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Volumn 15, Issue C, 1998, Pages 277-294

Rigidity of thermophilic enzymes

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EID: 77957074791     PISSN: 09210423     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0921-0423(98)80043-9     Document Type: Chapter
Times cited : (33)

References (103)
  • 1
    • 0027487614 scopus 로고
    • Enzymes and proteins from organisms that grow near and above 100°C
    • Adams M.W.W. Enzymes and proteins from organisms that grow near and above 100°C. Annu. Rev. Microbiol. 47 (1993) 627-658
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 627-658
    • Adams, M.W.W.1
  • 2
    • 0029055215 scopus 로고
    • Extremoenzymes: Expanding the limits of biocatalysis
    • Adams M.W.W., Perler F.B., and Kelly RM. Extremoenzymes: Expanding the limits of biocatalysis. Biotechnology 13 (1995) 662-668
    • (1995) Biotechnology , vol.13 , pp. 662-668
    • Adams, M.W.W.1    Perler, F.B.2    Kelly, RM.3
  • 3
    • 0029962635 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray studies of α-amylase from the antarctic psychrophile Alteromonas haloplanctis A23
    • Aghajari N., Feller G., Gerday C., and Haser R. Crystallization and preliminary X-ray studies of α-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. Protein Sci. 5 (1996) 2128-2129
    • (1996) Protein Sci. , vol.5 , pp. 2128-2129
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 4
    • 0024412497 scopus 로고
    • Mutational effects on protein stability
    • Alber T. Mutational effects on protein stability. Annu. Rev. Biochem. 58 (1989) 765-798
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 765-798
    • Alber, T.1
  • 5
    • 0020648847 scopus 로고
    • The role of mobility in the substrate binding and catalytic machinery of enzymes
    • Mobility and function in proteins and nucleic acids, Pitman, London
    • Mobility and function in proteins and nucleic acids. Alber T., Gilbert W.A., Ringe D., and Petsko G.A. The role of mobility in the substrate binding and catalytic machinery of enzymes. Ciba Symposium 93 (1983), Pitman, London 4-24
    • (1983) Ciba Symposium 93 , pp. 4-24
    • Alber, T.1    Gilbert, W.A.2    Ringe, D.3    Petsko, G.A.4
  • 7
    • 0032478172 scopus 로고    scopus 로고
    • Enzyme engineering reaches the boiling point
    • Arnold F.H. Enzyme engineering reaches the boiling point. Proc. Natl. Acad. Sci. USA 95 (1998) 2035-2036
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2035-2036
    • Arnold, F.H.1
  • 8
    • 0028950046 scopus 로고
    • Improvement of thermal stability of subtilisin J by changing primary autolysis site
    • Bae; K.H., Jang J.S., Park K.S., Lee S.H., and Byun S.M. Improvement of thermal stability of subtilisin J by changing primary autolysis site. Biochem. Biophys. Res. Commun. 207 (1995) 20-24
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 20-24
    • Bae1    , K.H.2    Jang, J.S.3    Park, K.S.4    Lee, S.H.5    Byun, S.M.6
  • 10
    • 0015919530 scopus 로고
    • Enolase from the thermophile Thermus X-1
    • Barnes L.D., and Stellwagen E. Enolase from the thermophile Thermus X-1. Biochemistry 12 (1973) 1559-1565
    • (1973) Biochemistry , vol.12 , pp. 1559-1565
    • Barnes, L.D.1    Stellwagen, E.2
  • 11
    • 0030850229 scopus 로고    scopus 로고
    • Dissection of the gene of the bifunctional PGK-TDvl fusion protein from the hyperthermophilic bacterium Thermotoga maritima: Designe and characterization of the separate triose phosphate isomerase
    • Beaucamp N., Hofman A., Kellerer B., and Jaenicke R. Dissection of the gene of the bifunctional PGK-TDvl fusion protein from the hyperthermophilic bacterium Thermotoga maritima: Designe and characterization of the separate triose phosphate isomerase. Protein Sci. 6 (1997) 2159-2165
    • (1997) Protein Sci. , vol.6 , pp. 2159-2165
    • Beaucamp, N.1    Hofman, A.2    Kellerer, B.3    Jaenicke, R.4
  • 12
    • 0026702925 scopus 로고
    • 2+ -binding loop into subtilisin BPN
    • 2+ -binding loop into subtilisin BPN. Biochemistry 31 (1992) 7796-7801
    • (1992) Biochemistry , vol.31 , pp. 7796-7801
    • Braxton, S.1    Wells, J.A.2
  • 13
    • 0025804130 scopus 로고
    • Large differences in the helix propensities of alanine and glycine
    • Chakrabartty A., Schellman J.A., and Baldwin R.L. Large differences in the helix propensities of alanine and glycine. Nature 351 (1991) 586-588
    • (1991) Nature , vol.351 , pp. 586-588
