View PDF Version
 
DOI: 10.1039/A603533G (Paper) Reference Section for: J. Chem. Soc., Perkin Trans. 1, 1997, 303-308

Glyceryl-ether monooxygenase [EC 1.14.16.5]. Part 9. Stereospecificity of the oxygenase reaction

(Note: The full text of this document is currently only available in the PDF Version )

Hiroyasu Taguchi, Bela Paal and Wilfred L. F. Armarego

Abstract

(2RS,1′R)-[1′-3H1 [hair space]]- and (2RS, 1′S)-[1′-3H1[hair space]]-Hexade cyloxypropane-1,2-diols (chimyl alcohols) have been prepared and their stereochemistry has been confirmed by synthesizing the [2H1[hair space]]-analogues using similar procedures. When they were used as substrates for glyceryl-ether monooxygenase from rat liver in the presence of oxygen and (RS)-6-methyl-5,6,7,8-tetrahydropterin as co-factor, the 1′S-isomer released 37% of its tritium into the aqueous buffer after 20 mins, whereas the 1′R-isomer released only 6.5% showing that the reaction was stereospecific for the pro-HS hydrogen atom of the glyceryl ether substrate. This was in agreement with the kinetic parameters of unlabelled-(2RS)-3-, (2RS, 1′R)-3-[1′-2H1[hair space]]-, (2RS, 1′S)-3-[1′-2H1]- and (2RS)-3-[1′,1′-2H2[hair space]]- hexadecyloxypropane-1,2-diols where the apparent Km values were about the same (49.4, 53.7, 49.3 and 54.0 µM respectively) but the apparent maximum velocities (Vmax in nmol min-1 mg-1 protein) of the first two substrates (37.5 and 37.5) were faster than for the latter two substrates (22.5 and 23.6), consistent with the pro-HS hydrogen atom being replaced by the hydroxy group and a primary deuterium isotope effect of ≈1.6.

References

  1. A. Tietz, M. Lindberg and M. Kennedy, J. Biol. Chem., 1964, 239, 4081 CAS.
  2. B. Kosar-Hashemi and W. L. F. Armarego, Biol. Chem., Hoppe-Seyler, 1993, 374, 9 CAS; W. L. F. Armarego and B. Kosar-Hashemi, Pteridines, 1992, 3, 95 Search PubMed.
  3. R. C. Pegler, C. Piantadosi and F. Snyder, Biochim. Biophys. Acta, 1967, 144, 633.
  4. L. A. Horrocks and M. Sharma, in Phospholipids, J. N. Hawthorne and G. B. Ansell, eds, Elsevier Biochemical Press, Amsterdam, 1982, p. 51 Search PubMed.
  5. B. Kosar-Hashemi, H. Taguchi and W. L. F. Armarego, Pteridines, 1994, 5, 1 Search PubMed.
  6. H. Taguchi, B. Paal and W. L. F. Armarego, Pteridines, 1995, 6, 45 Search PubMed.
  7. S. Kaufman, Proc. Natl. Acad. Sci., USA, 1963, 50, 1085 CAS; S. Kaufman, Adv. Enzymol., 1971, 35, 245 Search PubMed.
  8. C. Walsh, Enzymic Reaction Mechanisms, W. H. Freeman and Co, San Francisco, 1979, pp 114–116 Search PubMed.
  9. L. J. Morris, Biochem. J., 1970, 118, 681 CAS.
  10. L. J. Morris and C. Hitchcock, Eur. J. Biochem., 1968, 4, 146 CAS.
  11. E. Heinz, A. P. Tulloch and J. F. T. Spencer, J. Biol. Chem., 1969, 224, 882.
  12. M. Hayano, in Oxygenases, O. Hayaishi, ed., Academic Press, New York, 1962, pp. 217–219 Search PubMed.
  13. M. Hamberg, B. Samuelsson, I. Björkhem and H. Danielsson, in Molecular Mechanisms in Oxygen Activation, O. Hayaishi, ed., Academic Press, New York, 1974, pp. 29–85 Search PubMed.
  14. T. Galliard and P. K. Stumpf, J. Biol. Chem., 1966, 241, 5806 CAS.
  15. E. J. Corey and G. Schmidt, Tetrahedron Lett., 1979, 399 CrossRef CAS.
  16. M. M. Maidland, A. Tramontano and S. A. Zderic, J. Am. Chem. Soc., 1977, 99, 5211 CrossRef CAS.
  17. M. M. Maidland, S. Greer, A. Tramontano and S. A. Zderic, J. Am. Chem. Soc., 1979, 101, 2352 CrossRef CAS.
  18. H. C. Brown and G. G. Pai, J. Org. Chem., 1985, 50, 1384 CrossRef CAS.
  19. D. Arigoni and E. L. Eliel, Topics in Stereochemistry, 1969, 4, 107 Search PubMed and references therein.
  20. H. Gerlach and B. Zagalak, J. Chem. Soc., Chem. Commun., 1973, 274 RSC.
  21. E. Caspi and C. R. Eck, J. Org. Chem., 1977, 42, 767 CrossRef CAS.
  22. J. M. Schwab and J. B. Klassen, J. Am. Chem. Soc., 1984, 106, 7217 CrossRef CAS.
  23. W. W. Cleland, Methods Enzymol, 1979, 63, 103 CrossRef CAS.
  24. W. L. F. Armarego, A. Ohnishi and H. Taguchi, Biochem. J., 1986, 234, 335 CAS.
Click here to see how this site uses Cookies. View our privacy policy here.