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Fluoride Effects along the Reaction Pathway of Pyrophosphatase: Evidence for a Second Enzyme·Pyrophosphate Intermediate

Baykov, Alexander A., Fabrichniy, Igor P., Pohjanjoki, Pekka, Zyryanov, Anton B., Lahti, Reijo·2000·Biochemistry
DOI 10.1021/bi000627u
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Abstract

The fluoride ion is a potent and specific inhibitor of cytoplasmic pyrophosphatase (PPase). Fluoride action on yeast PPase during PP(i) hydrolysis involves rapid and slow phases, the latter being only slowly reversible [Smirnova, I. N., and Baykov, A. A. (1983) Biokhimiya 48, 1643-1653]. A similar behavior is observed during yeast PPase catalyzed PP(i) synthesis. The amount of enzyme.PP(i) complex formed from solution P(i) exhibits a rapid drop upon addition of fluoride, followed, at pH 7.2, by a slow increase to nearly 100% of the total enzyme. The slow reaction results in enzyme inactivation, which is not immediately reversed by dilution. These data show that fluoride binds to an enzyme.PP(i) intermediate during the slow phase and to an enzyme.P(i) intermediate during the rapid phase of the inhibition. In Escherichia coli PPase, the enzyme.PP(i) intermediate binds F(-) rapidly, explaining the lack of time dependence in the inhibition of this enzyme. The enzyme.PP(i) intermediate formed during PP(i) hydrolysis binds fluoride much faster (yeast PPase) or tighter (E. coli PPase) than the similar complex existing at equilibrium with P(i). It is concluded that PPase catalysis involves two enzyme.PP(i) intermediates, of which only one (immediately following PP(i) addition and predominating at acidic pH) can bind fluoride. Simulation experiments have indicated that interconversion of the enzyme.PP(i) intermediates is a partially rate-limiting step in the direction of hydrolysis an…

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  • F− salts inhibit enolase and F-ATPase, and also exert an inhibitory impact on pyrophosphatases and catalases.

    “A critical example of this sort is the inhibition of both enolase and F‐ATPase, although F− salts also exert an inhibitory impact on pyrophosphatases and catalases (Baykov et al., 2000; Li, 2003; Ma et al., 2014; Marquis et al., 2003; Qin et al., 2006; Samygina et al., 2007; Wackett, 2021b, 2021c).”

    From Role of the CrcB transporter of Pseudomonas putida in the multi‐level stress response elicited by mineral fluoride (2022) · cites this paper as Baykov et al., 2000

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Research works printed but not linked: 38

  1. Kornberg A., 1962, in Horizons in Biochemistry
  2. Cooperman B. S., 1992, Trends Biochem. Sci. 17, 262−266
  3. Baykov A. A., 1999, Prog. Mol. Subcell. Biochem. 23, 127−150
  4. Kunitz M., 1952, J. Gen. Physiol., 35, 10.1085/jgp.35.3.423 · DOI
  5. Baykov A. A., 1973, Eur. J. Biochem., 32, 10.1111/j.1432-1033.1973.tb02589.x · DOI
  6. Welsh K. M., 1983, Biochemistry 22, 2243−2248
  7. Baykov A. A., 1990, Eur. J. Biochem., 194, 10.1111/j.1432-1033.1990.tb19482.x · DOI
  8. Gonzalez M. A., 1984, Biochemistry 23, 797−801
  9. Janson C. A., 1979, J. Biol. Chem., 254, 10.1016/S0021-9258(18)50649-9 · DOI
  10. Hewitt E. J., 1963, in Metabolic Inhibitors
  11. Smith F. A., 1970, Handbook of Experimental Pharmacology, 2
  12. Pinkse M. W. H., 1999, Biochemistry 38, 9926−9936
  13. Smirnova I. N., 1983, Biokhimiya 48, 1643−1653
  14. Baykov A. A., 1992, Arch. Biochem. Biophys. 294, 238−243
  15. Avaeva S. M., 1999, Biochemistry (Moscow) 64, 169−174
  16. Morrisson J. F., 1988, Adv. Enzymol. Relat. Areas Mol. Biol. 61, 201−301
  17. Baykov A. A., 1977, Biochim. Biophys. Acta, 481
  18. Baykov A. A., 1979, Biochim. Biophys. Acta, 569
  19. Kurilova S. A., 1984, Bioorg. Khim. 10, 1153−1160
  20. Avaeva S., 1996, FEBS Lett., 399, 102, 10.1016/S0014-5793(96)01296-3 · DOI
  21. Heikinheimo P., 1996, Eur. J. Biochem., 239, 10.1111/j.1432-1033.1996.0138u.x · DOI
  22. Kolakowski L. F., Jr., 1988, Nucleic Acids Res. 16, 10441−10452
  23. Bradford M. M., 1976, Anal. Biochem. 72, 248−254
  24. Salminen T., 1995, Biochemistry 34, 782−791
  25. Wong S. C. K., 1970, J. Biol. Chem., 245
  26. Baykov A. A., 1981, Anal. Biochem., 116, 4, 10.1016/0003-2697(81)90313-4 · DOI
  27. Nýren P., 1985, Anal. Biochem. 151, 504−509
  28. Fabrichniy I. P., 1997, Biochemistry 36, 7746−7753
  29. Aziz A., 1969, Anal. Chim. Acta, 47, 56, 10.1016/S0003-2670(01)81804-3 · DOI
  30. Kohlrausch F., 1908, Z. Phys. Chem. 64, 129−169
  31. Baykov A. A., 1976, Biochim. Biophys. Acta, 429
  32. Springs B., 1981, Biochemistry 20, 6384−6391
  33. Baykov A. A., 1992, Eur. J. Biochem., 206, 10.1111/j.1432-1033.1992.tb16948.x · DOI
  34. Kasho V. N., 1989, Biochem. Biophys. Res. Commun. 161, 475−480
  35. Hackney D. D., 1980, J. Biol. Chem., 255, 10.1016/S0021-9258(19)70789-3 · DOI
  36. Huang C. Y., 1979, Methods Enzymol., 63, 84, 10.1016/0076-6879(79)63007-0 · DOI
  37. Cleland W. W., 1975, Biochemistry 14, 3220−3224
  38. Abbreviations, Escherichia coli PPase

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Metadata

Authors
Baykov, A. A., Fabrichniy, I. P., Pohjanjoki, P., Zyryanov, A. B., & Lahti, R.
Affiliations
A. N. Belozersky Institute of Physico-Chemical Biology and School of Chemistry, Moscow State University, Moscow 119899, Russia, and Department of Biochemistry, University of Turku, FIN-20014 Turku, Finland
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2000-09-02
Volume
39
Issue
39
Pages
11939-11947
ISSN
  • 0006-2960
  • 1520-4995
DOI
10.1021/bi000627u
Cited by
44
References
0
Language
en

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