• Title/Summary/Keyword: AMLK-335

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Identification of Streptomyces sp. AMLK-335 Producing Antibiotic Substance Inhibitory to Vancomycin-Resistant Enterococci

  • Rhee, Ki-Hyeong;Choi, Kyung-Hee;Kim, Chang-Jin;Kim, Chang-Han
    • Journal of Microbiology and Biotechnology
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    • v.11 no.3
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    • pp.469-474
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    • 2001
  • The actinomycete strain AMLK-335 was antagonistic to vancomycin-resistant enterococci (VRE). Based on the diaminopimelic acid (DAP) type, and morphological and physiological characteristics revealed by scanning electron microscopy (SEM), AMLK-335 was confirmed to belong to the genus Streptomyces. Analysis of the 16S rDNA nucleotide sequences found AMLK-335 to have a relationship with Streptomyces platensis. The production of antibiotic from this strain was most favorable when cultured on glucose, polypeptone, yeast extract (PY) medium for 6 days at $27^{\circ}$. The antibiotic was identified as cyclo(L-phenylalanyl-L-prolyl) by comparing ti with the reported MS and NMR spectral data. Cyclo(phe-pro) from the PY cultures of AMLK-335 was most effective (K-98-258). Futhermore, cyclo(phe-pro) had antimicrobial activity against Bacillus subtilis, Microcuccs luteus, Staphylococcus aureus, and Saccharomyces cerevisiae, but it wa ineffective against Candida albicans, Streptomyces murinus, and Aspergillus niger.

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Inhibition of DNA Topoisomerase I by Cyclo(L-Prolyl-L-Phenylalanyl) Isolated from Streptomyces sp. AMLK-335

  • Rhee, Ki-Hyeong
    • Journal of Microbiology and Biotechnology
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    • v.12 no.6
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    • pp.1013-1016
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    • 2002
  • Cyclo(L-prolyl-L-phenylalanyl) [cyclo(pro-phe)] was isolated from Streptomyces sp. AMLK-335 and found to inhibit DNA topoisomerase I activity. In a DNA relaxation assay using supercoiled pBR322 DNA, cyclo(pro-phe) inhibited the DNA topoisomerase activity more strongly than camptothecin, a known topoisomerase inhibitor. However, at a concentration of $10{\mu}M$, cyclo(pro-phe) produced a lower degree of DNA relaxation than camptothecin, therefore, the inhibition of topoisomerase I activity by cyclo(pro-phe) was also found to be dose dependent. Accordingly, the current results suggest that cyclo(pro-phe) may be a novel inhibitor of topoisomerase I.