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| − | <h1>Factories Network in Cells</h1>
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| − | <h1>Description</h1>
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| − | <h2>Background</h2> | + | <h2>Description</h2> |
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| − | <li>Biosynthesis plays a significant role in industrial production while enzymatic reaction rate is one of the key factors in an efficient production. Mutation, fusing and modification of enzymes are common ways to boost reaction rates, intended to change the properties of the enzymes. However, is there a novel system gaining an extra enhancement in reaction rate without remodeling the enzymes? | + | <li>Biosynthesis plays a significant role in industrial production while enzymatic reaction rate is one of the key factors in an efficient production. and concentration of enzymes is a widely employed solution. Here we engineered yeast cells to express enzymes for producing carotene, which would then be integrated into a protein scaffold based on the interaction between SUMO and SIM modules. The oligomerization of these modules could induce the proximity of enzymes, which enhances the speed of enzymatic reactions and the yield rate of products significantly. |
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| − | <h2>Scaffold and Network</h2>
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| − | <li>As is widely recognized, controlling the location and concentration of the enzymes is a widely recognized solution, in which synthetic protein scaffold has efficaciously increased the reaction rate just by gathering the enzymes together[1]. Here we propose an even better solution with higher rates and access to regulation. As the extension of the scaffold, we first attempt to join all the scaffolds together by a weak interaction attaining a large protein network, where SUMO and SIM comes to be the linker between the scaffolds[2]. As is expected, the SUMO clusters and SIM clusters gradually assemble forming a large protein network, where the concentration of the enzymes will largely increase which cause the chemical potential of the substrates around the network to decrease, driving the substrates to move into the network. We can also abandon the scaffold, just clustering the enzymes by SUMO/SIM. Simplifying the system, this may gather the enzymes more efficiently and give us the chance to regulate the networks by controlling the assembly and disassemble of the cluster.
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| − | <h2>Reference</h2>
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| − | <li> <a href="https://www.sciencedirect.com/science/article/pii/S0168165614009079"> Kim S, Hahn J S. Synthetic scaffold based on a cohesin–dockerin interaction for improved production of 2,3-butanediol in Saccharomyces cerevisiae[J]. Journal of Biotechnology, 2014, 192 Pt A(Pt A):192.
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| − | </a> </li>
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| − | <li> <a href="https://www.nature.com/articles/onc2010108"> Li Y J, Stark J M, Chen D J, et al. Role of SUMO:SIM-mediated protein|[ndash]|protein interaction in non-homologous end joining[J]. Oncogene, 2015, 29(24):3509-18.
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| − | </a> </li>
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| − | <li> <a href="https://www.ncbi.nlm.nih.gov/pubmed/17496128">Verwaal R, Wang J, Meijnen J P, et al. High-Level Production of Beta-Carotene in Saccharomyces cerevisiae by Successive Transformation with Carotenogenic Genes from Xanthophyllomyces dendrorhous[J]. Applied & Environmental Microbiology, 2007, 73(13):4342.
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| − | </a> </li>
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