Broad-spectrum antibiotic their greater potential to disrupt a larger variety of normal human flora. After continued exposure to an antibiotic, bacteria may develop changes in their structure or function that make them resistant to the antibiotic. These resistant organisms will live, while the susceptible organisms will die, leaving the population of bacteria entirely resistant to a given antibiotics. For example, after the discovery of penicillin and its subsequent use to treat bacterial infections, bacteria were found to have begun producing an enzyme, penicillinase, which rendered the penicillin molecule inactive. In response to this newly-acquired resistance, newer penicillins were produced that could not
Β-lactam antibiotic lower "c" values (better binding to PBPs). By definition, all β-lactam antibiotics have a β-lactam ring in their structure. The effectiveness of these antibiotics relies on their ability to reach the PBP intact and their ability to bind to the PBP. Hence, there are two main modes of bacterial resistance to β-lactams: If the bacterium produces the enzyme β-lactamase or the enzyme penicillinase, the enzyme will hydrolyse the β-lactam ring of the antibiotic, rendering the antibiotic ineffective. (An example of such an enzyme is New Delhi metallo-beta-lactamase 1, discovered in 2009.) The genes encoding these enzymes may be inherently present