Fluorescein Analogues Inhibit SecA ATPase: The First Sub‐micromolar Inhibitor of Bacterial Protein Translocation | Zendy

Huang YingJu | Zendy; Wang Hongyun | Zendy; Gao FenBiao | Zendy; Li Minyong | Zendy; Yang Hsiuchin | Zendy; Wang Binghe | Zendy; Tai Phang C. | Zendy

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Fluorescein Analogues Inhibit SecA ATPase: The First Sub‐micromolar Inhibitor of Bacterial Protein Translocation

Author(s) -

Huang YingJu,

Wang Hongyun,

Gao FenBiao,

Li Minyong,

Yang Hsiuchin,

Wang Binghe,

Tai Phang C.

Publication year - 2012

Publication title -

chemmedchem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.817

H-Index - 100

eISSN - 1860-7187

pISSN - 1860-7179

DOI - 10.1002/cmdc.201100594

Subject(s) - chromosomal translocation , fluorescein , atpase , chemistry , biochemistry , biophysics , microbiology and biotechnology , biology , fluorescence , enzyme , gene , physics , quantum mechanics

SecA is a central component of the general secretion system that is essential for bacterial growth and thus an ideal target for antimicrobial agents. A series of fluorescein analogues were first screened against the ATPase activity using the truncated unregulated SecA catalytic domain. Rose bengal (RB) and erythrosin B (EB) were found to be potent inhibitors SecA with IC 50 values of 0.5 μ M and 2 μ M , respectively. RB and EB inhibit the catalytic SecA ATPase more effectively than the F 1 F 0 ‐proton ATPase. We used three assays to test the effect of these compounds on full‐length SecA ATPase: in solution (intrinsic ATPase), in membrane preparation, and translocation ATPase. RB and EB show the following trend in terms of IC 50 values: translocation ATPase

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