penicillinase

With his colleagues, he also discovered penicillinase, a penicillin-destroying enzyme that disclosed much about resistance to penicillin.

An example would be the bacteria that secrete penicillinase, which is an enzyme that destroys penicillin.

Additional studies are in progress to assess the susceptibility of the penicillinase activity observed in these strains to beta-lactamase inhibitors.

Search for a penicillinase ancestor has focused on the class of proteins that must be a priori capable of specific combination with penicillin.

Dicloxacillin is insensitive to beta-lactamase (also known as penicillinase) enzymes secreted by many penicillin-resistant bacteria.

In one such study, Dr. Axe looked at a protein, called penicillinase, that gives bacteria the ability to survive treatment with the antibiotic penicillin.

"Penicillinase" was discovered in 1940 and renamed Beta-lactamase when the structure of the Beta-lactam ring was finally elucidated.

Penicillinase-resistant β-lactam antibiotics, such as methicillin, nafcillin, oxacillin, cloxacillin, dicloxacillin, and flucloxacillin, are able to resist degradation by staphylococcal penicillinase.

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.

PENICILLINASE, No Molecular Class (not inhibited by clavulanic acid)

In 1962, the presence of penicillinase was detected in dormant Bacillus licheniformis endospores, revived from dried soil on the roots of plants, preserved since 1689 in the British Museum.

Staphylococcal resistance to penicillin is mediated by penicillinase (a form of β-lactamase) production: an enzyme that cleaves the β-lactam ring of the penicillin molecule, rendering the antibiotic ineffective.

It was suggested that penicillinase may have emerged as a defense mechanism for bacteria in their habitats, such as the case of penicillinase-rich Staphylococcus aureus, living with penicillin-producing Trichophyton, however this was deemed circumstantial.

Dr. Kenneth R. Miller, a professor of biology at Brown University and a frequent sparring partner of design proponents, said that in his study, Dr. Axe did not look at penicillinase "the way evolution looks at the protein."