Enzymes to catalyse new drug production
Apr 15, 2006 - 9:28:00 AM
, Reviewed by: Vineet Gupta
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Modern drugs are designed to have structures that stick to enzymes and prevent them from catalysing the reactions, so our results need to be taken into account when designing new drugs
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By University of Manchester,
[RxPG] Groundbreaking research published in journal Science could revolutionise the way drugs are made and have major implications for the industrial sector, say its authors.
The University of Manchester team, working with colleagues in Bristol, has provided a unique insight into the working of enzymes biological molecules that speed up chemical reactions in the body.
When these chemical reactions go wrong they can lead to disease, so modern drugs are designed to target enzymes and 'switch them off'.
But their ability to accelerate chemical reactions means enzymes are also used in a number of commercial processes, including brewing, food processing, domestic cleaning and paper manufacturing.
"Improving our fundamental knowledge of how enzymes work is important to a wide range of pharmaceutical and industrial fields," said Professor Nigel Scrutton, one of the lead researchers at Manchester.
"Enzymes are central to the existence of life because most chemical reactions in our cells would take place too slowly or produce a different outcome without their involvement.
"But when enzymes malfunction they can cause serious diseases, so modern drugs are designed to prevent enzymes accelerating, or 'catalysing', inappropriate reactions.
"Our research has shown at an atomic level how enzymes act as catalysts; the findings are a radical departure from the traditional view of how they work and might explain why attempts to make artificial enzymes have so far been disappointing.
The work published as a major research article in the leading journal Science builds on earlier studies by Professor Scrutton and Manchester colleagues, Professor Michael Sutcliffe and Dr David Leys.
Together they have shown, now in unprecedented detail, how enzymes avoid unfavourable energy barriers caused by the resistance to a reaction by allowing matter to 'flow through' the barrier a process known as quantum mechanical tunnelling.
"We have provided new insight into how enzymes work from painstaking efforts of a large interdisciplinary group based on detailed experimental observations and theoretical analysis at the atomic level," said Professor Scrutton, who is based in the University's Faculty of Life Sciences.
"Modern drugs are designed to have structures that stick to enzymes and prevent them from catalysing the reactions, so our results need to be taken into account when designing new drugs.
"In the longer term, this research could also help us exploit enzymes more successfully and lead to better manufacturing processes in a number of commercial sectors.
"In cleaning products, for instance, enzymes help speed up the chemical reactions that break down protein and starch stains; a better understanding of how this process works could one day lead to more effective, faster acting agents."
Publication:
The research is published in Science on 14 April, 2006
On the web:
www.manchester.ac.uk 
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Additional information about the news article
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Professor Nigel Scrutton and Dr David Leys are based in The University of Manchester's Faculty of Life Sciences; Professor Michael Sutcliffe, who is joint head of the project with Professor Scrutton, is based in Manchester's School of Chemical Engineering and Analytical Science. The University of Bristol group is headed by Dr A Mulholland
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