Glutamate-119 of the large α-subunit is the catalytic base in the hydration of 2-trans-enoyl-coenzyme a catalyzed by the multienzyme complex of fatty acid oxidation from Escherichia coli

Biochemistry

Volumn 36, Issue 36, 1997, Pages 11044-11049

  He, Xue Ying ^a   Yang, Song Yu ^a  

^a NEW YORK STATE INSTITUTE FOR BASIC RESEARCH IN DEVELOPMENTAL DISABILITIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3 HYDROXYACYL COENZYME A DEHYDROGENASE; ACETYL COENZYME A ACYLTRANSFERASE; ASPARAGINE; ASPARTIC ACID; ENOYL COENZYME A HYDRATASE; GLUTAMIC ACID; GLYCINE; ISOMERASE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME SUBUNIT; ESCHERICHIA COLI; FATTY ACID OXIDATION; HYDRATION; NONHUMAN; PH; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ACYL COENZYME A; AMINO ACID SEQUENCE; ANIMALS; COENZYME A; ENOYL-COA HYDRATASE; ESCHERICHIA COLI; FATTY ACIDS; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; RATS; SEQUENCE ALIGNMENT;

ESCHERICHIA COLI; FELIS CATUS;

EID: 0030766386     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi970901t     Document Type: Article

References (50)

