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Rhizocticins — New phosphono‐oligopeptides with antifungal activity
Author(s) -
Rapp Claudius,
Jung Günther,
Kugler Martin,
Loeffler Wolfgang
Publication year - 1988
Publication title -
liebigs annalen der chemie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 0170-2041
DOI - 10.1002/jlac.198819880707
Subject(s) - tripeptide , chemistry , stereochemistry , antifungal , bacillus subtilis , peptide , amino acid , residue (chemistry) , oligopeptide , enantiomer , enzyme , serine , biochemistry , bacteria , microbiology and biotechnology , biology , genetics
The widely used and well‐known bacterial strain Bacillus subtilis ATCC 6633 was found to produce two novel, antifungal hydrophilic peptide antibiotics, L ‐arginyl‐ L ‐2‐amino‐5‐phosphono‐3‐ cis ‐pentenoic acid ( L ‐Arg‐ L ‐APPA, rhizocticin A) and L ‐valyl‐ L ‐arginyl‐ L ‐2‐amino‐5‐phosphono‐3‐ cis ‐pentenoic acid ( L ‐Val‐ L ‐Arg‐ L ‐APPA, rhizocticin B). Besides rhizocticin A and B, the main components, small amounts of related tripeptides were detected. Instead of the L ‐Val of rhizocticin B they contain L ‐Ile or L ‐Leu and are referred to as rhizocticins C and D, respectively. The C‐terminal residue was identified by NMR spectroscopy as the unsaturated phosphono amino acid L ‐APPA, known till now only as D enantiomer. Enzymatic cleavages of rhizocticin B yielded both L ‐APPA and rhizocticin A.