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    <!-- http://purl.obolibrary.org/obo/UPa_UPA00100 -->

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        <rdfs:label>bacilysin biosynthesis</rdfs:label>
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        <ns3:IAO_0000115>Biosynthesis of bacilysin (L-alanyl-(2.3-epoxycyclohexanone-4)-L-alanine). This dipeptide is one of the simplest peptide antibiotics known. It displays activity against some bacteria and fungi (Kenig and Abraham 1976; Tschen 1990). Its proposed amino-acid ligase mode of biosynthesis might offer strategies to engineer new derivatives with improved properties. Bacilysin contains an L-alanine residue at the N terminus and a non-proteinogenic amino acid, Lanticapsin, at the C terminus (Walker and Abraham 1970). Its antibiotic activity depends on the anticapsin moiety, which becomes released by peptidases (Kenig et al. 1976; Chmara et al. 1982) after bacilysin uptake into susceptible cells by a distinct peptide permease system (Perry and Abraham 1979; Chmara et al. 1981). The intracellular anticapsin then blocks the glucosamine synthetase, and hence, bacterial peptidoglycan or fungal mannoprotein biosynthesis. This leads to cell protoplasting and lysis (Whitnney and Funderburk 1970; Kenig et al. 1976; Chmara et al. 1982; Chmara 1985; Milewski 1993).</ns3:IAO_0000115>
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