Team:Copenhagen/Project
From 2011.igem.org
Line 119: | Line 119: | ||
<tr> | <tr> | ||
<td align="center"> | <td align="center"> | ||
- | <table class=" | + | <table class="https://static.igem.org/mediawiki/2011/4/4c/Evolva.jpg" align="center"> |
- | <tr><td><img src=" | + | <tr><td><img src="https://static.igem.org/mediawiki/2011/4/4c/Evolva.jpg" width="100px"></td></tr> |
</table><br> | </table><br> | ||
</tr> | </tr> |
Revision as of 09:30, 21 July 2011
Table of Contents |
Rescue
CyperMan - Kills fungus We hope to be able to develop bacteria that can kill fungus. Cytochrome p450 - the source of CyperMans power Cytochromes p450 is one of the largest gene superfamilies coding for enzymes present in the genomes in all biological kingdoms [6]. The enzymatic activities of these proteins are extremely diverse with activity in biotransformation of drugs, bioconversion of xenobiotics, biosynthesis of compounds as steroids, fatty acids, eicosanoids, fat soluble vitamins and bile acids. Furthermore, cytochrome p450’s are involved in the conversion of alkanes, terpenes and aromatic compounds as well as degradation of herbecides and insecticides [6]. We will exploit this activity of cytochromes p450 in the bioconversion of xenobiotics to neutralize damaging medical residues in waste water. Cytochromes p450 are defined as heme-thiolate proteins featuring a particular spectral signature at 450 nm, thus the name [7]. Despite the label as cytochromes, these proteins are not involved in electron transfers, but act as monooxygenases in a wide range of reactions such as epoxidation, N-dealkylation, O-dealkylation, S-oxidation and hydroxylation [8]. We will focus on the hydroxylating property of the cytochromes, which is also the defining reaction for these enzymes. The reductive activation of molecular oxygen reduces one of the oxygen atoms to a molecule of water, as the other is inserted into the substrate [7].
Fig 1
A key donor of electrons for the reduction of molecular oxygen is the NADPH dependent cytochrome p450 reductase (CPR). This protein shuttles electrons from NADPH through the FAD and FMN- coenzymes into the iron of the prosthetic heme group of cytochrome p450 [9]. A characterization of the cytochromes p450 is the main objective with this project. We will exploit the wide specificity of these cytochromes to target many different damaging agents continuously by hydroxylation, which can reduce the damaging activity of e.g. estrogen. Impact factors: Open source BioBricks: Our project has the aim to characterize Cytochrome p450 as a BioBrick and thus add it to the partsregistry of BioBricks, a continuously growing collection of genetic parts that can be mixed and matched to build synthetic biology devices and systems (partsregistry.org). Hence our project contributes to the expansion of the partsregistry, benefitting all researchers with interest in this particular protein, since cytochrome p450 doesn’t exist in the partsregistry. The partsregistry is founded on an open source philosophy, a philosophy we see as a great advantage for development and improvement of the number BioBricks already existing. The addition of cytochrome p450 to this catalogue will perhaps encourage other groups to look at other aspects of the many functions of p450 and thus contribute to the formation of new biological systems – further expanding the field of synthetic biology. Ecological and economical prospects: Our future aim with our project is to improve wastewater treatments and thus contribute to a cleaner and uncontaminated drinking water for everyone. With this scientific project, we will move towards this realization, but more research is needed. Our belief is that further research on the use of cytochrome p450 will give a valid and an inexpensive product for use in wastewater treatment plants, thus benefitting the environment and our planet. References [6] F. Hannemann, A. Bichet, K. M. Ewen, R. Bernhardt: Cytochrome p450 systems – biological variations of electron transport chains. Biochemica et Biophysica Acta 1770 (2007) 330 - 344 [7] Paul R. Ortiz de Montellano. Hydrocarbon Hydroxylation by Cytochrome P450 Enzymes. Chem Rev. 2010 February 10; 110(2): 932 [8] http://www.anaesthetist.com/physiol/basics/metabol/cyp/Findex.htm [9] T. Laursen, K. Jensen,B. L. Møller: Conformational changes of the NADPH dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450. Biochemica et Biophysica Acta 1814 (2011) 132-138
|
iGEM Medals Requirements Bronze Team registrationComplete Project Summary form Team Wiki Present a poster and a talk at the iGEM Jamboree At least one new submitted and well-characterized standard BioBrick Part or Device. Silver
Demonstrate that at least one new BioBrick Part of your own design and construction works as expected Gold For Gold Medal, either of the following must be checked
Improve an existing BioBrick Part or Device. |
Comments or questions to the team? Please mail us at igemcopenhagen@gmail.com |