미생물학회지 (Korean Journal of Microbiology)
- 제29권2호
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- Pages.97-103
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- 1991
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- 0440-2413(pISSN)
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- 2383-9902(eISSN)
Streptomyces tubercidicus에서 glutamine phosphoribosylpyrophosphate amidotransferase의 정제 및 특성
Purification and characterization of glutamine phosphoribosylpyrophosphate amidotransferase from streptomyces tubercidicus
초록
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,
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