Creating New Enzyme Actions De Novo

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ABSTRACT

Enzymes are molecules, specifically proteins that catalyze chemical reactions. Enzymes, like all catalysts, accelerate the rate of a reaction by lowering the activation energy. Nucleic acid RNA molecules called ribozymes can also act as enzymes and catalyze reactions. The development of new enzymes for the synthesis of chemical reactions, pharmaceuticals, and tools for molecular biology is a new and upcoming interest. Work has previously been done in the development for modifying and improving already existing enzymes. There is also much to still learn involving the designs and evolution of enzymes because it is greatly reliant on extensive knowledge of the mechanisms of these reactions. In this paper it is shown that new enzymatic activities can be created de novo, which means from scratch or very differently. There is no need for previous mechanistic information. This is done by selecting from a naive protein library, or one in which it is not designed to do what they are actually doing with it. This library is made up of a trillion different proteins with different amino acid sequences, so there is not much need for a plan. Messenger RNA, RNA used specifically to translate proteins, display is used and the proteins are covalently linked to their encoding mRNA, meaning that they share stable chemical bonds and are tethered to each other. Functional proteins are selected from an in vitro translated protein library. This is not an obvious way to link the genetic information that encodes it together. It is done without constraints imposed by any in vivo step, which simplifies the process when it is in vitro. This specific technique has been used to evolve short or small proteins called peptides as well as specific prote...

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...enzymes is much less guided process.

Future research will involve continuing to optimize the enzyme’s activity, i.e., seeing if they can get it to catalyze RNA ligation even faster.

Sources Cited

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Seelig, Burckhard, and Jack W. Szostak. "Selection and evolution of enzymes from a partially randomized non-catalytic scaffold." Nature 448 (Aug. 2007): 828-833.

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