Evidence for Characterization of Lys5 Activity

Evidence for Characterization of Lys5 Activity
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Lysine is regarded as one of the building blocks of protein. It is one of the essential nucleic acids that ensures that the cell can produce the form and functions that it needs to ensure, not only to meet its everyday needs but also to ensure its long-term survival. However, another common function and use of lysine is muscle turnover and normal growth. Although less-known, scientists have long utilized techniques that would be able to make certain chemical changes regarding its biosynthesis.
In this article written by Ehmann, Gehring, and Walsh (1999), the fungal biosynthesis of lysine was done through common laboratory activities with the use of fungus as the main medium. Particularly, the authors have utilized the “enzymatic reduction of R-aminoadipate at C6 to the semialdehyde, which required two gene products in Saccharomyces cerevisiae, Lys2 and Lys5”.
First, the scientists tried use Coenzyme A samples directly as a substrate by crushing it and locating it. By doing this, they were able to use the coenzyme as a cosubstrate. These chemicals were then activated with the help of various other processes to ensure that they can be used for the next process – catalysis. However, due to need for a specific enzyme that would fuel this reaction, most catalyst were degraded the organic remains, and the scientists have utilized various techniques that could maximize the recovery of these matters, such as extraction and solid-phase extraction, among others CITATION Cla08 \l 1033 (Clancy, 2008). One of the processes that were done was the subcloning process of Lys2 from S. cerevisiae and the subsequent expression of the same matter from “Escherichia coli as a full-length 155-kDa enzyme, as a 105-kDa adenylation/peptidyl carrier protein (A/PCP) fragment (residues 1-924), and as a 14-kDa PCP fragment ...