Directed evolution of (βα)8-barrel enzymes: Establishing phosphoribosylanthranilate isomerisation activity on the scaffold of the tryptophan synthase α-subunit

Protein Engineering, Design and Selection

Volumn 25, Issue 6, 2012, Pages 285-293

  Evran, Serap ^a,b   Telefoncu, Azmi ^a   Sterner, Reinhard ^b  

^a EGE UNIVERSITY   (Turkey)

^b UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

( )8 barrel; enzyme evolution; protein design; tryptophan biosynthesis

Indexed keywords

ACTIVE SITE; AMINO ACID SUBSTITUTION; BOUND LIGANDS; CATALYTIC RESIDUE; COMPLEMENTATION; DIRECTED EVOLUTION; DNA SHUFFLING; E. COLI; ERROR PRONE PCR; EVOLUTIONARY ORIGIN; GENE DUPLICATIONS; GENE LIBRARIES; IN-VITRO; IN-VIVO; ISOMERASES; ISOMERISATION; PHOSPHATE BINDING; PROTEIN DESIGN; PROTEIN ENGINEERING; RANDOM MUTAGENESIS; SALMONELLA TYPHIMURIUM; SITE DIRECTED MUTAGENESIS; TRYPTOPHAN SYNTHASE; WILD TYPES;

AMINO ACIDS; BIOCHEMISTRY; BIOSYNTHESIS; ENZYME KINETICS; ESCHERICHIA COLI; GENES; GENETIC ENGINEERING; ISOMERIZATION; POLYMERASE CHAIN REACTION; SALMONELLA; SCAFFOLDS (BIOLOGY);

CATALYST ACTIVITY;

ENZYME; PHOSPHORIBOSYLANTHRANILATE ISOMERASE; TRYPTOPHAN SYNTHASE; TRYPTOPHAN SYNTHASE ALPHA SUBUNIT; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; DNA SHUFFLING; ENZYME KINETICS; ESCHERICHIA COLI; GENE DELETION; GENE DUPLICATION; ISOMERIZATION; MUTAGENESIS; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN ENGINEERING; SALMONELLA TYPHIMURIUM;

ALDOSE-KETOSE ISOMERASES; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CATALYTIC DOMAIN; DIRECTED MOLECULAR EVOLUTION; DNA SHUFFLING; ESCHERICHIA COLI; GENE LIBRARY; GENETIC COMPLEMENTATION TEST; KINETICS; MODELS, MOLECULAR; PROTEIN ENGINEERING; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; SALMONELLA TYPHIMURIUM; TRYPTOPHAN; TRYPTOPHAN SYNTHASE;

ESCHERICHIA COLI; SALMONELLA TYPHIMURIUM;

EID: 84861588442     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzs015     Document Type: Article

References (53)

