – that are driven by light. Scientists have identified only three so far. The newest one, discovered in 2017, is called fatty acid photodecarboxylase (FAP). Derived from microscopic algae, FAP uses blue light to convert fatty acids into hydrocarbons that are similar to those found in crude oil.

“A growing number of researchers envision using FAPs for green chemistry applications because they can efficiently produce important components of solvents and fuels, including gasoline and jet fuels.” says Martin Weik, the leader of a research group at the Institut de Biologie Structurale at the Université Grenoble Alpes.

Weik is one of the primary investigators in a new study that has captured the complex sequence of structural changes, or photocycle, that FAP undergoes in response to light, which drives this fatty acid transformation. Researchers had proposed a possible FAP photocycle, but the fundamental mechanism was not understood, partly because the process is so fast that it’s very difficult to measure. Specifically, scientists didn’t know how long it took FAP to split a fatty acid and release a hydrocarbon molecule.

Experiments at the Linac Coherent Light Source (LCLS) at the Department of Energy’s SLAC National Accelerator Laboratory helped answer many of these outstanding questions. The researchers described their results in Science.

Read more on the SLAC website

Image: A study using SLAC’s LCLS X-ray laser captured how light drives a series of complex structural changes in an enzyme called FAP, which catalyzes the transformation of fatty acids into starting ingredients for solvents and fuels. This drawing captures the starting state of the catalytic reaction. The dark green background represents the protein’s molecular structure. The enzyme’s light-sensing part, called the FAD cofactor, is shown at center right with its three rings absorbing a photon coming from bottom left. A fatty acid at upper left awaits transformation. The amino acid shown at middle left plays an important role in the catalytic cycle, and the red dot near the center is a water molecule.

Credit: Damien Sorigué/Université Aix-Marseille

A new enzyme cocktail can digest plastic waste six times faster

A new enzyme cocktail can digest plastic waste six times faster

Research undertaken at Diamond has allowed scientists to create a super-enzyme that degrades plastic bottles six times faster than before.

The super-enzyme, derived from bacteria that lives on a diet of plastic, enables the full recycling of plastic bottles. 

Plastic pollution is a global threat as plastics are rarely biodegradable and they can remain in the environment for centuries. One of the most abundant plastics that contributes hugely to this dire situation is poly(ethylene terephthalate) (PET). 
 
PET is used largely in textiles, where it is commonly referred to as polyester, but it is also used as packaging for liquids and foodstuffs. PET’s excellent water-repellent properties led to it being the plastic of choice for soft drink bottles. However, the water resistance of PET means that they are highly resistant to natural biodegradation and can take hundreds of years to break down in the environment. 

In 2018, researchers discovered that a unique bacterium (Ideonella sakaiensis 201-F6) was found feeding on waste from an industrial PET recycling facility. The bacterium had the amazing ability to degrade PET and use it to provide carbon for energy. Central to this ability was the production of a PET-digesting enzyme, known as PETase. 

Read more on the Diamond website

How cellular proteins control cancer spread

How cellular proteins control cancer spread

New finding may help focus the search for anti-cancer drugs

A new insight into cell signals that control cancer growth and migration could help in the search for effective anti-cancer drugs. A team of researchers has revealed key biochemical processes that advance our understanding of colorectal cancer, the third most common cancer among Canadians.

Using the CMCF beamline at the Canadian Light Source (CLS) at the University of Saskatchewan, scientists from McGill University and Osaka University in Japan were able to unlock the behavior of an enzyme involved in the spread of cancer cells. The team found that there is a delicate interaction between the enzyme, PRL3, and another protein that moves magnesium in and out of cells. This interaction is crucial to colorectal cancer growth.

A new insight into cell signals that control cancer growth and migration could help in the search for effective anti-cancer drugs. A team of researchers has revealed key biochemical processes that advance our understanding of colorectal cancer, the third most common cancer among Canadians.

Using the CMCF beamline at the Canadian Light Source (CLS) at the University of Saskatchewan, scientists from McGill University and Osaka University in Japan were able to unlock the behavior of an enzyme involved in the spread of cancer cells. The team found that there is a delicate interaction between the enzyme, PRL3, and another protein that moves magnesium in and out of cells. This interaction is crucial to colorectal cancer growth.

Read more on the Canadian Light Source website

Image: Members of the Gehring research laboratory discussing the results of a protein purification.

Research could lead to better herbicides and infection treatments

Research could lead to better herbicides and infection treatments

Researchers from the University of Queensland (UQ) have used the Australian Synchrotron and cryo-electron microscopy in China to determine the three-dimensional structure of a complex enzyme found in plants microbes that could be used to develop advanced herbicides and treatments for infection.

A large international team led by Prof Luke Guddat of UQ published the structure of the enzyme acetohydroxyacid synthase (AHAS) in the journal Nature and also explained the first step in how the enzyme regulates the biosynthesis of three essential amino acids, leucine, valine and isoleucine.

“The way that the complex regulates this pathway had been unknown until now. We were finally able to explain it by understanding how the entire structure was assembled,” said Prof Guddat, who has been researching this enzyme for twenty years.

Read more on the Australian Synchrotron website

Image: The 3D structure resembles a ‘Maltese Cross’.