The consequences of engineering an extra disulfide bond in the Penicillium camembertii mono- and diglyceride specific lipase

Protein Engineering

Volumn 9, Issue 9, 1996, Pages 789-795

  Yamaguchi, S ^a   Takeuchi, K ^a   Mase, T ^a   Oikawa, K ^b,c   McMullen, T ^b   Derewenda, U ^b,c   McElhaney, R N ^b   Kay, C M ^b   Derewenda, Z S ^b,c  

^a Amano Enzyme Inc   (Japan)

^b UNIVERSITY OF ALBERTA   (Canada)

^c UNIVERSITY OF VIRGINIA   (United States)

Author keywords

Enzyme engineering; Protein stability; Site specific mutagenesis; Thermostability

Indexed keywords

ACYLGLYCEROL LIPASE; DIACYLGLYCEROL; LIPOPROTEIN LIPASE; MONOACYLGLYCEROL;

AMINO ACID SEQUENCE; ARTICLE; BIOPHYSICS; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME MODIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; NONHUMAN; PENICILLIUM; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN METABOLISM; RHIZOPUS; TEMPERATURE; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY;

BASE SEQUENCE; DIGLYCERIDES; DISULFIDES; DNA PRIMERS; ENZYME STABILITY; GLYCERIDES; LIPASE; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; PENICILLIUM; PROTEIN CONFORMATION; PROTEIN ENGINEERING; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 0029821990     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (43)

1. Betz, S.F. (1993) Protein Sci., 2, 1551-1558.
2. Brunger, A.T. (1988) X-PLOR Manual. Yale University, New Haven, CT.
3. Brzozowski, A.M. et al. (1991) Nature, 351, 491-494.
4. Carson, M. (1987) J. Mol. Graphics, 5, 103-106.
5. Creighton, T.E. and Goldenberg, D.P. (1984) J. Mol. Biol., 179, 497-526.
6. Derewenda, U., Brzozowski, A.M., Lawson, D.M. and Derewenda, Z.S. (1992a) Biochemistry, 31, 1532-1541.
7. Derewenda, U., Swenson, L., Green, R., Wei, Y, Dodson, G.G., Yamaguchi, S., Haas, M.J. and Derewenda, Z.S. (1994a) Nature Struct. Biol., 1, 36-47.
8. Derewenda, U., Swenson, L., Wei, Y., Green, R., Kobos, P.M., Joerger, R., Haas, M.J. and Derewenda, Z.S. (1994b) J. Lipid Res., 35, 524-534.
9. Derewenda, Z.S. (1995) Nature Struct. Biol., 2, 347-349.
10. Derewenda, Z.S., Derewenda, U. and Dodson, G.G. (1992b) J. Mol. Biol., 227, 818-839.
11. Desnuelle, P., Sarda, L. and Aihaud, G. (1960) Biochim. Biophys. Acta, 37, 570-571.
12. Doig, A.J. and Williams, D.H. (1991) J. Mol. Biol., 217, 389-398.
13. Flory, P.J. (1956) J. Am. Chem. Soc., 78, 5222-5235.
14. Goldenberg, D.P., Bekeart, L.S., Laheru, D.A. and Zhou, J.D. (1993) Biochemistry, 32, 2835-2844.
15. Grochulski, P., Yunge, L., Schrag, J.D., Bouthillier, F., Smith, P., Harrison, D., Rubin, B. and Cygler, M. (1993) J. Biol. Chem., 268, 12843-12847.
16. Harwood, J. (1989) Trends Biochem. Sci., 14, 125-126.
17. Jones, A. (1978). J. Appl. Crystallogr., 11, 268-272.
18. Johnson, R.E., Adams, P. and Rupley, J.A. (1978) Biochemistry, 17, 1479-1484.
19. Kanaya, S. et al. (1991) J. Biol. Chem., 261, 15480-15485.
20. Kunkel, T.A. (1985) Proc. Natl Acacl. Sci. USA, 82, 488-492.
21. Kuramitsu, S., Hiromi, K., Hayashi, H., Morino, Y. and Kagamiyama, H. (1990) Biochemistry, 29, 5469-5476.
22. Kuroki, R., Inaka, K., Taniyama, Y., Kidokoro, S., Matsushima, M., Kikuchi, M. and Yutani, K. (1992) Biochemistry, 31, 8323-8328.
23. Lin, T.Y. and Kim, P.S. (1989) Biochemistry, 28, 5282-5287.
24. Matsumura, M., Becktel, W.J., Levitt, M. and Matthews, B.W. (1989a) Proc. Natl Acad. Sci. USA, 86, 6562-4566.
25. Matsumura, M., Signor, G. and Matthews, B.W. (1989b) Nature, 342, 291-293.
26. Mitchinson, C. and Wells, J.A. (1989) Biochemistry, 28, 4807-4-815.
27. Ollis, D.I. et al. (1992) Proteins, 5, 197-211.
28. Pace, C.N. (1986) Methods Enzymol., 131, 266-279.
29. Pace, C.N., Grimsley, J.R., Thompson, J.A. and Barnett, B.J. (1988) J. Biol. Chem., 263, 11820-11825.
30. Pappas, J.A. (1977) J. Am. Chem. Soc., 99, 311-321.
31. Poland, D.C. and Scheraga, H.A. (1965) Biopolymers, 3, 379-399.
32. Pollitt, S. and Zalkin, H. (1983) J. Bacteriol., 153, 27-32.
33. Richardson, J.S. (1981) Adv. Protein Chem., 34, 167-339.
34. Rosenfield, R.E., Parthasarathy, R. and Dunitz, J.D. (1977) J. Am. Chem. Soc., 99, 4860-4862.
35. Sanger, F., Nicklen, S. and Coulsen, A.R. (1977) Proc. Natl Acad. Sci. USA, 74, 5463-5467.
36. Soichet, B.K., Baase, W.A., Kuroki, R. and Matthews, B.W. (1995) Proc. Natl Acad. Sci. USA, 92, 452-456.
37. Srinivasan, N., Sowdhamini, R., Ramakrishnan, C. and Balaram, P. (1990) Int. J. Peptide Protein Res., 36, 147-155.
38. Szajewski, R.P. and Whitesides, G.M. (1980) J. Am. Chem. Soc., 102, 2011-2026.
39. Thornton, J.M. (1981) J. Mol. Biol. 151, 261-287.
40. Unkles, S.E. et al. (1989) Mol. Gen. Genet., 218, 99-104.
41. van Tilbeurgh, H., Egloff, M.-P., Martinez, C., Rugani, N., Verger, R. and Cambillau, C. (1993) Nature, 362, 814-820.
42. Yamaguchi, S. and Mase, T. (1991) Appl. Microbiol. Biotechnol., 34, 720-725.
43. Yamaguchi, S., Mase, T. and Takeuchi, K. (1992) Biosci. Biotechnol. Biochem., 56, 315-319.