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[9] [10] If rifamycin binds the polymerase after the chain extension process has started, no inhibition is observed on the biosynthesis, consistent with a steric-occlusion mechanism. Single step high level resistance to the rifamycins occurs as the result of a single amino acid change in the bacterial DNA dependent RNA polymerase.
Rifampicin, also known as rifampin, is an ansamycin antibiotic used to treat several types of bacterial infections, including tuberculosis (TB), Mycobacterium avium complex, leprosy, and Legionnaires' disease. [3]
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Rifaximin is a semisynthetic broad spectrum antibacterial drug, derived through chemical modification of the natural antibiotic rifamycin. [29] It has very low bioavailability due to its poor absorption after oral administration.
Rifapentine, sold under the brand name Priftin, is an antibiotic used in the treatment of tuberculosis. [2] In active tuberculosis it is used together with other antituberculosis medications. [2]
For Mycobacterium tuberculosis, the rifamycin-resistant mutations most commonly encountered involve codons 516, 526, and 531 (numbered, by convention, as in Escherichia coli rpoB). [ 11 ] [ 12 ] These mutations result in high rifampicin resistance with a relatively low loss of fitness. [ 8 ]
In enzymology, a rifamycin-B oxidase (EC 1.10.3.6) is an enzyme that catalyzes the chemical reaction rifamycin B + O 2 ⇌ {\displaystyle \rightleftharpoons } rifamycin O + H 2 O 2 Thus, the two substrates of this enzyme are rifamycin B and O 2 , whereas its two products are rifamycin O and H 2 O 2 .
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