A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability

Biochemistry

Volumn 36, Issue 32, 1997, Pages 9655-9662

  Schliebs, Wolfgang ^a,b   Thanki, Narmada ^a   Jaenicke, Rainer ^c   Wierenga, Rik K ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b RUHR UNIVERSITY BOCHUM   (Germany)

^c UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CATALYSIS; DIMERIZATION; ESCHERICHIA COLI; GENE MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; THERMOSTABILITY; ULTRACENTRIFUGATION;

CATALYSIS; DIMERIZATION; ENZYME ACTIVATION; ENZYME STABILITY; KINETICS; MUTAGENESIS, SITE-DIRECTED; THERMODYNAMICS; TRIOSE-PHOSPHATE ISOMERASE; VARIATION (GENETICS);

ESCHERICHIA COLI; FELIS CATUS;

EID: 0030857332     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi963086a     Document Type: Article

References (41)

1. Abagyan, R. A., & Totrov, M. M. (1994) J. Mol. Biol. 235, 983-1002.
2. Abagyan, R. A., Totrov, M., & Kuznetsov, D. (1994) J. Comput. Chem. 15, 488-506.
3. Beernink, P. T., & Tolan, D. R. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 5374-5379.
4. Bertini, I., Piccoli, M., Viezzoli, M. S., Chiu, C. Y., & Mullenbach, G. T. (1994) Eur. Biophys. J. 23, 167-176.
5. Bode, W., & Huber, R. (1991) Curr. Opin. Struct. Biol. 1, 45-52.
6. Borchert, T. V., Abagyan, R., Radha Kishan, K. V., Zeelen, J. P., & Wierenga, R. K. (1993a) Structure 1, 205-213.
7. Borchert, T. V., Pratt, K., Zeelen, J. P., Callens, M., Noble, M. E. M., Opperdoes, F. R., Michels, P. A. M., & Wierenga, R. K. (1993b) Eur. J. Biochem. 211, 703-710.
8. Borchert, T. V., Abagyan, R., Jaenicke, R., & Wierenga, R. K. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 1515-1518.
9. Borchert, T. V., Zeelen, J. P., Schliebs, W., Callens, M., Minke, W., Jaenicke, R., & Wierenga, R. K. (1995) FEBS Lett. 367, 315-318.
10. Breiter, D. R., Resnik, E., & Banaszak, L. J. (1994) Protein Sci. 3, 2023-2032.
11. Bullock, W. O., Fernandez, J. M., & Short, J. M. (1987) BioTechniques 5, 376-378.
12. Casal, J. I., Ahern, T. J., Davenport, R. C., Petsko, G. A., & Klibanov, A. M. (1987) Biochemistry 26, 1258-1264.
13. Chothia, C. (1991) Curr. Opin. Struct. Biol. 1, 53-59.
14. Dickason, R. R., & Huston, D. P. (1996) Nature 379, 652-655.
15. Erhardt, J., & Dirr, H. (1995) Eur. J. Biochem. 230, 614-620.
16. Fell, D. A., & Branford White, J. (1975) Biochem. Biophys. Res. Commun. 67, 1013-1018.
17. Gawehn, K., & Bergmeyer, H. U. (1974) in Methoden der enzymatischen Analyse (Bergmeyer, H. U., Ed.) pp 1542-1544, Verlag Chemie GmbH, Weinheim, Germany.
18. Goodsell, D. S., & Olson, A. J. (1993) Trends Biochem. Sci. 18, 65-68.
19. Higuchi, R. (1990) in PCR protocols: a guide to methods and applications (Innis, M. A., Gelford, D. H., Sinsky, J. J., & White, T. J., Eds.) pp 177-183, Academic Press, San Diego, CA.
20. Jaenicke, R. (1987) Prog. Biophys. Mol. Biol. 49, 117-237.
21. Jaenicke, R. (1996) Curr. Top. Cell. Regul. 34, 209-314.
22. Janin, J. (1995) Biochemie 77, 497-505.
23. Janin, J., & Chothia, C. (1990) J. Biol. Chem. 265, 16027-16030.
24. Janin, J., Miller, S., & Chothia, C. (1988) J. Mol. Biol. 204, 155-164.
25. Jones, S., & Thornton, J. M. (1995) Prog. Biophys. Mol. Biol. 63, 31-63.
26. Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) Acta Crystallogr. 47A, 110-119.
27. Knowles, J. R. (1991) Nature 350, 121-124.
28. Lambeir, A.-M., Opperdoes, F. R., & Wierenga, R. K. (1987) Eur. J. Biochem. 168, 69-74.
29. Mainfroid, V., Trepstra, P., Beauregard, M., Frere, J.-M., Mande, S. C., Hol. W. G. J., Martial, J. A., & Goraj, K. (1996) J. Mol. Biol. 257, 441-456.
30. Mossing, M. C., & Sauer, R. T. (1990) Science 250, 1712-1715.
31. Pekrun, A., Neubauer, B. A., Eher, S. W., Lakamek, M., Seidel, H., & Schröter, W. (1995) Clin. Genet. 47, 175-179.
32. Porvari, K. S., Herrala, A. M., Kurkela, R. M., Taavitsainen, P. A., Lindqvist, Y., Schneider, G., & Vikho, P. T. (1994) J. Biol. Chem. 269, 22642-22646.
33. Rietveld, A. W. M., & Ferreira, S. T. (1996) Biochemistry 35, 7743-7751.
34. Schliebs, W., Thanki, N., Eritja, R., & Wierenga, R. (1996) Protein Sci. 5, 229-239.
35. Steif, C., Weber, P., Hinz, H.-J., Flossdorf, J., Cesareni, G., & Kokkinidis, M. (1993) Biochemistry 32, 3867-3876.
36. Thanki, N., Zeelen, J. Ph., Mathieu, M., Jaenicke, R., Abagyan, R. A., Wierenga, R. K., & Schliebs, W. (1997) Protein Eng. 10, 159-167.
37. Vriend, G. (1990) J. Mol. Graphics 8, 52-56.
38. Ward, W. H. J., Hugh Jones, D., & Fersht, A. R. (1987) Biochemistry 26, 4131-4138.
39. Wierenga, R. K., Noble, M. E. M., & Davenport, R. C. (1992) J. Mol. Biol. 224, 1115-1126.
40. Yphantis, D. A. (1964) Biochemistry 3, 297-317.
41. Zabori, S., Rudolph, R., & Jaenicke, R. (1980) Z. Naturforsch. 35C, 999-1004.