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New Apoproteins Study Results from Institute for Biology Research Described (300-Fold Increase in Production of the Zn2+-Dependent Dechlorinase TrzN...

July 15, 2014



New Apoproteins Study Results from Institute for Biology Research Described (300-Fold Increase in Production of the Zn2+-Dependent Dechlorinase TrzN in Soluble Form via Apoenzyme Stabilization)

By a News Reporter-Staff News Editor at Life Science Weekly -- Research findings on Proteins are discussed in a new report. According to news reporting out of Grenoble, France, by NewsRx editors, research stated, "Microbial metalloenzymes constitute a large library of biocatalysts, a number of which have already been shown to catalyze the breakdown of toxic chemicals or industrially relevant chemical transformations. However, while there is considerable interest in harnessing these catalysts for biotechnology, for many of the enzymes, their large-scale production in active, soluble form in recombinant systems is a significant barrier to their use."

Our news journalists obtained a quote from the research from Institute for Biology Research, "In this work, we demonstrate that as few as three mutations can result in a 300-fold increase in the expression of soluble TrzN, an enzyme from Arthrobacter aurescens with environmental applications that catalyzes the hydrolysis of triazine herbicides, in Escherichia coli. Using a combination of X-ray crystallography, kinetic analysis, and computational simulation, we show that the majority of the improvement in expression is due to stabilization of the apoenzyme rather than the metal ion-bound holoenzyme. This provides a structural and mechanistic explanation for the observation that many compensatory mutations can increase levels of soluble-protein production without increasing the stability of the final, active form of the enzyme."

According to the news editors, the research concluded: "This study provides a molecular understanding of the importance of the stability of metal ion free states to the accumulation of soluble protein and shows that differences between apoenzyme and holoenzyme structures can result in mutations affecting the stability of either state differently."

For more information on this research see: 300-Fold Increase in Production of the Zn2+-Dependent Dechlorinase TrzN in Soluble Form via Apoenzyme Stabilization. Applied and Environmental Microbiology, 2014;80(13):4003-4011. Applied and Environmental Microbiology can be contacted at: Amer Soc Microbiology, 1752 N St NW, Washington, DC 20036-2904, USA. (American Society for Microbiology - www.asm.org; Applied and Environmental Microbiology - aem.asm.org)

Our news journalists report that additional information may be obtained by contacting C.J. Jackson, Inst Biol Struct, Grenoble, France. Additional authors for this research include C.W. Coppin, P.D. Carr, A. Aleksandrov, M. Wilding, E. Sugrue, J. Ubels, M. Paks, J. Newman, T.S. Peat, R.J. Russell, M. Field, M. Weik, J.G. Oakeshott and C. Scott (see also Proteins).

Keywords for this news article include: France, Europe, Grenoble, Apoenzymes, Apoproteins

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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