Engineering a Hyperstable Enzyme by Manipulation of Early Steps in the Unfolding Process

References

• Arnold F. H. “Enzyme engineering reaches the boiling point”. Proc. Natl. Acad. Sci. USA 1998a; 95: 2035–2036
   PubMed Web of Science ®Google Scholar
• Arnold F. H. “Design by directed evolution”. Acc. Chem. Res 1998b; 31: 125–131
   Web of Science ®Google Scholar
• Chrunyk B. A., Wetzel R. “Breakdown in the relationship between thermal and thermodynamic stability in an interleukin-1 β point mutant modified in a surface loop”. Protein Engng 1993; 6: 733–738
   PubMedGoogle Scholar
• Corbett R. J.T., Ahmad F., Roche R. S. “Domain unfolding and the stability of thermolysin in guanidine hydrochloride”. Biochem. Cell Biol 1986; 64: 953–961
   PubMed Web of Science ®Google Scholar
• Dahlquist F. W., Long J. W., Bigbee W. L. “Role of calcium in thermal stability of thermolysin”. Biochemistry 1976; 15: 1103–1111
   PubMed Web of Science ®Google Scholar
• Eijsink V. G.H., Dijkstra B. W., Vriend G., Van der Zee J. R., Veltman OR, Van der Vinne B., Van den Burg B., Kempe S., Venema G. “The effect of cavity-filling mutations on the thermostability of Bacillus stearothermophilus neutral protease”. Protein Engng 1992a; 5: 421–426
   PubMedGoogle Scholar
• Eijsink V. G.H., Vriend G., Van der Vinne B., Hazes B., Van den Burg B., Venema G. “Effects of changing the interaction between subdomains on the thermostability of Bacillus neutral proteases”. Proteins 1992b; 14: 224–236
   PubMed Web of Science ®Google Scholar
• Eijsink V. G.H., Veltman O. R., Aukema W., Vriend G., Venema G. “Structural determinants of the stability of thermolysin-like proteases”. Nature Struct. Biol 1995; 2: 374–379
   PubMedGoogle Scholar
• Facchiano A. M., Colonna G., Ragone R. “Helix stabilizing factors and stabilization of thermophilic proteins: an X-ray based study”. Protein Engng 1998; 11: 753–760
   PubMedGoogle Scholar
• Fink A. L. “Protein aggregation: folding aggregates, inclusion bodies and amyloid”. Folding & Design 1998; 3: R9–R23
   PubMedGoogle Scholar
• Fontana A. “Structure and stability of thermophilic enzymes; studies on thermolysin”. Biophys. Chem 1988; 29: 181–193
   PubMed Web of Science ®Google Scholar
• Giver L., Gershenson A., Freskgard P.-O., Arnold F. H. “Directed evolution of a thermostable esterase”. Proc. Natl. Acad. Sci. USA 1998; 95: 12809–12813
   PubMed Web of Science ®Google Scholar
• Haney P. J., Badger J. H., Buldak G. L., Reich C. I., Woese C. R., Olsen G. J. “Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species”. Proc. Natl. Acad. Sci. USA 1999; 96: 3578–3583
   PubMed Web of Science ®Google Scholar
• Holmes M. A., Matthews B. W. “Structure of thermolysin refined at 1.6 Å resolution”. J. Mol. Biol 1982; 160: 623–639
   PubMed Web of Science ®Google Scholar
• Hoseki J., Yano T., Koyama Y., Kuramitsu S., Kagamiyama H. “Directed evolution of thermostable kanamysin-resistance gene: a convenient selection marker for Thermus thermophilus”. J. Biochem. (Tokyo) 1999; 126: 951–956
   PubMed Web of Science ®Google Scholar
• Hubbard S. J. “The structural aspects of limited proteolysis of native proteins”. Biochim. Biophys. Acta 1998; 1382: 191–206
   PubMed Web of Science ®Google Scholar
• Kidokoro S., Miki Y, Endo K., Wada A., Nagao H., Miyake T., Aoyama A., Yoneya X, Kai K., Ooe S. “Remarkable activity enhancement of thermolysin mutants”. FEBS Lett 1995; 367: 73–76
   PubMed Web of Science ®Google Scholar
• Lebbink J. H.G., Knapp S., Van der Oost J., Rice D., Ladenstein R., De Vos W. M. “Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase II: construction of a 16-residue ion-pair network at the subunit interface”. J. Mol. Biol 1999; 289: 357–369
   PubMed Web of Science ®Google Scholar
• Malakauskas S. M., Mayo S. L. “Design, structure and stability of a hyperthermophilic protein variant”. Nature Struct. Biol 1998; 5: 470–475
   PubMedGoogle Scholar
• Mansfeld J., Vriend G., Dijkstra B. W., Veltman O. R., Van den Burg B., Venema G., Tjlbrich-Hofmann R., Eijsink V. G.H. “Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond”. J. Biol. Chem 1997; 272: 11152–11156
   PubMed Web of Science ®Google Scholar
• Mansfeld J., Vriend G., Van den Burg B., Eijsink V. G.H., Ulbrich-Hofmann R. “Probing the unfolding region in a thermolysin-like protease by site-specific immobilization”. Biochemistry 1999; 38: 8240–8245
   PubMed Web of Science ®Google Scholar
• Matthews B. W. “Structural basis of the action of thermolysin and related zinc peptidases”. Acc. Chem. Res 1988; 21: 333–340
   Web of Science ®Google Scholar
• Matthews B. W., Weaver L. H., Kester W. R. “The conformation of thermolysin”. J. Biol. Chem 1974; 249: 8030–8044
   PubMed Web of Science ®Google Scholar
