Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

How Enzymes Work: UB Chemists Publish A Major Discovery

20.06.2007
In a publication selected as a "2007 Hot Article" by the journal Biochemistry, University at Buffalo chemists report the discovery of a central mechanism responsible for the action of the powerful biological catalysts known as enzymes.

The UB research provides critical insight into why catalysis is so complex and may help pave the way for improving the design of synthetic catalysts.

"The more that is known about catalysis, the better chances we have of designing active catalysts," said John P. Richard, Ph.D., professor of chemistry in the UB College of Arts and Sciences and co-author of the paper with Tina L. Amyes, Ph.D., UB adjunct associate professor of chemistry.

"Attempts to replicate evolution and design catalysts of non-biological reactions with enzyme-like activity have failed, because scientists have yet to unravel the secrets of enzyme catalysis," Richard said.

But, he said, these secrets, once revealed, have the potential to transform the chemical industry in processes ranging from soft-drink manufacturing to the production of ethanol and countless other industrial processes.

"Enzymes are the products of billions of years of cellular evolution," he said.

While attempts to design catalysts have been somewhat successful, the catalysis that results is far less efficient than that produced by reactions with enzymes.

Richard explained that protein catalysts are distinguished by their enormous molecular weights, ranging from 10,000 to greater than 1,000,000 Daltons, whereas a synthetic molecule with a weight of 1,000 would be considered large.

The recent results by Richard and Amyes provide critical insight into why effective catalysis requires such large molecules.

Catalysis starts with molecular recognition of the substrate by the catalyst, Richard explained.

The so-called "catalytic" recognition is limited in man-made catalysts to several atoms that participate in the chemical reaction.

Amyes and Richard have provided compelling evidence that interactions between enzymes and non-reacting portions of the substrate are critical for large catalytic rate accelerations.

"These findings demonstrate a simple principle of catalysis that is important for many enzymes that catalyze reactions of substrates containing phosphate groups and which can be generalized to all enzymes," said Richard.

He explained that the chemistry between a catalyst and substrate occurs where groups of amino acid residues interact with the substrate.

But enzymes also have domains that interact with the non-reacting parts of the substrate, he continued.

"A flexible loop on the enzyme wraps around the substrate, burying it in an environment that's favorable for catalysis," he said. "In order to bury the substrate, certain interactions are necessary that allow the loop to wrap around the substrate and that's what the phosphate groups on the substrate are doing."

The UB research demonstrates just how important this process is to catalysis.

"We've shown that these interactions are critical to the process of making reactions faster," said Richard.

The critical experiment by the UB researchers was to clip the covalent bond that links the phosphate groups to the substrate.

"We have found that the interactions between phosphate groups and several enzymes are used to promote the chemistry even in the absence of a covalent linkage," said Richard. "These results have surprised many enzymologists."

To conduct the research, Richard and Amyes developed a specialized and technically difficult assay for enzyme activity that uses nuclear magnetic resonance spectroscopy to detect chemical reactions that would normally be invisible.

Richard and Amyes have applied their method during the past 10 years to a wide variety of chemical and enzymatic reactions with results published in approximately 25 papers in Biochemistry and The Journal of the American Chemical Society. Richard's work on enzymes has been supported continuously since 1987 by grants from the National Institutes of Health.

The University at Buffalo is a premier research-intensive public university, the largest and most comprehensive campus in the State University of New York. UB's more than 27,000 students pursue their academic interests through more than 300 undergraduate, graduate and professional degree programs. Founded in 1846, the University at Buffalo is a member of the Association of American Universities.

Ellen Goldbaum | EurekAlert!
Further information:
http://www.buffalo.edu

Further reports about: Amyes Catalysis Substrate catalyst enzyme interactions phosphate

More articles from Life Sciences:

nachricht The birth of a new protein
20.10.2017 | University of Arizona

nachricht Building New Moss Factories
20.10.2017 | Albert-Ludwigs-Universität Freiburg im Breisgau

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

Die letzten 5 Focus-News des innovations-reports im Überblick:

Im Focus: Neutron star merger directly observed for the first time

University of Maryland researchers contribute to historic detection of gravitational waves and light created by event

On August 17, 2017, at 12:41:04 UTC, scientists made the first direct observation of a merger between two neutron stars--the dense, collapsed cores that remain...

Im Focus: Breaking: the first light from two neutron stars merging

Seven new papers describe the first-ever detection of light from a gravitational wave source. The event, caused by two neutron stars colliding and merging together, was dubbed GW170817 because it sent ripples through space-time that reached Earth on 2017 August 17. Around the world, hundreds of excited astronomers mobilized quickly and were able to observe the event using numerous telescopes, providing a wealth of new data.

Previous detections of gravitational waves have all involved the merger of two black holes, a feat that won the 2017 Nobel Prize in Physics earlier this month....

Im Focus: Smart sensors for efficient processes

Material defects in end products can quickly result in failures in many areas of industry, and have a massive impact on the safe use of their products. This is why, in the field of quality assurance, intelligent, nondestructive sensor systems play a key role. They allow testing components and parts in a rapid and cost-efficient manner without destroying the actual product or changing its surface. Experts from the Fraunhofer IZFP in Saarbrücken will be presenting two exhibits at the Blechexpo in Stuttgart from 7–10 November 2017 that allow fast, reliable, and automated characterization of materials and detection of defects (Hall 5, Booth 5306).

When quality testing uses time-consuming destructive test methods, it can result in enormous costs due to damaging or destroying the products. And given that...

Im Focus: Cold molecules on collision course

Using a new cooling technique MPQ scientists succeed at observing collisions in a dense beam of cold and slow dipolar molecules.

How do chemical reactions proceed at extremely low temperatures? The answer requires the investigation of molecular samples that are cold, dense, and slow at...

Im Focus: Shrinking the proton again!

Scientists from the Max Planck Institute of Quantum Optics, using high precision laser spectroscopy of atomic hydrogen, confirm the surprisingly small value of the proton radius determined from muonic hydrogen.

It was one of the breakthroughs of the year 2010: Laser spectroscopy of muonic hydrogen resulted in a value for the proton charge radius that was significantly...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

ASEAN Member States discuss the future role of renewable energy

17.10.2017 | Event News

World Health Summit 2017: International experts set the course for the future of Global Health

10.10.2017 | Event News

Climate Engineering Conference 2017 Opens in Berlin

10.10.2017 | Event News

 
Latest News

Terahertz spectroscopy goes nano

20.10.2017 | Information Technology

Strange but true: Turning a material upside down can sometimes make it softer

20.10.2017 | Materials Sciences

NRL clarifies valley polarization for electronic and optoelectronic technologies

20.10.2017 | Interdisciplinary Research

VideoLinks
B2B-VideoLinks
More VideoLinks >>>