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Amiclenomycin Peptides ‐ Isolation and Structure Elucidation of New Biotin Antimetabolites
Author(s) -
Kern Armin,
Kabatek Ursula,
Jung Günther,
Werner Rolf G.,
Poetsch Matthias,
Zähner Hans
Publication year - 1985
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.198519850502
Subject(s) - chemistry , tripeptide , pronase , peptide , stereochemistry , antibiotics , biochemistry , bacteria , amino acid , streptomyces , enzyme , trypsin , biology , genetics
Six peptide antibiotics were isolated from the culture filtrate of Streptomyces venezuelae Tü 2460. The 4‐amino‐2,5‐cyclohexadienyl ring of the amino acid amiclenomycin (Acm, 7 ) was found to be the essential structural element of the three dipeptides L‐MeIle‐L‐Acm ( 1 , stravidin S 3 ), L‐Ile‐L‐Acm ( 2 ), and L‐MeVal‐L‐Acm ( 3 , stravidin S 2 ) as well as the three tripeptides L‐MeIle‐L‐Acm‐L‐Gln ( 4 ), L‐Ile‐L‐Acm‐L‐Gln ( 5 ) and L‐Val‐L‐Acm‐L‐Gln ( 6 ). In addition L‐amiclenomycin ( 7 ) and L‐Acm‐L‐Gln ( 8 ) were obtained by enzymatic cleavage with pronase P. All eight antibiotics inhibit the growth of gram‐negative bacteria by blocking the biotin biosynthesis. A synergistic enhancement of the antibiotic action was found by a polypeptide L ( 9 ) also isolated from S. Venezuelae Tü 2460. Further screening Supplemented on correction(Nov. 7,1985). revealed, that the S. Venezuelae strain Tü 2605 produces the antibiotic L‐MeIle‐L‐Acm‐L‐Glu ( 10 ).