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the main role in the catalytic process. And they speculated the catalytic mechanism of Ceas2, as | the main role in the catalytic process. And they speculated the catalytic mechanism of Ceas2, as | ||
shown below [2].</h4> | shown below [2].</h4> | ||
− | <img src="https://static.igem.org/mediawiki/2017/2/29/Basicpart.png" class="img-responsive"> | + | <center><img src="https://static.igem.org/mediawiki/2017/2/29/Basicpart.png" class="img-responsive"></center> |
− | <h4> </h4> | + | |
+ | <h4> | ||
+ | <h2 style="text-align:center"> How we use these basic parts?</h2> | ||
+ | <center> <img src="https://static.igem.org/mediawiki/2017/c/ce/5%2C6%2C7%2C8%EF%BC%8C10.png" class="img-responsive"></center> | ||
+ | <center>Fig.5:DAK;6:NOX;7,ceaS2;8:gld;10:CAT</center> | ||
+ | <h4>We designed a GDC (GlyDH-DAK-Ceas2) pathway that could produce acrylic acid using glycerol. In this pathway, | ||
+ | GlyDH (Glycerol dehydrogenase,BBa_K2347001) can efficiently convert glycerol to DHA (1,3-Dihydroxyacetone), and | ||
+ | then DAK(Dihydroxyacetone kinase,BBa_K2347002) enzyme can phosphorylate DHA to DHAP, and then the ceaS2 Enzyme | ||
+ | BBa_K2347000)can make it into acrylic acid. | ||
+ | <br>In addition, since GlyDH is NAD + dependent, in order to increase the supply of reducing force, we also | ||
+ | added the NOX (NADH dehydrogenase, BBa_K2347003) and CAT (Catalase, BBa_K2347004) to this pathway, providing | ||
+ | the reduction force for GlyDH through two layers of substrate. Finally, we created the new combination of GNCDC | ||
+ | (GlyDH-NOX-CAT-DAK-ceaS2) pathway using five enzymes from BBa_K2347000 to BBa_K2347004 to produce acrylic acid.</h4> | ||
+ | <br> | ||
+ | <center><img src="https://static.igem.org/mediawiki/2017/1/1b/Basicpart2.png" class="img-responsive"></center> | ||
+ | <br> | ||
+ | <h5>[1] MERSKI M, TOWNSEND C A. Observation of an Acryloyl–Thiamin Diphosphate Adduct in the First Step of | ||
+ | Clavulanic Acid Biosynthesis [J]. Journal of the American Chemical Society, 2007, 129(51): 15750-1. | ||
+ | <br> [2] CAINES M E, ELKINS J M, HEWITSON K S, et al. Crystal structure and mechanistic implications | ||
+ | of N2-(2-carboxyethyl)arginine synthase, the first enzyme in the clavulanic acid biosynthesis pathway | ||
+ | [J]. Journal of Biological Chemistry, 2004, 279(7): 5685-92.</h5> | ||
+ | </h4> | ||
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Latest revision as of 02:34, 2 November 2017