A common antibiotic called rifampicin, used to treat tuberculosis, leprosy, and Legionnaire's disease, is becoming less effective as the bacteria that cause the diseases develop more resistance.
One of the mechanisms leading to rifampicin's resistance is the action of the enzyme Rifampicin monooxygenase.
Pablo Sobrado, a professor of biochemistry in the College of Agriculture and Life Sciences, and his team used a special technique called X-ray crystallography to describe the structure of this enzyme. They also reported the biochemical studies that allow them to determine the mechanisms by which the enzyme deactivates this important antibiotic.
The enzyme, Rifampicin monooxygenase, is a flavoenzyme -- a family of enzymes that catalyze chemical reactions that are essential for microbial survival. These latest findings represent the first detailed biochemical characterization of a flavoenzyme involved in antibiotic resistance.
Details on the latest research can be found in the following papers:
Heba Abdelwahab, Julia S. Martin Del Campo, Yumin Dai, Camelia Adly, Sohby El-Sohaimy, Pablo Sobrado. Mechanism of Rifampicin Inactivation in Nocardia farcinica. PLOS ONE, 2016; 11 (10): e0162578 DOI:10.1371/journal.pone.0162578
Posted by Dr. Tim Sandle