    • Chakrabartty, A.1    Schellman, J.A.2    Baldwin, R.L.3
  • 14
    • 77957023639 scopus 로고
    • A correlation between protein thermostability and resistance to proteolysis
    • Daniel R.M., Cowan D.A., Morgan H.W., and Curran P. A correlation between protein thermostability and resistance to proteolysis. Biochem. J. 29 (1982) 181-193
    • (1982) Biochem. J. , vol.29 , pp. 181-193
    • Daniel, R.M.1    Cowan, D.A.2    Morgan, H.W.3    Curran, P.4
  • 18
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill K.A. Dominant forces in protein folding. Biochemistry 29 (1990) 7134-7155
    • (1990) Biochemistry , vol.29 , pp. 7134-7155
    • Dill, K.A.1
  • 19
    • 0017571023 scopus 로고
    • Exposure of tryptophanyl residues and tryptophan dynamics
    • Eftink M.R., and Ghiron C.A. Exposure of tryptophanyl residues and tryptophan dynamics. Biochemistry 16 (1976) 5546-5551
    • (1976) Biochemistry , vol.16 , pp. 5546-5551
    • Eftink, M.R.1    Ghiron, C.A.2
  • 20
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink M.R., and Ghiron C.A. Fluorescence quenching studies with proteins. Anal. Biochem. 114 (1981) 199-227
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 21
    • 0029162070 scopus 로고
    • Understanding and increasing protein stability
    • Fágáin C. Understanding and increasing protein stability. Biochim. Biophys. Acta 1252 (1995) 1-14
    • (1995) Biochim. Biophys. Acta , vol.1252 , pp. 1-14
    • Fágáin, C.1
  • 22
    • 0030681366 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Molecular basis of cold adaptation
    • Feller G., and Gerday C. Psychrophilic enzymes: Molecular basis of cold adaptation. Cell Mol. Life Sci. 53 (1997) 830-841
    • (1997) Cell Mol. Life Sci. , vol.53 , pp. 830-841
    • Feller, G.1    Gerday, C.2
  • 25
    • 0027462173 scopus 로고
    • Principles of protein stability derived from protein engineering experiments
    • Fersht A.R., and Serrano L. Principles of protein stability derived from protein engineering experiments. Curr. Opin. Struct. Biol. 3 (1993) 75-83
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 75-83
    • Fersht, A.R.1    Serrano, L.2
  • 26
    • 0001834289 scopus 로고
    • How nature engineers protein (thermo)stability
    • di Prisco G. (Ed), Springer Verlag, Heidelberg
    • Fontana A. How nature engineers protein (thermo)stability. In: di Prisco G. (Ed). Life in extreme conditions (1990), Springer Verlag, Heidelberg 89-113
    • (1990) Life in extreme conditions , pp. 89-113
    • Fontana, A.1
  • 27
    • 0026210241 scopus 로고
    • Analysis and modulation of protein stability
    • Fontana A. Analysis and modulation of protein stability. Curr. Opinion Biotechnol. 2 (1991) 551-560
    • (1991) Curr. Opinion Biotechnol. , vol.2 , pp. 551-560
    • Fontana, A.1
  • 28
    • 77957055440 scopus 로고    scopus 로고
    • Rigidity of thermophilic enzymes
    • Commun. TU-138. Budapest, 17-21 August 1997
    • Commun. TU-138. Fontana A. Rigidity of thermophilic enzymes. Proc. 8th Eur. Congress on Biotechnology. Budapest, 17-21 August 1997 (1997)
    • (1997) Proc. 8th Eur. Congress on Biotechnology
    • Fontana, A.1
  • 29
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • Fontana A., Fassina G., Vita C., Dalzoppo D., Zamai M., and Zambonin M. Correlation between sites of limited proteolysis and segmental mobility in thermolysin. Biochemistry 25 (1986) 1847-1851
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6
  • 30
    • 0003831915 scopus 로고
    • Molecular aspects of proteolysis
    • van den Tweel W., Harder A., and Buitelaar M. (Eds), Elsevier Sci. Publ., Amsterdam
    • Fontana A., Polverino de Laureto P., and De Filippis V. Molecular aspects of proteolysis. In: van den Tweel W., Harder A., and Buitelaar M. (Eds). Stability and stabilization of enzymes (1993), Elsevier Sci. Publ., Amsterdam 101-110
    • (1993) Stability and stabilization of enzymes , pp. 101-110
    • Fontana, A.1    Polverino de Laureto, P.2    De Filippis, V.3
  • 31
    • 0017263308 scopus 로고
    • Purification and properties of D-glyceraldehyde-3-phosphate dehydrogenase from the extreme thermophile Thermus thermophilus HB8
    • Fujita S., Oshima T., and Imahori K. Purification and properties of D-glyceraldehyde-3-phosphate dehydrogenase from the extreme thermophile Thermus thermophilus HB8. Eur. J. Biochem. 64 (1976) 57-68
    • (1976) Eur. J. Biochem. , vol.64 , pp. 57-68
    • Fujita, S.1    Oshima, T.2    Imahori, K.3
  • 33
    • 0016017019 scopus 로고
