Studies of acyl-CoA dehydrogenase catalyzed allylic isomerization: A one-base or two-base mechanism?

Journal of the American Chemical Society

Volumn 118, Issue 45, 1996, Pages 10971-10979

  Dakoji, Srikanth ^a   Shin, Injae ^a   Becker, Donald F ^a   Stankovich, Marian T ^a   Liu, Hung Wen ^a  

^a University of Minnesota   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A DEHYDROGENASE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; MUTANT;

EID: 0029969133     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja962532e     Document Type: Article

References (65)

1. (a) Thorpe, C.; Matthews, R. G.; Williams, C. H. Biochemistry 1979, 18, 331.
2. (b) Ghisla, S.; Thorpe, C.; Massey, V. Biochemistry 1984, 23, 3154.
3. (c) Pohl, B.; Raichle, T.; Ghisla, S. Eur. J. Biochem. 1986, 160, 109.
4. (d) Ghisla, S. In Flavins and Flavoproteins; Bray, R. C., Engel, P. C., Mayhew, S. G., Eds.; Walter de Gruyter & Co.: Berlin, 1984; p 385 and references cited therein.
5. (a) Beinert, H. Enzymes 1963, 7, 447.
6. (b) Engel, P. C. In Chemistry and Biochemistry of Flavoenzymes; Müller, F., Ed.; CRC Press: New York, 1991; p 597.
7. (c) Schulz, H. In Fatty Acid Oxidation: Clinical, Biochemical, and Molecular Aspects; Tanaka, K., Coates, P. M., Eds.; Alan R. Liss: New York, 1990; p 23.
8. (a) Ghisla, S.; Engst, S.; Moll, M.; Bross, P.; Strauss, A.; Kim, J. J. P. In New Developments in Fatty Acid Oxidation; Coates, P. M., Tanaka, K., Eds.; Wiley-Liss: New York, 1992; p 127.
9. (b) Kim, J. J. P. In Flavins and Flavoproteins; Curti, B., Ronchi, S., Zanetti, G., Eds.; de Gruyter: New York, 1991; p 291.
10. (c) Kim, J. J. P.; Wang, M.; Djordjevic, S.; Paschke, R. In New Developments in Fatty Acid Oxidation; Coates, P. M., Tanaka, K., Eds.; Wiley-Liss: New York, 1992; p 111.
11. (d) Kim, J. J. P.; Wang, M.; Paschke, R. Proc. Natl. Acad. Sei. U.S.A. 1993, 90, 7523.
12. (e) Brass, P.; Engst, S.; Strauss, A. W.; Kelley, D. P.; Rasched, I.; Ghisla, S. J. Biol. Chem. 1990, 265, 7116.
13. (f) Becker, D. F.; Fuchs, J. A.; Banfield, D. K.; Walter, F. D.; MacGillivray, R. T. A.; Stankovich, M. T. Biochemistry 1993, 32, 10736.
14. (a) Fendrich, G.; Abeles, R. H. Biochemistry- 1982, 21, 6685.
15. (b) Cummings, J. G.; Thorpe, C. Biochemistry 1994, 33, 788.
16. (a) Powell, P. J.; Thorpe, C. Biochemistry 1988,27, 8022.
17. (b) Freund, K.; Mizzer, J. P.; Dick, W.; Thorpe, C. Biochemistry 1985, 25, 5996.
18. (c) Lundberg, N. N.; Thorpe, C. Arch. Biochem. Biopliys. 1993, 305, 454.
19. (a) Frerman, F. E.; Miziorko, H. M.; Beckmann, J. D. J. Biol. Chem. 1980. 255, 11192.
20. (b) Gomes, B.; Fendrich, G.; Abeles, R. H. Biochemistry 1981. 20, 1481.
21. The α-H exchange is due to the reversible deprotonation-reprotonation mediated by E367. However, the exchange of β-H is a result of reversible hydride transfer between the substrate anion and the flavin coenzyme, and it is the reduced flavin that undergoes proton exchange.
22. A few examples include: (a) Shokat, K.; Uno, T.; Schultz, P. G. J. Am. Chem. Soc. 1994, 116, 2261.
23. (b) Willson, M.; Lauth, N.; Perie, J.; Callens, M.; Opperdoes, F. R. Biochemistry 1994,33, 214.
24. (c) Kim, D. H.; Kirn, K. B. J. Am. Chem. Soc. 1991,113, 3200.
25. (d) Mühlbacher, M.; Poulter, C. D. Biochemistry 1988, 27, 7315.
26. (e) Pollack, R. M.; Bantia, S.; Bounds, P. L.; Koffman, B. M. Biochemistry 1986, 25, 1905.
27. (f) Kiorpes, T. C.; Hoerr, D.; Ho, W.; Weaner, L. E.; Inman, M. G.; Tutwiler, G. F. J. Biol. Chem. 1984, 259, 9750.
28. Payne, G. B.; Williams, P. H. J. Org. Chem. 1959, 24, 54.
29. (a) Belcher, M. Methods Enzymol. 1981, 72, 404.
30. (b) Lai, M.-t.; Liu, L.-d.; Liu, H.-w. J. Am. Chem. Soc. 1991, 113, 7863.
