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KMID : 0603820070130030169
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Journal of Experimental & Biomedical Science
2007 Volume.13 No. 3 p.169 ~ p.173
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Phosphoryl Transferring Activity was Revealed from F_1-ATPase of Escherichia coli by {31}P NMR Investigation
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Sohn Joon-Hyung
NamKung Jun
Yoon Joon-Ho
Yeh Byung-Il
Choi Jong-Whan
Kim Hyun-Won
Woo Mi-Kyoung
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Abstract
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[{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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KEYWORD
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{31}P NMR spectroscopy, F_1-ATPase of Escherichia coli, Adenylate kinase activity, Methyl phosphate, Phosphoryl transferring activity
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