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Streptomyces tubercidicus ME-9189 균주가 생산하는 nucleoside계 제초 활성 물질
김원곤,김종평,김창진,유익동 한국미생물생명공학회 ( 구 한국산업미생물학회 ) 1996 한국미생물·생명공학회지 Vol.24 No.1
방선균으로부터 제초활성 물질을 탐색하던 중 쇠비름과 바랭이에 대하여 강한 제초활성을 갖는 균주를 선발하여, 그 균주가 생산하는 활성물질을 분리 정제한 후 구조를 결정하고 정제된 물질에 대한 활성을 조사하였다. 선발된 ME-9189 균주의 미생물학적 특성을 조사한 결과 본 균주는 Streptomyces tubercidicus로 동정되어 본 균주를 Streptomyces tubercidicus ME-9189로 명명하였다. 또한 균 배양 상등액으로부터 활성탄, silica gel, sephadex LH-20 column chromatography 및 재결정화를 통하여 제초활성 물질 ME-9189 화합물을 정제한 후 UV, ^1H 및 ^13C-NMR, EIMS 등의 기기분석을 한 결과 본 물질을 tubercidin(4-amino-7β-D-ribofuranosyl-7H-pyrrolo[2,3-d]pyrimidine)으로 동정하였다. Tubercidin은 10ppm의 농도에서 무우의 발아후 생육을 50% 저해하였으며, herbicidin A보다 약 2배 강한 활성을, toyocamycin과는 비슷한 활성을 나타내었다. Three thousand microbial strains collected from different sources were screened for herbicidal activity. A strain of ME-9189 showed herbicidal activity against Digitaria sanguinalis and Portulaca oleracea was isolated from a mountainy soil. Based on taxonomic studies, the strain was identified as Streptomyces tubercidicus. The active compound of ME-9189 was purified from the culture broth by charcoal. silica gel, sephadex LH-20 column chromatography and crystalization, consecutively. The ME-9189 compound was identified as tubercidin by spectroscopic methods of UV, ^1H and ^13C-NMR, and EIMS. In the bioassay, growth of radish shoot and root was inhibited by 50% with tubercidin treatment of 10 ppm, showing 2 times higher activity than that of herbicidin A and similar to that of toyocamycin.
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Streptomyces tubercidicus에서 glutamine phosphoribosylpyrophosphate amidotransferase의 정제 및 특성
하영칠,유진철 한국미생물학회 1991 미생물학회지 Vol.29 No.2
Glutamine phosphoribosylpyrophosphate amidotransferase of Streptomyces tubercidicus was purified and characterized. Molecular weight of the isolated enzyme was determined to be approximately 230,000 and was composed foru identical subunits having a molecular weight of 58,000. This enzyme was strongly inhibited by AMP while considerably inhibited by ATP and GTP. Inhibition effect of enzyme activity by AMP was antagonized by increased concentration of substrate, PRPP, and metal ion (especially, $Mg^{++}$) was essential in both catalytic activity and nucleotide inhibition of this enzyme. Therefore, it was confirmed that end product inhibition of glutamine phosphoribosylpyrophosphate amidotransferase by adenine participated in the regulation of tubercidin biosynthesis from Streptomyces tubercidicus.s.
ScienceON
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