In silico determination of substrate spectrum of lactonases, hydrolyzing various N-acyl homoserine lactones

Aslanli, A.G.; Efremenko, E.N.

Авторы: Aslanli A.G., Efremenko E.N.
Журнал: IOP Conference Series: Materials Science and Engineering
Том: 848
Год издания: 2020
Издательство: -
Местоположение издательства: Krakow
Первая страница: 012006
DOI: 10.1088/1757-899X/848/1/012006
Аннотация: The rapid growth in the number of resistant pathogenic bacteria has led to a decreasein the effectiveness of the existing antimicrobial agents. N-acyl homoserine lactones (N-AHLs)are the key molecules responsible for the formation of antibiotic resistance of gram-negativebacteria. The combination of various lactonases, capable of hydrolyzing a wide range of NAHLs, with antibiotics, is one of the most appropriate ways to solve the problem ofmaintaining the effectiveness of the latter. The most interesting is the combination oflactonases with different substrate spectrum of action. In this study, using the moleculardocking method, we investigated the substrate range of various lactonases in order to selectenzymes suitable to combine with hexahistidine-tagged organophosphorus hydrolase (His6-OPH), for which high lactonase activity against a number of N-AHLs and the possibility ofcomplex formation with antibiotics have been shown previously. It was found that all thestudied lactonases hydrolyze predominantly long chain N-AHLs, while, among all studiedlactonases, the SsoPox enzyme from the class of phosphotriesterases-like lactonases was thebest candidate for the development of combined enzyme preparations.
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In silico determination of substrate spectrum of lactonases, hydrolyzing various N-acyl homoserine lactonesстатья

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