| Title | Streptomyces tubercidicus에서 glutamine phosphoribosylpyrophosphate amidotransferase의 정제 및 특성 | ||
| Author | 하영칠 · 유진철 | ||
| Address | 서울대학교 자연과학대학 미생물학과; 조선대학교 약학대학 약학과 * | ||
| Bibliography | Korean Journal of Microbiology, 29(2),97-103, 1991 | ||
| DOI | |||
| Key Words | Glutamine phosphoribosylpyrophosphate amidotransferase, purification, characterization, tubercidin, biosynthesis, Streptomyces tubercidicus | ||
| Abstract | 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. | ||
| Download PDF | Kor_290205_97-103p.pdf | ||