首页> 外文期刊>Bulletin of the Korean Chemical Society >P NMR Spectroscopy Revealed Adenylate kinase-1 ike Activity and Phosphotransferase-like Activity from F1-ATPase of Escherichia coli
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P NMR Spectroscopy Revealed Adenylate kinase-1 ike Activity and Phosphotransferase-like Activity from F1-ATPase of Escherichia coli

机译:P NMR光谱显示大肠杆菌F1-ATPase的腺苷酸激酶1 ike活性和磷酸转移酶样活性

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摘要

Adenylate kinase-like activity and phosphotransferase-like activity from F1-ATPase of Escherichia coli was revealed by ~(31)P NMR spectroscopy. Incubation of Fi-ATPase with ADP in the presence of Mg~(2+) shows the appearance of ~(31)P resonances from AMP and Pi, suggesting generation of AMP and ATP by adenylate kinase-like activity and the subsequent hydrolysis to Pi. Incubation of Fi-ATPase with ADP in the presence of methanol shows additional peak from methyl phosphate, suggesting phosphotransferase-like activity of Fi-ATPase. Both adenylate kinase-like activity and phosphotransferase-like activity has not been reported from Fi-ATPase of Escherichia coli. ~(31)P NMR could be a valuable tool for the investigation of phosphorous related enzyme.
机译:〜(31)P NMR光谱揭示了大肠杆菌F1-ATPase的腺苷酸激酶样活性和磷酸转移酶样活性。在Mg〜(2+)存在下,Fi-ATPase与ADP的孵育显示AMP和Pi出现〜(31)P共振,表明通过腺苷酸激酶样活性产生AMP和ATP,随后水解为Pi 。在甲醇存在下,将ADP与Fi-ATPase一起温育显示出来自甲基磷酸的另一个峰,表明Fi-ATPase的磷酸转移酶样活性。尚未从大肠杆菌的Fi-ATP酶报道腺苷酸激酶样活性和磷酸转移酶样活性。 〜(31)P NMR可能是研究磷相关酶的有价值的工具。

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