Protein Synthesis Essay

During protein digestion, a water molecule is added which breaks down the carbonyl-carbon-nitrogen sin the peptide bonds of proteins causing the liberation of amino acids. This process is referred to as proteolysis. Water molecules break down the carbonyl-carbon-nitrogen single bond (peptide bond) that holds single amino acid molecules together (Caroline Ritchie, 2013. This process is called hydrolysis and is catalysed by protease.
The three main protease enzymes produced during digestion are pepsin trypsin and cymotrypsin. Pepsin is released into the stomach and begins digestion by breaking down proteins into smaller molecules called peptides. Trypsin and cymotrypsin are released into the intestines completing protein digestion.There are fourmajor
They can be classed according to the type of proteases they inhibit and the way in which they carry out this inhibition. Those inhibitors that bind to protease with multiple non-covalent interactions without any reaction of the inhibitor itself is called a reversible inhibitor (Caroline Ritchie, 2013). The types of reversible inhibitors include competitive, uncompetitive and non – competitive (Caroline Ritchie, 2013). Irreversible inhibitors on the other hand form covalent bonds with the protease causing its active site to be altered. Protease inhibitors can be bought individually or as a cocktail containing multiple protease inhibitors at appropriate amounts (Caroline Ritchie, 2013)
Protease inhibitors can be used in medicine to treat different diseases and viruses which depend on protease for its mechanism of action. Protease inhibitors are most commonly used in the treatment of HIV/AIDS. Protease is responsible for the synthesis of new viral cells which would cause HIV to spread to uninfected cells. When the protease is introduced however, non-infectious vial particles are produced. The protease involved in HIV is called the HIV protease which is an aspartic protease (San Francisco General Hospital,