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    請使用永久網址來引用或連結此文件: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/25366

    題名: The S subunit of D-ornithine aminomutase from Clostridium sticklandii is responsible for the allosteric regulation in D-α-lysine aminomutase
    作者: Tseng, Cheng-Hsing;Yang, Cheng-His;Lin, Heng-Ju;Wu, Chun-hung;Chen, Hao-Ping
    貢獻者: 淡江大學化學學系
    關鍵詞: B12;Clostridium sticklandii;OraS
    日期: 2007-06-21
    上傳時間: 2009-12-01
    出版者: Oxford: Oxford University Press
    摘要: Ornithine and lysine are degraded in quite a similar way in Clostridium sticklandii. Both pathways involve adenosylcobalamin-dependent enzymes, d-ornithine 4,5-aminomutase and lysine 5,6-aminomutase. According to previous reports, lysine 5,6-aminomutase is an ATP-dependent allosteric enzyme with many different activators and inhibitors. However, recent studies indicate that ATP does not have a regulatory effect on the recombinant enzyme. To monitor the activity of lysine aminomutase, a novel capillary electrophoresis-based assay method was developed. The present results demonstrate that the S subunit of d-ornithine aminomutase, OraS, is capable of forming a complex with KamDE of lysine 5,6-aminomutase and restores the enzyme's ATP-dependent allosteric regulation. Not only does ATP lower the K(m) of the KamDE-OraS complex for adenosylcobalamin and pyridoxal phosphate, but also OraS protein alone lowers the K(m) of KamDE for adenosylcobalamin and pyridoxal phosphate. The activity of reconstituted enzyme can also be activated by ammonium ion as reported by Morley and Stadtman.
    關聯: FEMS Microbiology Letters 274(1), pp.148-153
    DOI: 10.1111/j.1574-6968.2007.00820.x
    顯示於類別:[化學學系暨研究所] 期刊論文


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