1. Beismann-Driemeyer, S. and Sterner, R. (2001) J. Biol. Chem., 276, 20387-20396.
2. Bershtein, S. and Tawfik, D.S. (2008) Curr. Opin. Chem. Biol., 12, 151-158.
3. Caetano-Annolles, G., Kim, H.S. and Mittenthal, J.E. (2007) Proc. Natl Acad. Sci. USA, 104, 9358-9363.
4. Caetano-Anolles, G., Wang, M., Caetano-Anolles, D. and Mittenthal, J.E. (2009) Biochem. J., 417, 621-637.
5. Claren, J., Malisi, C., Hocker, B. and Sterner, R. (2009) Proc. Natl Acad. Sci. USA, 106, 3704-3709.
6. Copley, R.R. and Bork, P. (2000) J. Mol. Biol., 303, 627-641.
7. DeLano, W.L. (2002) PyMOL molecular graphics system. Available at: http:// www.pymol.org.
8. Eisenbeis, S. and Hocker, B. (2010) J. Pept. Sci., 16, 538-544.
9. Gerlt, J.A. and Raushel, F.M. (2003) Curr. Opin. Chem. Biol., 7, 252-264.
10. Hennig, M., Darimont, B.D., Jansonius, J.N. and Kirschner, K. (2002) J. Mol. Biol., 319, 757-766.
11. Henn-Sax, M., Hocker, B., Wilmanns, M. and Sterner, R. (2001) Biol. Chem., 382, 1315-1320.
12. Henn-Sax, M., Thoma, R., Schmidt, S., Hennig, M., Kirschner, K. and Sterner, R. (2002) Biochemistry, 41, 12032-12042.
13. Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. and Pease, L.R. (1989) Gene, 77, 51-59.
14. Hocker, B., Jurgens, C., Wilmanns, M. and Sterner, R. (2001) Curr. Opin. Biotechnol., 4, 376-381.
15. Hommel, U., Eberhard, M. and Kirschner, K. (1995) Biochemistry, 34, 5429-5439.
16. Horowitz, N.J. (1945) Proc. Natl Acad. Sci. USA, 31, 153-157.
17. Jackel, C. and Hilvert, D. (2010) Curr. Opin. Chem. Biol., 21, 753-759.
18. Jurgens, C., Strom, A., Wegener, D., Hettwer, S., Wilmanns, M. and Sterner, R. (2000) Proc. Natl Acad. Sci. USA, 97, 9925-9930.
19. Kirschner, K., Lane, A.N. and Strasser, A.W. (1991) Biochemistry, 30, 472-478.
20. Lang, D., Thoma, R., Henn-Sax, M., Sterner, R. and Wilmanns, M. (2000) Science, 289, 1546-1550.
21. Leopoldseder, S., Claren, J., Jurgens, C. and Sterner, R. (2004) J. Mol. Biol., 337, 871-879.
22. Lim, W.K., Shin, H.J., Milton, D.L. and Hardman, J.K. (1991a) J. Bacteriol., 173, 1886-1893.
23. Lim, W.K., Sarkar, S.K. and Hardman, J.K. (1991b) J. Biol Chem., 266, 20205-20212.
24. List, F., Sterner, R. and Wilmanns, M. (2011) ChemBioChem, 12, 1487-1494.
25. Merz, A., Yee, M.C., Szadkowski, H., Pappenberger, G., Crameri, A., Stemmer, W.P., Yanofsky, C. and Kirschner, K. (2000) Biochemistry, 39, 880-889.
26. Nagano, N., Orengo, C.A. and Thornton, J.M. (2002) J. Mol. Biol., 321, 741-765.
27. Neuenschwander, M., Butz, M., Heintz, C., Kast, P. and Hilvert, D. (2007) Nat. Biotechnol., 25, 1145-1147.
28. Pal, C., Papp, B. and Lercher, M.J. (2006) Nat. Rev. Genet., 7, 337-348.
29. Patrick, W.M. and Matsumura, I. (2008) J. Mol. Biol., 377, 323-336.
30. Pujadas, G. and Palau, J. (1999) Biologia (Bratisl)., 54, 231-253.
31. Raine, A.R., Scrutton, N.S. and Mathews, F.S. (1994) Protein Sci., 3, 1889-1892.
32. Riechmann, L. and Winter, G. (2006) J. Mol. Biol., 363, 460-468.
33. Romero, P.A. and Arnold, F.H. (2009) Nat. Rev. Mol. Cell Biol., 10, 866-876.
34. Saab-Rincon, G., Olvera, L., Olvera, M., Rudino-Pinera, E., Benites, E., Soberon, X. and Morett, E. (2012) J. Mol. Biol., 416, 255-270.
35. Schmidt, D.M., Mundorff, E.C., Dojka, M., Bermudez, E., Ness, J.E., Govindarajan, S., Babbitt, P.C., Minshull, J. and Gerlt, J.A. (2003) Biochemistry, 42, 8387-8393.
36. Schneider, W.P., Nichols, B.P. and Yanofsky, C. (1981) Proc. Natl Acad. Sci. USA, 78, 2169-2173.
37. Setiyaputra, S., Mackay, J.P. and Patrick, W.M. (2011) J. Mol. Biol., 408, 291-303.
38. Shatsky, M., Nussinov, R. and Wolfson, H.J. (2004) Proteins, 56, 143-156.
39. Soskine, M. and Tawfik, D.S. (2010) Nat. Rev. Genet., 11, 572-582.
40. Stemmer, W.P. (1994) Proc. Natl Acad. Sci. USA, 91, 10747-10751.
41. Sterner, R. and Hocker, B. (2005) Chem. Rev., 105, 4038-4055.
42. Sterner, R., Dahm, A., Darimont, B., Ivens, A., Liebl, W. and Kirschner, K. (1995) EMBO J., 14, 4395-4402.
43. Sterner, R., Kleemann, G.R., Szadkowski, H., Lustig, A., Hennig, M. and Kirschner, K. (1996) Protein Sci., 5, 2000-2008.
44. Stuebe, D., Matile, H. and Garotta, G. (1990) Immunol. Methods, 4, 121-152.
45. Todd, A.E., Orengo, C.A. and Thornton, J.M. (1999) Curr. Opin. Chem. Biol., 3, 548-556.
46. Weischet, W.O. and Kirschner, K. (1976) Eur. J. Biochem., 65, 375-385.
47. Weyand, M. and Schlichting, I. (1999) Biochemistry, 38, 16469-16480.
48. Wierenga, R.K. (2001) FEBS Lett., 492, 193-198.
49. Wilmanns, M., Hyde, C.C., Davies, D.R., Kirschner, K. and Jansonius, J.N. (1991) Biochemistry, 30, 9161-9169.
50. Wright, H., Noda-Garc?a, L., Ochoa-Leyva, A., Hodgson, D.A., Fulop, V. and Barona-Gomez, F. (2008) Biochem. Biophys. Res. Commun., 365, 16-21.
51. Yadid, I. and Tawfik, D.S. (2007) J. Mol. Biol., 365, 10-17.
52. Yanofsky, C., Miles, E.W., Bauerle, R. and Kirschner, K. (1999) In Creighton, T.E. (ed), The Encyclopedia of Molecular Biology. New York: Wiley, pp. 2676-2689.
53. Zhang, J. (2003) Trends Ecol. Evol., 18, 292-298.