The S subunit of D-ornithine aminomutase from Clostridium sticklandii is responsible for the allosteric regulation in D-α-lysine aminomutase
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
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