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KMID : 0364819910290020097
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Korean Journal of Microbiology
1991 Volume.29 No. 2 p.97 ~ p.103
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Purification and Characterization of Glutamine Phosphoribosylpyrophosphate Amidotransferase from Streptomyces tubercidicus
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Abstract
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1
Guutamine 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 four 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 Streplomyces tubercidicus.
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