Penicillin Research Paper

An enzyme inhibitor works by binding to an enzyme to decrease the activity of the enzyme. Many drugs are enzyme inhibitors because they have the ability to kill pathogens or correct a metabolic imbalance. The enzyme inhibitor that I chose to write about is the drug penicillin, which most of us are probably very familiar with as being used as an antibiotic. It was the first antibiotic to be used medically (Newman, 2017). There are both natural and synthetic types of penicillin that are used today. “The basic structure of all penicillins, natural and semisynthetic, is 6-aminopenicillanic acid composed of a four membered heterocyclic β-lactam ring fused with a five membered (benzylpenicillin), penicillin V (Phenoxymethyl penicillin), thiazolidine ring” (Garg, n.d., para. 4). According to Garg, the β-lactam ring appears to be required in order for penicillin to function as needed (n.d.).

Peptidoglycan is an element of the composition of bacterial cell walls that supplies a rigid firmness (Guzman, n.d.). In short, the synthesis of the peptidoglycan is broken down into three parts. During the last stage of the biosynthesis of peptidoglycan, the β-lactam ring comes into play. It takes part in making sure the formation of the peptidoglycan does not occur (Guzman, n.d.). “Penicillin kills bacteria through binding of the beta-lactam ring to DD-transpeptidase, inhibiting its cross-linking activity and preventing new cell wall formation” (Chow, 2015, para. 3). As the cell walls divide, small holes are opened up. Typically during cell division, these holes are refilled by the new peptidoglycans. However, when penicillin inhibits this new cell wall formation, the difference in pressure causes water to rush into these holes and eventually bursts the bacterium (Newman,