|
type |
Journal Article |
authors |
Poetsch, M.; Zahner, H.; Werner, R. G.; Kern, A.; Jung, G. |
title |
Metabolic products from microorganisms. 230. Amiclenomycin-peptides, new antimetabolites of biotin. Taxonomy, fermentation and biological properties |
journal |
J Antibiot (Tokyo) |
Activity |
2.6.1.62 |
ui |
85234134 |
year |
(1985) |
volume |
38 |
number |
3 |
pages |
312-20. |
| |
keywords |
Aminobutyric Acids/isolation & purification/metabolism/pharmacology |
abstract |
Four new and two known peptide antibiotics containing amiclenomycin (Acm) have been isolated from a culture of Streptomyces venezuelae Tu 2460: L-MeIle-L-Acm (1), L-Ile-L-Acm (2), L-MeVal-L-Acm (3), L-MeIle-L- Acm-L-Gln (4), L-Ile-L-Acm-L-Gln (5) and L-Val-L-Acm-L-Gln (6). These di- and tripeptides exhibited antimicrobial activity on a minimal medium against Gram-negative bacteria, which could be reversed by biotin. It was shown that the antibiotics were decomposed by peptidases to provide amiclenomycin (7) after their uptake into cells of Escherichia coli via peptide-permeases. The antimicrobial activity of the amiclenomycin-peptides was the inhibition of DAPA-aminotransferase by the amiclenomycin-warhead, however, amiclenomycin itself was hardly transported into the cells. Since the amiclenomycin peptides misuse general transport systems, they are presented here as examples for the illicit transport concept. |
last changed |
2002/11/12 16:17 |
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