Enzyme catalysis unravelled in new research

October 7, 2013
Enzyme catalysis unravelled in new research

(Phys.org) —New research by the School of Chemistry has significantly advanced our understanding of how enzymes (proteins) increase the rate of chemical reaction. Now potentially able to achieve greater control of enzyme action, this will clear the way for scientists to design new enzymes with important implications in a range of industries, and to develop new anti-infective and anti-cancer drugs.

Enzymes are fundamental to life. They are proteins that catalyse chemical reactions, for example in metabolic processes such as the release of energy from foods, and in cell growth and repair. Often, they increase reaction rates by several trillion times. In addition to their presence in nature, they find uses in industries such as food, cosmetics, detergents, pharmaceuticals and chemical manufacturing.

Understanding exactly how enzymes increase reaction rates – typically much more effectively and under more environmentally friendly conditions than artificial catalysts – is an important goal in biotechnology. Therefore, a thorough understanding of how enzymes achieve their phenomenal rate enhancements is of great importance to fields like biocatalysis, bioenergy, drug design and the emerging field of .

Despite the development of several theories to explain the enormous catalytic power of enzymes, even after a century of study it is not fully understood. Some recent theories have proposed that internal 'promoting motions' of the - specific motions that act to reduce the height or width of the energy barrier to the reaction - are used to drive the chemistry. This remains a topic of considerable debate, particularly since the identification and analysis of dynamical effects in enzyme-catalysed reactions has proven very challenging.

Led by Cardiff University's Professor Rudolf Allemann, the team consists of researchers from Cardiff University's School of Chemistry, the University of Bristol, the University of València and Jaume I University in Castelló. They used a combination of experimental and computational approaches to study the enzyme dihydrofolate reductase - an important target for anti-infective and anti-cancer drugs.

The scientists were able to alter the enzyme's motions on a wide range of timescales whilst leaving its chemical properties unchanged. They found no significant role for 'promoting motions' in the reaction, but did demonstrate a general coupling of enzyme motions to the catalysed reaction.

Professor Allemann, Distinguished Research Professor and Head of Cardiff's School of Chemistry said: "This is a leap forward in our understanding of enzyme catalysis. It shows that 'promoting motions' are not, after all, required to explain rate enhancements, but shows that enzyme motions are involved in the through a passive rather than an active mechanism. Ultimately, it reveals that enzymes are not fundamentally different from man-made catalysts, they are just much better."

Professor Jim Murray, Head of the Molecular Biosciences division of the School of Biosciences at Cardiff, said: "This is an important advance that has far-reaching implications beyond its immediate field, for example in biotechnology and synthetic biology. It challenges current thinking in the field of , but it also provides new opportunities to use our knowledge to create societal impact."

The work is published in the prestigious journal Proceedings of the National Academy of Sciences.

Explore further: Quantum biology and Ockham's razor

More information: www.pnas.org/content/early/2013/09/18/1312437110.abstract

Related Stories

Quantum biology and Ockham's razor

February 6, 2012

(PhysOrg.com) -- In a paper just published in Nature Chemistry, a team of University of Bristol scientists explores whether new models or concepts are needed to tackle one of the 'grand challenges' of chemical biology: understanding ...

Form and function in enzyme activity

April 6, 2012

Many industrial chemistry applications, such as drug or biofuel synthesis, require large energy inputs and often produce toxic pollutants. But chemistry and chemical biology professor Mary Jo Ondrechen said enzymes — ...

Tweaking Mother Nature's chemistry box

September 27, 2013

Natural enzymes are very clever molecular machines. They are the catalyst for many of nature's chemical transformations. And the conditions they need to perform their task are rather precisely defined. There is a need to ...

Study finds new moves in protein's evolution

September 29, 2013

Highlighting an important but unexplored area of evolution, scientists at The Scripps Research Institute (TSRI) have found evidence that, over hundreds of millions of years, an essential protein has evolved chiefly by changing ...

New small-molecule catalyst does the work of many enzymes

October 3, 2013

Researchers report that they have created a man-made catalyst that is an "enzyme mimic." Unlike most enzymes, which act on a single target, the new catalyst can alter the chemical profiles of numerous types of small molecules. ...

Recommended for you

A new form of real gold, almost as light as air

November 25, 2015

Researchers at ETH Zurich have created a new type of foam made of real gold. It is the lightest form ever produced of the precious metal: a thousand times lighter than its conventional form and yet it is nearly impossible ...

Getting under the skin of a medieval mystery

November 23, 2015

A simple PVC eraser has helped an international team of scientists led by bioarchaeologists at the University of York to resolve the mystery surrounding the tissue-thin parchment used by medieval scribes to produce the first ...

Moonlighting molecules: Finding new uses for old enzymes

November 27, 2015

A collaboration between the University of Cambridge and MedImmune, the global biologics research and development arm of AstraZeneca, has led researchers to identify a potentially significant new application for a well-known ...

1 comment

Adjust slider to filter visible comments by rank

Display comments: newest first

1 / 5 (7) Oct 07, 2013
"New research by the School of Chemistry has significantly advanced our understanding of how enzymes...."


"Enzymes are fundamental to life. They are proteins that catalyse chemical reactions...."


"Understanding exactly how enzymes increase reaction rates – typically much more effectively and under more environmentally friendly conditions...."


"Despite the development of several theories to explain the enormous catalytic power of enzymes...."


The real story here is brilliant and fascinating since they made an entire enzyme out of heavy isotopes to make its physical motions inertially slower and yet did not actually observe a big enough real slow down to support a mechanical assist view of enzyme effectiveness.


Please sign in to add a comment. Registration is free, and takes less than a minute. Read more

Click here to reset your password.
Sign in to get notified via email when new comments are made.