• Matthews B. W., Nicholson H., Becktel W. J. “Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding”. Proc. Natl. Acad. Sci. USA 1987; 84: 6663–6667
   PubMed Web of Science ®Google Scholar
• Mitchinson C., Wells J. A. “Protein engineering of disulphide bonds in subtilisin BPN'”. Biochemistry 1989; 28: 4807–4815
   PubMed Web of Science ®Google Scholar
• Roche R. S., Voordouw G. “The structural and functional roles of metal ions in thermolysin”. CRC Crit. Rev. Biochem 1978; 5: 1–23
   PubMed Web of Science ®Google Scholar
• Schwehm J. M., Kristyanne E. S., Biggers C. C., Stites WE. “Stability effects of increasing the hydrophobicity of solvent-exposed side chains in staphylococcal nuclease”. Biochemistry 1998; 37: 6939–6948
   PubMed Web of Science ®Google Scholar
• Spiller B., Gershenson A., Arnold F. H., Stevens R. C. “A structural view on evolutionary divergence”. Proc. Natl. Acad. Sci. USA 1999; 96: 12305–12310
   PubMed Web of Science ®Google Scholar
• Stemmer W. P.C. “Rapid evolution of a protein in vitro by DNA shuffling”. Nature 1994; 370: 389–391
   PubMed Web of Science ®Google Scholar
• Takagi M., Imanaka T., Aiba S. “Nucleotide sequence and promoter region for the neutral protease gene from Bacillus stearothermophilus”. J. Bacteriol 1985; 163: 824–831
   PubMed Web of Science ®Google Scholar
• Ulbrich-Hofmann R., Arnold U., Mansfeld J. “The concept of the unfolding region for approaching the mechanisms of enzyme stabilization”. J. Mol. Catal. B-Enzymat 1999; 7: 125–131
   Google Scholar
• Van den Burg B., Dijkstra B. W., Vriend G., Van der Vinne B., Venema G., Eijsink V. G.H. “Protein stabilization by hydrophobic interactions at the surface”. Eur, J. Biochem 1994; 220: 981–985
   PubMedGoogle Scholar
• Van den Burg B., Vriend G., Veltman O. R., Venema G., Eijsink V. G.H. “Engineering an enzyme to resist boiling”. Proc. Natl. Acad. Sci. USA 1998; 95: 2056–2060
   PubMed Web of Science ®Google Scholar
• Van den Burg B., De Kreij A., Winkel C., Venema G. “Hydrolysis of industrial substrates by an extremely stable thermolysin-like protease variant obtained by protein engineering”. Biotechnol. Lett 1999a; 21: 537–542
   Web of Science ®Google Scholar
• Van den Burg B., De Kreij A., Van der Veek P., Mansfeld J., Venema G. “Characterization of a novel stable biocatalyst obtained by protein engineering”. Biotechnol. Appl. Biochem 1999b; 30: 35–40
   PubMed Web of Science ®Google Scholar
• Veltman O. R., Vriend G., Middelhoven P. J., Van den Burg B., Venema G., Eijsink V. G.H. “Analysis of structural determinants of the stability of thermolysin-like proteases by molecular modelling and site-directed mutagenesis”. Protein Engng 1996; 9: 1181–1190
   PubMedGoogle Scholar
• Veltman O. R., Vriend G., Hardy F., Mansfeld J., Van den Burg B., Venema G., Eijsink V. G.H. “Mutational analysis of a surface area that is critical for the thermal stability of thermolysin-like proteases”. Eur, J. Biochem 1997a; 248: 433–440
   PubMedGoogle Scholar
• Veltman O. R., Vriend G., Van den Burg B., Hardy F., Venema G., Eijsink V. G.H. “Engineering thermolysin-like proteases whose stability is largely independent of calcium”. FEBS Lett 1997b; 405: 241–244
   PubMed Web of Science ®Google Scholar
• Veltman O. R., Vriend G., Berendsen H. J.C., Van den Burg B., Venema G., Eijsink V. G.H. “A single calcium binding site is crucial for the calcium-dependent thermal stability of thermolysin-like proteases”. Biochemistry 1998; 37: 5312–5319
   PubMed Web of Science ®Google Scholar
• Vita C, Fontana A., Jaenicke R. “Folding of thermolysin fragments”. Eur, J. Biochem. 1989; 183: 513–518
   PubMedGoogle Scholar
• Vriend G. “what if, A molecular modelling and drug design program”. J. Mol. Graphics 1990; 8: 52–56
   PubMed Web of Science ®Google Scholar
• Vriend G., Eijsink V. G.H. “Prediction and analysis of structure, stability and unfolding of Bacillus neutral proteases”. J. Comput. Aided Mol. Des. 1993; 7: 367–396
   PubMed Web of Science ®Google Scholar
• Vriend G., Berendsen H. J.C., Van den Burg B., Venema G., Eijsink V. G.H. “Early steps in the unfolding of thermolysin-like proteases”. J. Biol. Chem 1998; 273: 35074–35077
   PubMed Web of Science ®Google Scholar
• Wells J. A. “Additivity of mutational effects in proteins”. Biochemistry 1990; 29: 8509–8517
   PubMed Web of Science ®Google Scholar
• Williams J. C., Zeelen J. P., Neubauer G., Vriend G., Backmann J., Michels P. A.M., Lambeir A.-M, Wierenga R. K. “Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power”. Protein Engng 1999; 12: 243–250
   PubMedGoogle Scholar
• Zhao H., Arnold F. H. “Directed evolution converts subtilisin E into a functional equivalent of thermrtase”. Protein Engng 1999; 12: 47–53
   PubMedGoogle Scholar