Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli | Zendy

Philip E. Brandish | Zendy; Kenichi Kimura | Zendy; M Inukai | Zendy; Robert Southgate | Zendy; John T. Lonsdale | Zendy; Timothy D. H. Bugg | Zendy

Open Access

Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli

Author(s) -

Philip E. Brandish,

Kenichi Kimura,

M Inukai,

Robert Southgate,

John T. Lonsdale,

Timothy D. H. Bugg

Publication year - 1996

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.40.7.1640

Subject(s) - pentapeptide repeat , tunicamycin , non competitive inhibition , biochemistry , translocase , escherichia coli , chemistry , substrate (aquarium) , enzyme , biology , stereochemistry , peptide , ecology , chromosomal translocation , unfolded protein response , endoplasmic reticulum , gene

Using a continuous fluorescence-based enzyme assay, we have characterized the antibacterial agents tumicamycin and liposidomycin B as inhibitors of solubilized Escherichia coli phospho-N-acetylmuramyl-pentapeptide translocase. Tunicamycin exhibited reversible inhibition (Ki = 0.55 +/- 0.1 microM) which was noncompetitive with respect to the lipid acceptor substrate and competitive with respect to the fluorescent substrate analog, dansyl-UDPMurNAc-pentapeptide. Liposidomycin B exhibited slow-binding inhibition (Ki = 80 +/- 15 nM) which was competitive with respect to the lipid acceptor substrate and noncompetitive with respect to dansyl-UDPMurNAc-pentapeptide. These results provide insight into the molecular mechanisms of action of these two classes of nucleoside antibiotics.

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