Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:


The tiniest mutation will give a detoxification enzyme a completely new function

Researchers at Uppsala University have made the surprising discovery that the smallest possible mutation in a detoxification enzyme can alter what type of chemical reaction it will catalyse. The results has been published online by the respected journal, Proceedings of the National Academy of Sciences, PNAS.

In all living organisms, molecules are transformed into new chemical substances through processes which are catalysed by enzymes. Enzymes are proteins whose catalysing capacity enables chemical reactions which otherwise would not occur with sufficient speed or in a controlled way. The molecular evolution of enzymes is based on major or minor structural changes in a protein, which acquires new catalytic characteristics through the modification. The mutations in the genetic material which cause these structural changes have been regarded as random, but in certain cases it appears as if certain positions in a protein mutate more frequently than other positions in the protein. These positions are assumed to be particularly important to the biological functions of the protein.

Glutathione transferases are a family of enzymes which catalyse the detoxification of a broad spectrum of mutagens and carcinogens. Through major or minor structural variations, these enzymes have acquired new characteristics, thereby giving rise to more detoxification enzymes and a reinforced defence against toxic substances. A team of researchers led by Professor Bengt Mannervik has now shown that mutations in a single position in a glutathione transferase can dramatically alter the enzyme’s capacity to act selectively on various toxic substances. Through one type of mutation, the enzyme will become adapted to reactions in which the reactive group in the toxic substance is split off and replaced by glutathione, the body’s protective substance; through alternative mutations, the enzyme acquires the capacity to neutralise other reactive groups by linking them with glutathione.

“This discovery shows how the evolution of new enzyme functions may be quickly adapted to new needs. This is particularly significant for the defence against new toxins which may appear and threaten the survival of biological organisms,” says Bengt Mannervik.

This new study complements an earlier study by the research team, published in Science in January, which showed how a protein could be tailored to fulfil new functions through major changes to its structure.

Anneli Waara | alfa
Further information:

More articles from Life Sciences:

nachricht First time-lapse footage of cell activity during limb regeneration
25.10.2016 | eLife

nachricht Phenotype at the push of a button
25.10.2016 | Institut für Pflanzenbiochemie

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Etching Microstructures with Lasers

Ultrafast lasers have introduced new possibilities in engraving ultrafine structures, and scientists are now also investigating how to use them to etch microstructures into thin glass. There are possible applications in analytics (lab on a chip) and especially in electronics and the consumer sector, where great interest has been shown.

This new method was born of a surprising phenomenon: irradiating glass in a particular way with an ultrafast laser has the effect of making the glass up to a...

Im Focus: Light-driven atomic rotations excite magnetic waves

Terahertz excitation of selected crystal vibrations leads to an effective magnetic field that drives coherent spin motion

Controlling functional properties by light is one of the grand goals in modern condensed matter physics and materials science. A new study now demonstrates how...

Im Focus: New 3-D wiring technique brings scalable quantum computers closer to reality

Researchers from the Institute for Quantum Computing (IQC) at the University of Waterloo led the development of a new extensible wiring technique capable of controlling superconducting quantum bits, representing a significant step towards to the realization of a scalable quantum computer.

"The quantum socket is a wiring method that uses three-dimensional wires based on spring-loaded pins to address individual qubits," said Jeremy Béjanin, a PhD...

Im Focus: Scientists develop a semiconductor nanocomposite material that moves in response to light

In a paper in Scientific Reports, a research team at Worcester Polytechnic Institute describes a novel light-activated phenomenon that could become the basis for applications as diverse as microscopic robotic grippers and more efficient solar cells.

A research team at Worcester Polytechnic Institute (WPI) has developed a revolutionary, light-activated semiconductor nanocomposite material that can be used...

Im Focus: Diamonds aren't forever: Sandia, Harvard team create first quantum computer bridge

By forcefully embedding two silicon atoms in a diamond matrix, Sandia researchers have demonstrated for the first time on a single chip all the components needed to create a quantum bridge to link quantum computers together.

"People have already built small quantum computers," says Sandia researcher Ryan Camacho. "Maybe the first useful one won't be a single giant quantum computer...

All Focus news of the innovation-report >>>



Event News

#IC2S2: When Social Science meets Computer Science - GESIS will host the IC2S2 conference 2017

14.10.2016 | Event News

Agricultural Trade Developments and Potentials in Central Asia and the South Caucasus

14.10.2016 | Event News

World Health Summit – Day Three: A Call to Action

12.10.2016 | Event News

Latest News

Ice shelf vibrations cause unusual waves in Antarctic atmosphere

25.10.2016 | Earth Sciences

Fluorescent holography: Upending the world of biological imaging

25.10.2016 | Power and Electrical Engineering

Etching Microstructures with Lasers

25.10.2016 | Process Engineering

More VideoLinks >>>