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31P NMR Spectroscopy Revealed Adenylate kinase-like Activity and Phosphotransferase-like Activity from F1-ATPase of Escherichia coli

  • Kim, Hyun-Won (Department of Biochemistry and Institute of Basic Medical Science, Yonsei University)
  • Received : 2010.10.19
  • Accepted : 2010.11.10
  • Published : 2011.01.20

Abstract

Adenylate kinase-like activity and phosphotransferase-like activity from $F_1$-ATPase of Escherichia coli was revealed by $^{31}P$ NMR spectroscopy. Incubation of F1-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 $F_1$-ATPase with ADP in the presence of methanol shows additional peak from methyl phosphate, suggesting phosphotransferase-like activity of $F_1$-ATPase. Both adenylate kinase-like activity and phosphotransferase-like activity has not been reported from $F_1$-ATPase of Escherichia coli. $^{31}P$ NMR could be a valuable tool for the investigation of phosphorous related enzyme.

Keywords

References

  1. Senior, A. E.; Wise, J. G. J. Membr. Biol. 1983, 73, 105. https://doi.org/10.1007/BF01870434
  2. Senior, A. E. Physiol. Revs. 1988, 68, 177. https://doi.org/10.1152/physrev.1988.68.1.177
  3. Futai, M.; Noumi, T.; Maeda, M. Ann. Rev. Biochem. 1989, 8, 111.
  4. Penefsky, H. S.; Cross, R. Adv. Enzymol. 1991, 64, 173.
  5. Cross, R. L.; Nalin, C. M. J. Biol. Chem. 1982, 257, 2874.
  6. Senior, A. E. J. Bioenerg. Biomembr. 1992, 24, 479. https://doi.org/10.1007/BF00762365
  7. Boyer, P. D. Biochim. Biophys. Acta 1993, 1140, 215. https://doi.org/10.1016/0005-2728(93)90063-L
  8. Abrahams, J. P.; Leslie, A. G. W.; Lutter. R.; Walker, J. E. Nature 1994, 370, 621. https://doi.org/10.1038/370621a0
  9. Perlin, D. S.; Latchney, L. R.; Wise, J. G.; Senior, A. E. Biochemistry 1984, 23, 4998. https://doi.org/10.1021/bi00316a026
  10. Wise, J. G.; Duncan, T. M.; Latchney, L. R.; Cox, D. N.; Senior, A. E. Biochemical. J. 1983, 21, 343.
  11. Moudrianakis, E. N.; Tiffert, M. A. J. Biol. Chem. 1976, 251, 7796.
  12. Carr, M.; Mulvery, D.; Willis, A.; Ferguson, S. J.; Campbell, I. D. Biochim. Biophys. Acta 1990, 1015, 79. https://doi.org/10.1016/0005-2728(90)90218-S
  13. Jung, S.; Kim, H.-W. J. Biochem. Mol. Biol. 1998, 31, 33.
  14. Lee, H. W.; Sohn, J. H.; Yeh, B. I.; Choi, J. W.; Kim, H.-W. J. Biochem. 1998, 1271, 1053.
  15. Yoon, J.; Sohn, J. H.; Lee, H-W.; Yeh, B. I.; Choi, J. W.; Jung, S.; Kim, H.-W. Bull. Korean Chem. Soc. 2001, 22, 90.
  16. Choi, J. W.; Lee, Y. B.; Sohn, J. H.; Jun, N.; Yeh, B. I.; Kim, H.-W. Bull. Korean Chem. Soc. 2001, 29, 2499.
  17. Ting, L. P.; Wang, J. J. Biochemistry 1980, 19, 5665. https://doi.org/10.1021/bi00566a001
  18. Bradford, M. M. Anal. Biochem. 1994, 72, 248. https://doi.org/10.1016/0003-2697(76)90527-3
  19. Jeong, B. C.; Kim, H. W.; Owen, S.; Dick, R. E.; Macaskie, L. Appl. Biochem. Biotechnol. 1994, 47, 21. https://doi.org/10.1007/BF02788672
  20. Drobindskaya, I. Y.; Kzlov, I. A.; Mirataliev, M. B.; Vulfosn, E. N. FEBS Lett. 1985, 182, 419. https://doi.org/10.1016/0014-5793(85)80346-X
  21. Yoshida, M.; Allison, W. S. J. Biol. Chem. 1986, 261, 5714.
  22. Vogel, P. D.; Cross, R. A. J. Biol. Chem. 1991, 266, 6101.
  23. Webb, M. R.; Grubmeyer, C.; Penefsky, H. S.; Trentham, D. R. J. Biol. Chem. 1980, 255, 24, 11637.

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