Biomedical Science Letters (대한의생명과학회지)

The Korean Society for Biomedical Laboratory Sciences (대한의생명과학회)
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Phosphoryl Transferring Activity was Revealed from $F_1-ATPase$ of Escherichia coli by $^{31}P$ NMR Investigation

  • Sohn, Joon-Hyung (Department of Biochemistry and Institute of Basic Medical Science, Wonju College of Medicine, Yonsei University) ;
  • NamKung, Jun (Department of Biochemistry and Institute of Basic Medical Science, Wonju College of Medicine, Yonsei University) ;
  • Yoon, Joon-Ho (Department of Biochemistry and Institute of Basic Medical Science, Wonju College of Medicine, Yonsei University) ;
  • Woo, Mi-Kyoung (Department of Biochemistry and Institute of Basic Medical Science, Wonju College of Medicine, Yonsei University) ;
  • Yeh, Byung-Il (Department of Biochemistry and Institute of Basic Medical Science, Wonju College of Medicine, Yonsei University) ;
  • Choi, Jong-Whan (Department of Biochemistry and Institute of Basic Medical Science, Wonju College of Medicine, Yonsei University) ;
  • Kim, Hyun-Won (Department of Biochemistry and Institute of Basic Medical Science, Wonju College of Medicine, Yonsei University)
  • Published : 2007.09.30
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Abstract

[ $^{31}PNMR$ ] spectroscopy revealed the adenylate kinase-like activity and the phosphotransferase activity from $F_1-ATPase$ of Escherichia coli. Incubation of $F_1-ATPase$ with ADP in the presence of $Mg^{2+}$ shows the appearance of $^{31}P$ resonances from AMP and Pi, suggesting the generation of AMP and ATP by adenylate kinase-like activity and the subsequent hydrolysis to Pi. Incubation of $F_1-ATPase$ with ADP in the presence of methanol shows additional peak from methyl phosphate, suggesting phosphotransferase activity of $F_1-ATPase$. Both adenylate kinase-like activity and the phosphotransferase activity has not been reported from $F_1-ATPase$ from Escherichia coli. $^{31}P$ NMR proved that it could be a valuable tool for the investigation of phosphorous related enzyme.

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