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Updated: Apr 17, 2026

Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes
Published on: October 3, 2019
Improved Synthesis of Biotinol-5'-AMP: Implications for Antibacterial Discovery
William Tieu1, Steven W Polyak2, Ashleigh S Paparella3
1School of Chemistry and Physics, University of Adelaide , Adelaide, South Australia 5005, Australia ; Centre for Molecular Pathology, The University of Adelaide , Adelaide, South Australia 5005, Australia.
Abstract:
An improved synthesis of biotinol-5'-AMP, an acyl-AMP mimic of the natural reaction intermediate of biotin protein ligase (BPL), is reported. This compound was shown to be a pan inhibitor of BPLs from a series of clinically important bacteria, particularly Staphylococcus aureus and Mycobacterium tuberculosis, and kinetic analysis revealed it to be competitive against the substrate biotin. Biotinol-5'-AMP also exhibits antibacterial activity against a panel of clinical isolates of S. aureus and M. tuberculosis with MIC values of 1-8 and 0.5-2.5 μg/mL, respectively, while being devoid of cytotoxicity to human HepG2 cells.
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