| The S subunit of D-ornithine aminomutase from Clostridium sticklandii is responsible for the allosteric regulation in D-α-lysine aminomutase | |
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| 學年 | 95 |
| 學期 | 2 |
| 出版（發表）日期 | 2007-06-21 |
| 作品名稱 | The S subunit of D-ornithine aminomutase from Clostridium sticklandii is responsible for the allosteric regulation in D-α-lysine aminomutase |
| 作品名稱（其他語言） | |
| 著者 | Tseng, Cheng-Hsing; Yang, Cheng-His ;Lin, Heng-Ju; Wu, Chun-hung; Chen, Hao-Ping |
| 單位 | 淡江大學化學學系 |
| 出版者 | Oxford: Oxford University Press |
| 著錄名稱、卷期、頁數 | FEMS Microbiology Letters 274(1), pp.148-153 |
| 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. |
| 關鍵字 | B12; Clostridium sticklandii; OraS |
| 語言 | en |
| ISSN | 0378-1097 |
| 期刊性質 | 國外 |
| 收錄於 | SCI |
| 產學合作 | |
| 通訊作者 | |
| 審稿制度 | |
| 國別 | GBR |
| 公開徵稿 | |
| 出版型式 | 紙本 電子版 |
| 相關連結 |
機構典藏連結 ( http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/25366 ) |
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