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Scripps Research scientists find early evolution maximized the 'spellchecking' of protein sequences

Scientists at Scripps Research Institute have discovered that two separate functions—alanine adding and editing—were joined together in a single enzyme during early evolution. The findings show that the C-Ala domain enhances collaboration between the aminoacylation and editing domains, making them work together synergistically.

SourceScripps Research Institute·JournalScience·DateAug 6, 2009

A 'super sensor' for cancer and CSIs

The 'super sensor' can detect pathogens, pollution, and disease biomarkers with high precision, making it suitable for various environments and situations. The device's potential applications include early warning systems for heart attacks, detecting pollutants in drinking water, and monitoring pesticides in organic food.

Toxin detection as close as an inkjet printer

Researchers at McMaster University developed a method for printing toxin-detecting biosensors on paper using an inkjet printer, utilizing lateral flow sensing technology. The sensors retain enzyme activity for months, making them suitable for monitoring environmental toxins and detecting diseases in remote settings.

SourceMcMaster University·JournalAnalytical Chemistry·DateJul 13, 2009

Study could help target new pancreatitis treatments

Researchers have discovered that deleting specific genes can significantly reduce toxic calcium release in pancreatic cells, which can trigger pancreatitis. The study's findings may lead to the development of more effective treatments for the disease, particularly those related to excessive drinking.

SourceUniversity of Liverpool·JournalProceedings of the National Academy of Sciences·DateJun 29, 2009

LSUHSC research identifies enzyme that makes survival molecule for key vision cells

Researchers at LSU Health Sciences Center identified the 15-LOX-1 enzyme, which produces neuroprotectin D1, a molecule that protects retinal cells key to vision. This discovery has potential applications in treating retinal degenerative diseases and neurodegenerative conditions like Parkinson's disease.

SourceLouisiana State University Health Sciences Center·JournalJournal of Biological Chemistry·DateJun 26, 2009

Structures from the human immune system's oldest branch shed light on a range of diseases

Researchers have discovered two new structures involving the central component of an enzyme important to the complement system of the immune response. These findings may pave the way for more efficient therapeutics for diseases such as age-related macular degeneration, rheumatoid arthritis, and systemic lupus erythematosus.

SourceUniversity of Pennsylvania School of Medicine·JournalNature Immunology·DateJun 17, 2009

The microbial hydrocarbon diet

Researchers have found the optimal conditions for a new microbe to degrade n-hexadecane, suggesting a more effective approach to bioremediation. The team discovered that enzymes within the microbial cell and its membrane are responsible for degradation, with neutral pH and 30 Celsius temperature being ideal conditions.

SourceInderscience Publishers·JournalInternational Journal of Environment and Pollution·DateJun 11, 2009

Enzyme involved in inflammatory bowel disease discovered at Penn State College of Medicine

Researchers at Penn State College of Medicine have discovered an enzyme called meprin that plays a key role in the severity of inflammatory bowel diseases (IBD) such as ulcerative colitis and Crohn's disease. The study found that mice lacking meprin had more severe intestinal damage, indicating that meprin reduces inflammation.

Capsules encapsulated

Scientists have created a microcontainer that can hold thousands of individual 'carrier units' - a 'capsosome'. These are polymer capsules with embedded liposomes, combining the advantages of both systems. The capsosomes were produced by several steps and demonstrated successful transport of an enzyme model cargo.

SourceWiley·DateMay 19, 2009

Starve a yeast, sweeten its lifespan

Researchers found that acetylation affects yeast lifespan through the NuA4 enzyme complex, which also controls sugar production in cells. This discovery may have implications for understanding aging and human diseases, as the mechanisms identified are conserved across species.

SourceJohns Hopkins Medicine·JournalCell·DateMar 23, 2009

No hiding place for infecting bacteria

Researchers in Colorado discovered a way to disrupt Pseudomonas aeruginosa biofilm formation by targeting protein and DNA with specific enzymes. This breakthrough could lead to improved treatment strategies for infections caused by this bacteria, which are prevalent in burns, wounds, and cystic fibrosis patients.

SourceMicrobiology Society·JournalJournal of Medical Microbiology·DateMar 15, 2009

Cells get two chances, not just one, to fix their mistakes

Researchers at Ohio State University discovered that cells have a second chance to correct errors in protein production, which could lead to new insights into neurodegenerative disorders and the development of targeted antibiotics. This discovery gives scientists a better understanding of the mechanism behind protein synthesis mistakes.

SourceOhio State University·JournalMolecular Cell·DateMar 12, 2009

Commercial yeasts upgraded with an enzyme for biofuel production

Researchers at Goethe University Frankfurt have discovered an enzyme that enables yeast cells to ferment xylose into ethanol, a waste sugar in the cellulosic ethanol production process. This single-step conversion technology has the potential to increase biofuel production efficiency and reduce competition with food and feed production.

SourceGoethe University Frankfurt·JournalApplied and Environmental Microbiology·DateFeb 24, 2009

Bioremediation to keep atrazine from waterways

A new enzyme developed by CSIRO Australia successfully removes over 90% of atrazine from contaminated water in a trial, providing a promising solution to reduce off-farm water contamination. The enzyme works against various triazine herbicides and is expected to benefit farmers worldwide.

Duke software dramatically speeds enzyme design

A Duke University-led team has developed a computer program that can redesign enzymes to produce natural antibiotics. The algorithm, called K*, sorts through possible shapes and changes of the key enzyme that produces gramicidin S, a natural antibiotic. This new technique may pave the way for more automated redesign of old drugs.

SourceDuke University·JournalProceedings of the National Academy of Sciences·DateFeb 16, 2009

Mutant rats resist warfarin

Researchers identified eighteen new genetic changes in rats from four continents that enable resistance to warfarin. VKORC1 gene mutations may cause heritable resistance by preventing coumarin derivatives from interfering with the reductase enzyme activity.

SourceBMC (BioMed Central)·JournalBMC Genetics·DateFeb 5, 2009

Potential new herpes therapy studied

Researchers have made a breakthrough in developing a new gene-targeting therapy that uses an RNA enzyme to inhibit strains of the herpes simplex virus. The technique has shown promise in experiments with mice and rabbits, but further research is needed before it can be attempted in people infected with herpes.

SourceUniversity of Florida·JournalJournal of Virology·DateFeb 3, 2009

Researchers find pathway and enzyme unique to tularemia organism

Researchers at UTSA have made a breakthrough discovery in the fight against tularemia, a deadly bio-warfare agent. They identified a unique metabolic pathway and enzyme, nicotinamide adenine dinucleotide synthetase (NMS), that is specific to Francisella tularensis, making it a potential target for therapeutic development.

SourceUniversity of Texas at San Antonio·JournalProceedings of the National Academy of Sciences·DateFeb 3, 2009

Discovery fleshes out metabolism of key environmental and energy bacteria

A team of researchers has discovered a new enzyme in Shewanella that works together to oxidize lactate, a food and energy source for many microbes. The discovery suggests that dozens of bacteria use this multi-protein enzyme instead of the single-protein version, which could help clean up toxic pollutants.

SourceDOE/Pacific Northwest National Laboratory·JournalProceedings of the National Academy of Sciences·DateFeb 2, 2009