... include chymotrypsin, elastase and trypsin. Proteases catalyse peptide bonds in polypeptides and proteins and according to Mathews et al (2000) serine proteases are distinct because they all have a serine residue that plays a critical role in the catalytic process. These serine proteases all have a similar three-dimensional structure with an aspartate, histidine and serine residue clustered about the active region. There is also always a pocket located close to the active region and according to Mathews et al (2000) the nature of this pocket gives each serine protease its specificity. For example, trypsin has a deep and narrow negatively charged pocket to attract positively charged long ions and chymotrypsin has a pocket that is lined with hydrophobic residues to attract hydrophobic compounds, see figure 1. The hydrolysis of a peptide bond by chymotrypsin has six steps, see figure 2. Firstly, the hydrophobic polypeptide substrate binds noncovalently to chymotrypsin pocket (stage ...

See this essay or coursework document in full right now