1. Binstock, J. F., and Schulz, H. (1981) Methods Enzymol. 71, 403-411.
2. Yang, S.-Y., and Schulz, H. (1983) J. Biol. Chem. 258, 9780-9785.
3. Yang, S.-Y., Yang, X.-Y. H., Healy-Louie, G., Schulz, H., and Elzinga, M. (1990) J. Biol. Chem. 265, 10424-10429.
4. Yang, X.-Y. H., Schulz, H., Elzinga, M., and Yang, S.-Y. (1991) Biochemistry 30, 6788-6795.
5. He, X.-Y., and Yang, S.-Y. (1996) Biochemistry 35, 9625-9630.
6. He, X.-Y., Deng, H., and Yang, S.-Y. (1997) Biochemistry 36, 261-268.
7. Yang, S.-Y., and Elzinga, M. (1993) J. Biol. Chem. 268, 6588-6592.
8. Yang, S.-Y., He, X.-Y., and Schulz, H. (1995) Biochemistry 34, 6441-6447.
9. Müller-Newen, G., Janssen, U., and Stoffel, W. (1995) Eur. J. Biochem. 228, 68-73.
10. Willadsen, P., and Eggerer, H. (1975) Eur. J. Biochem. 54, 247-252.
11. Wakil, S. J. (1956) Biochim. Biophys. Acta 19, 497-504.
12. Stern, J. R. (1961) in The Enzymes (Boyer, P. D., Lardy, H., and Myrbäck, K., Eds.) 2nd ed., Vol. 5, pp 511-529, Academic Press, New York.
13. Steinman, H. M., and Hill, R. L. (1975) Methods Enzymol. 35, 136-151.
14. Fong, J. C., and Schulz, H. (1981) Methods Enzymol. 71, 390-398.
15. He, X.-Y., Yang, S.-Y., and Schulz, H. (1992) Arch. Biochem. Biophys. 298, 527-531.
16. Mohrig, J. R., Moerke, K. A., Cloutier, D. L., Lane, B. D., Person, E. C. and Onasch, T. B. (1995) Science 269, 527-529.
17. Gerlt, J. A., and Gassman, P. G. (1992) J. Am. Chem. Soc. 114, 5928-5934.
18. Bahnson, B. J., and Anderson, V. E. (1991) Biochemistry 30, 5894-5906.
19. D'Ordine, R. L., Tonge, P. J., Carey, P. R., and Anderson, V. E. (1994) Biochemistry 33, 12635-12643.
20. Luo, M. J., He, X.-Y., Sprecher, H., and Schulz, H. (1993) Arch. Biochem. Biophys. 304, 266-271.
21. Weeks, G., and Wakil, S. J. (1968) J. Biol. Chem. 243, 1180-1189.
22. Seubert, W. (1960) Biochem. Prep. 7, 80-83.
23. Goldman, P., and Vagelos, P. R. (1961) J. Biol. Chem. 236, 2620-2623.
24. Staack, H., Binstock, J. F., and Schulz, H. (1978) J. Biol. Chem. 253, 1827-1831.
25. Deng, W. P., and Nickoloff, J. A. (1992) Anal. Biochem. 200, 81-88.
26. Sanger, F., Nicklen, S., and Coulson, A. R. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 5463-5467.
27. Chung, C. T., Niemela, S. L., and Miller, R. H. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 2172-2175.
28. Yang, S.-Y., Li, J., He, X.-Y., Cosloy, S. D., and Schulz, H. (1988) J. Bacteriol. 170, 2543-2548.
29. Bradford, M. M. (1976) Anal. Biochem. 72, 248-254.
30. Blackshear, P. J. (1984) Methods Enzymol. 104, 237-255.
31. Cornish-Bowden, A. (1995) Analysis of Enzyme Kinetic Data, Oxford University Press, New York.
32. Segel, I. H. (1975) Enzyme Kinetics, Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme System, Wiley Interscience, New York.
33. Tipton, K. F., and Dixon, H. B. F. (1979) Methods Enzymol. 63, 183-234.
34. D'Ordine, R. L., Bahnson, B. J., Tonge, P. J., and Anderson, V. E. (1994) Biochemistry 33, 14733-14742.
35. Gerlt, J. A., and Gassman, P. G. (1993) Biochemistry 32, 11943-11952.
36. Yang, S.-Y., Cuebas, D., and Schulz, H. (1986) J. Biol. Chem. 261, 15390-15395.
37. Wu, W.-J., Anderson, V. E., Raleigh, D. P., and Tonge, P. J. (1997) Biochemistry 36, 2211-2220.
38. Engel, C. K., Mathieu, M., Zeelen, J. P., Hiltunen, J. K., and Wierenga, R. K. (1996) EMBO J. 15, 5135-5145.
39. Rossmann, M. G., Liljas, A., Brändén, C. I., and Banaszak, L. J. (1975) in The Enzymes, 3rd Ed. (Boyer, P. D. Ed.) Vol. 11, pp 61-102, Academic Press, New York.
40. Poyner, R. R., Laughlin, L. T., Sowa, G. A., and Reed, G. H. (1996) Biochemistry 35, 1692-1699.
41. Osumi, T., Ishii, N., Hijikata, M., Kamijo, K., Ozasa, H., Furuta, S., Miyazawa, S., Kondo, K., Inoue, K., Kagamiyama, H., and Hashimoto, T. (1985) J. Biol. Chem. 260, 8905-8910.
42. Yang, S.-Y., He, X.-Y., Styles, J., Luo, M. J., Schulz, H., and Elzinga, M. (1994) Biochem. Biophys. Res. Commun. 198, 431-437.
43. Minami-Ishii, N., Taketani, S., Osumi, T., and Hashimoto, T. (1989) Eur. J. Biochem. 185, 73-78.
44. Kanazawa, M., Ohtake, A., Abe, H., Yamamoto, S., Satoh, Y., Takayanagi, M., Niimi, H., Mori, M., and Hashimoto, T. (1993) Enzyme Protein 47, 9-13.
45. Waterson, R. M., Castellino, F. J., Hass, G. M., and Hill, R. L. (1972) J. Biol. Chem. 247, 5266-5271.
46. Jackson, S., Schaefer, J., Middleton, B., and Turnbull, D. M. (1995) Biochem. Biophys. Res. Commun. 214, 247-253.
47. Nakagawa, J., Waldner, H., Meyer-Monard, S., Hofsteenge, J., Jenö, P., and Moroni, C. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 2051-2055.
48. Preisig-Müller, R., Gühnemann-Schäfer, K., and Kindl, H. (1994) J. Biol. Chem. 269, 20475-20481.
49. Palosaari, P. M., Vihinen, M., Mantsala, P. I., Alexson, S. E. H., Pihlajaniemi, T., and Hiltunen, J. K. (1991) J. Biol. Chem. 266, 10750-10753.
50. Boynton, Z. L., Bennett, G. N., and Rudolph, F. B. (1996) J. Bacteriol. 178, 3015-3024.