淡江大學機構典藏:Item 987654321/25366
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    Please use this identifier to cite or link to this item: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/25366


    Title: The S subunit of D-ornithine aminomutase from Clostridium sticklandii is responsible for the allosteric regulation in D-α-lysine aminomutase
    Authors: Tseng, Cheng-Hsing;Yang, Cheng-His;Lin, Heng-Ju;Wu, Chun-hung;Chen, Hao-Ping
    Contributors: 淡江大學化學學系
    Keywords: B12;Clostridium sticklandii;OraS
    Date: 2007-06-21
    Issue Date: 2009-12-01
    Publisher: Oxford: Oxford University Press
    Abstract: 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.
    Relation: FEMS Microbiology Letters 274(1), pp.148-153
    DOI: 10.1111/j.1574-6968.2007.00820.x
    Appears in Collections:[Graduate Institute & Department of Chemistry] Journal Article

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