منابع مشابه
ATP synthase in mycobacteria: special features and implications for a function as drug target.
ATP synthase is a ubiquitous enzyme that is largely conserved across the kingdoms of life. This conservation is in accordance with its central role in chemiosmotic energy conversion, a pathway utilized by far by most living cells. On the other hand, in particular pathogenic bacteria whilst employing ATP synthase have to deal with energetically unfavorable conditions such as low oxygen tensions ...
متن کاملMycobacterial CYP121 as a target for anti-TB drug discovery
Despite the introduction of the first line treatment regimen forty years ago and the continuous trials since that time to introduce new regimens, tuberculosis (TB) is considered to be the cause of considerable mortality worldwide. Recent research highlighted the Mycobacterium tuberculosis (Mtb)CYP450s as potential drug targets. This article reviews mycobacterial CYP121 as a target for anti-TB d...
متن کاملProbing the Interaction of the Diarylquinoline TMC207 with Its Target Mycobacterial ATP Synthase
Infections with Mycobacterium tuberculosis are substantially increasing on a worldwide scale and new antibiotics are urgently needed to combat concomitantly emerging drug-resistant mycobacterial strains. The diarylquinoline TMC207 is a highly promising drug candidate for treatment of tuberculosis. This compound kills M. tuberculosis by binding to a new target, mycobacterial ATP synthase. In thi...
متن کاملBedaquiline Targets the ε Subunit of Mycobacterial F-ATP Synthase
The tuberculosis drug bedaquiline inhibits mycobacterial F-ATP synthase by binding to its c subunit. Using the purified ε subunit of the synthase and spectroscopy, we previously demonstrated that the drug interacts with this protein near its unique tryptophan residue. Here, we show that replacement of ε's tryptophan with alanine resulted in bedaquiline hypersusceptibility of the bacteria. Overe...
متن کاملRespiratory ATP synthesis as drug target for combating tuberculosis
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2010
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2010.04.099