التفاصيل البيبلوغرافية
| العنوان: |
Quinolone resistance-associated amino acid substitutions affect enzymatic activity of Mycobacterium leprae DNA gyrase. |
| المؤلفون: |
Yamaguchi, Tomoyuki, Nakajima, Chie, Suzuki, Yasuhiko, Yokoyama, Kazumasa |
| المصدر: |
Bioscience, Biotechnology & Biochemistry; Jul2017, Vol. 81 Issue 7, p1343-1347, 5p |
| مصطلحات موضوعية: |
QUINOLONE antibacterial agents, DNA topoisomerase II, MYCOBACTERIUM leprae genetics |
| مستخلص: |
Quinolones are important antimicrobials for treatment of leprosy, a chronic infectious disease caused byMycobacterium leprae.Although it is well known that mutations in DNA gyrase are responsible for quinolone resistance, the effect of those mutations on the enzymatic activity is yet to be studied in depth. Hence, we conductedin vitroassays to observe supercoiling reactions of wild type and mutatedM. lepraeDNA gyrases. DNA gyrase with amino acid substitution Ala91Val possessed the highest activity among the mutants. DNA gyrase with Gly89Cys showed the lowest level of activity despite being found in clinical strains, but it supercoiled DNA like the wild type does if applied at a sufficient concentration. In addition, patterns of time-dependent conversion from relaxed circular DNA into supercoiled DNA by DNA gyrases with clinically unreported Asp95Gly and Asp95Asn were observed to be distinct from those by the other DNA gyrases. DNA gyrase supercoiling activity largely changed by acquisition of quinolone resistance. [ABSTRACT FROM PUBLISHER] |
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| قاعدة البيانات: |
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