A.G. Scientific is using this week to focus on what is considered to be an odd group of proteins in biology, namely a family of catalysts called Serine Proteases, also sometimes referred to as serpins, are each integral to the process of regulating enzymes. Until an enzyme becomes active, they idle patiently in surrounding glands and in specialized cells as a pre-cursor molecule, referred to as a zymogen, also sometimes called a proenzyme. These pre-cursor zymogen molecules become turned ON when Serine Proteases attack a single, specific peptide bond within the zymogen. The mechanism itself is highly precise, however, the process of activating one is irreversible and will occur once only in the entire life of that enzyme.
Research conducted by Kansas State University biochemists discovered that Stappholoccacus aureus secretes a family of proteins that prevent neutrophil serine proteases, or NSPs, from working properly â€” an important finding for understanding how infections become rooted.