31. Eberhard, A. Chromatogram 1987, 8, 10.
32. (a) Engel, P. C.; Massey, V. Biochem. J. 1971, 125, 889.
33. (b) Williamson, G. Ph.D. Thesis, University of Sheffield, 1983.
34. Thorpe, C. Methods Enzymol. 1981, 71, 366.
35. Shin, I.; Li, D.; Becker, D. F.; Stankovich, M. T.; Liu, H.-w. J. Am. Chem. Soc. 1994, 116, 8843.
36. Marshall, J. A.; Jenson, T. M.; DeHoff, B. S. J. Org. Chem. 1987, 52, 3860.
37. Pons, D.; Savignac, M.; Genet, J.-P. Tetrahedron Lett. 1990, 5023.
38. Lai, M.-t.; Li, D.; Oh, E.; Liu, H.-w. J. Am. Chem. Soc. 1993, 115, 1619.
39. (a) Rathke, M. W.; Sullivan, D. Tetrahedron Lett. 1972, 4249.
40. (b) Martin, S. R; Tu, C.-y.; Chou, T.-s. J. Am. Chem. Soc. 1980, 102, 5274.
41. The substrate recognition residues in the active-site of AI. elsdenii SCAD were identified by crystal structural analysis of the enzymeacetoacetyl-CoA complex (Djordjevic, S.; Pace, C. P.; Stankovich, M. T.; Kim, J. J. P. Biochemistry 1995, 34, 2163).
42. (a) Osmundsen, H.; Sherratt, H. S. A. FEBS Lett. 1975, 55, 81.
43. (b) Kean, E. A. Biochem. Biophys. Ada 1976, 422, 81.
44. (c) Abeles, R. H. In Enyme Activated Irreversible Inhibitors; Seiler, N., Jung, M. J. KochWeser, J., Eds.; Elsevier-North Holland: Amsterdam, 1978; p 1.
45. (d) Ghisla, S.; Wenz, A.; Thorpe, C. In Enzyme Inhibitors; Brodbeck, U., Ed.; Verlag Chim: Weinheim, Germany, 1980; p 43.
46. (e) Wenz, A.; Thorpe, C.; Ghisla, S. J. Biol. Chem. 1981,256,9809.
47. (f) Ghisla, S.; Melde, K.; Zeller, H. D.; Boschert, W. In Fatty Add Oxidation; Clinical, Biochemical, and Molecular Aspects; Tanaka, K., Coates, P. M., Eds.; Alan R. Liss, Inc.: New York, 1990; p 185.
48. (a) Thorpe, C.; Massey, V. Biochemistry 1983,22,2972.
49. (b) Thorpe, C.; Ciardelli, T. L.; Stewart, C. J.; Wieland, Th. Eur. J. Biochem. 1981, 118, 279.
50. (c) Auer, H. E.; Frerman, F. E. J. Biol. Chem. 1980, 255, 8157.
51. Corey, E. J.; Fuchs, P. L. Tetrahedron Lett. 1972, 36, 3769.
52. For a good review of HMQC experiment, see: Martin, G. E.; Zektzer, A. S. Two-Dimensional NMR Methods for Establishing Molecular Connectivity; VCH Publishers: New York, 1988.
53. For general references, see: Silverman, R. B. Mechanism-based Enzyme Inactivation: Chemistry and Enzymology; CRC Press: Boca Raton, FL, 1988; Vols. I and II.
54. (a) Endo, K.; Helmkamp, G. M., Jr.; Block, K. J. Biol. Chem. 1970, 245, 4293.
55. (b) Schwab, J. M.; Ho, C.-K.; Li, W.-B.; Townsend, C. A.; Salituro, G. M. /. -4m. Chem, Soc. 1986, 106, 5309.
56. (a) Penning, T. M.; Talalay, P. J. Biol. Chem. 1981, 256, 6851.
57. (b) Penning, T. M.; Heller, D. N.; Balasubramanian, T. M.; Fenselau, C. C.; Talalay, P. J. Biol. Chem. 1982, 257, 12589.
58. Analysis of the X-ray crystal structure of the SCAD/acetoacetylCoA complex revealed a distance of 3.00 A between the nearest carboxylate oxygen (Ol) of Glu-367 and the pro-R α-H of the acyl thioester. Interestingly, the distance between the nearest carboxylate oxygen (O2) of Glu-367 and the γ-H of the inhibitor was measured as 2.84 A.
59. (a) Schwab, J. M.; Henderson, B. S. Chem. Rev. 1990, 90, 1203.
60. (b) Creighton, D. J.; Murthy, N. S. R. K. The Enzymes; Academic Press: San Diego, 1990; Vol. XIX, p 323.
61. (a) Bevins, C. L.; Bantia, S.; Pollack, R. M.; Bounds, P. L.; Kayser, R. H. J. Am. Chem. Soc. 1984, 706, 4957.
62. (b) Bounds, P. L.; Pollack, R. M. Biochemistry 1987, 26, 2263.
63. (a) Kuliopulos, A.; Mildvan, A. S.; Shonle, D.; Talalay, P. Biochemistry 1989, 28, 149.
64. (b) Xue, L.; Talalay, P.; Mildvan, A. S. Biochemistry, 1990, 29, 7491.
65. (c) Kuliopulos, A.; Mullen, G. P.; Xue, L.; Mildvan, A. S. Biochemistry 1991, 30, 3169.