Team:UNITN-Trento/Safety

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An unwanted byproduct is produced in the last step of ethylene synthesis: cyanide, an highly toxic compound that inhibits the cychrome C oxydase enzyme. Plants however have a complex detoxyfication mechanism. <b>That's why we don't die when we eat a fruit!</b></p>
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An unwanted byproduct is produced in the last step of ethylene synthesis: cyanide, an highly toxic compound that inhibits the cychrome C oxydase enzyme. Plants however have a complex detoxyfication mechanism.</p> <center><h3><b>That's why we don't die when we eat a fruit!</b><h3></center><br/>
<center><img title="This is the exception that proves the rule. Bruno in fact is allergic to almost all fruit and would die in any case!!!" id="brunoide" src="https://static.igem.org/mediawiki/2013/5/5a/Tn-2013-bruno_face_2.jpg" /></center>
<center><img title="This is the exception that proves the rule. Bruno in fact is allergic to almost all fruit and would die in any case!!!" id="brunoide" src="https://static.igem.org/mediawiki/2013/5/5a/Tn-2013-bruno_face_2.jpg" /></center>

Revision as of 09:54, 24 September 2013

Safety

When we decide to engineer a biological system able to produce ethylene and methyl-salycilate, we looked at all the existing natural pathways. For ethylene we firstly checked the plants producing pathway.

An unwanted byproduct is produced in the last step of ethylene synthesis: cyanide, an highly toxic compound that inhibits the cychrome C oxydase enzyme. Plants however have a complex detoxyfication mechanism.

That's why we don't die when we eat a fruit!


We immediately though this detoxification path was too complicate to be insered into a microrganism. This due for example that plants enzymes often have diffent glycosilisation pattern that bacteria can not produce. A wrong glycosilation pattern can affect protein folding and activity. In order to avoid these problems, we quitted this path and focused on a more interesting one. Pseudomonas Syrigae pv., a plant pathogen bacteria, is able to produce ethylene explointing only one enzyme. 2-Oxoglutarate Oxygenase/Decarboxylase enzyme takes 2-Oxoglutarate as substrate and transforms it into ethylene + water + carbon-dioxyde. Goto M. Plant and Cell Physiology (2012) 26, 141-150.

Safety form;