    • Intracellular protein degradation in mammalian and bacterial cells
    • Goldberg A.L., and Dice J.F. Intracellular protein degradation in mammalian and bacterial cells. Annu. Rev. Biochem. 43 (1974) 835-864
    • (1974) Annu. Rev. Biochem. , vol.43 , pp. 835-864
    • Goldberg, A.L.1    Dice, J.F.2
  • 34
    • 0015867173 scopus 로고
    • Isocitrate lyase from a thermophilic Bacillus: Effect of salts on enzyme activity
    • Griffiths M.W., and Sundaram T.K. Isocitrate lyase from a thermophilic Bacillus: Effect of salts on enzyme activity. J. Bacteriol. 116 (1973) 1160-1169
    • (1973) J. Bacteriol. , vol.116 , pp. 1160-1169
    • Griffiths, M.W.1    Sundaram, T.K.2
  • 35
    • 0024971021 scopus 로고
    • Stability and activity of a thermostable malic enzyme in denaturants and water-miscible organic solvents
    • Guagliardi A., Manco G., Rossi M., and Bartolucci S. Stability and activity of a thermostable malic enzyme in denaturants and water-miscible organic solvents. Eur. J. Biochem. 183 (1989) 25-30
    • (1989) Eur. J. Biochem. , vol.183 , pp. 25-30
    • Guagliardi, A.1    Manco, G.2    Rossi, M.3    Bartolucci, S.4
  • 39
    • 0017232786 scopus 로고
    • Esterase activity of zinc proteases
    • Holmquist B., and Vallee B.L. Esterase activity of zinc proteases. Biochemistry 15 (1976) 101-107
    • (1976) Biochemistry , vol.15 , pp. 101-107
    • Holmquist, B.1    Vallee, B.L.2
  • 40
    • 49249151121 scopus 로고
    • Conformational flexibility and its functional significance in some proteins
    • Huber R. Conformational flexibility and its functional significance in some proteins. Trends Biochem. Sci. 4 (1979) 271-274
    • (1979) Trends Biochem. Sci. , vol.4 , pp. 271-274
    • Huber, R.1
  • 41
    • 0019363271 scopus 로고
    • Enzymes under extremes of physical conditions
    • Jaenicke R. Enzymes under extremes of physical conditions. Annu. Rev. Biophys. Bioeng. 10 (1981) 1-67
    • (1981) Annu. Rev. Biophys. Bioeng. , vol.10 , pp. 1-67
    • Jaenicke, R.1
  • 42
    • 0026320508 scopus 로고
    • Protein stability and molecular adaptation to extreme conditions
    • Jaenicke R. Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202 (1991) 715-728
    • (1991) Eur. J. Biochem. , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 43
    • 0030067190 scopus 로고    scopus 로고
    • Stability and folding of ultrastable proteins: Eye lens crystallins and enzymes from thermophiles
    • Jaenicke R. Stability and folding of ultrastable proteins: Eye lens crystallins and enzymes from thermophiles. FASEB J. 10 (1996) 84-92
    • (1996) FASEB J. , vol.10 , pp. 84-92
    • Jaenicke, R.1
  • 44
    • 0029786277 scopus 로고    scopus 로고
    • Structure and stability of hyperstable proteins: Glycolytic enzymes from the hyperthermostable bacterium Thermotoga maritima
    • Jaenicke R., Schurig H., Beaucamp N., and Ostendorp R. Structure and stability of hyperstable proteins: Glycolytic enzymes from the hyperthermostable bacterium Thermotoga maritima. Adv. Protein Chem. 48 (1996) 181-269
    • (1996) Adv. Protein Chem. , vol.48 , pp. 181-269
    • Jaenicke, R.1    Schurig, H.2    Beaucamp, N.3    Ostendorp, R.4
  • 46
    • 0024298964 scopus 로고
    • How do enzymes work?
    • Kraut J. How do enzymes work?. Science 242 (1988) 533-540
    • (1988) Science , vol.242 , pp. 533-540
    • Kraut, J.1
  • 47
    • 0031467464 scopus 로고    scopus 로고
    • Dynamics and unfolding pathways of a hyperthermophilic and a mesophilic rubredoxin
    • Lazaridis T., Lee I., and Karplus M. Dynamics and unfolding pathways of a hyperthermophilic and a mesophilic rubredoxin. Protein Sci. 6 (1997) 2589-2605
    • (1997) Protein Sci. , vol.6 , pp. 2589-2605
    • Lazaridis, T.1    Lee, I.2    Karplus, M.3
  • 48
    • 0026728020 scopus 로고
    • Cumulative stabilizing effects of glycine to alanine substitutions in Bacillus subtilis neutral protease
    • Margarit I., Campagnoli S., Frigerio F., Grandi G., De Filippis V., and Fontana A. Cumulative stabilizing effects of glycine to alanine substitutions in Bacillus subtilis neutral protease. Protein Eng. 5 (1992) 543-550
    • (1992) Protein Eng. , vol.5 , pp. 543-550
    • Margarit, I.1    Campagnoli, S.2    Frigerio, F.3    Grandi, G.4    De Filippis, V.5    Fontana, A.6
  • 49
    • 0024972502 scopus 로고
    • Substantial increase of protein stability by multiple disulfide bonds
    • Matsumura M., Signor G., and Matthews B.W. Substantial increase of protein stability by multiple disulfide bonds. Nature 142 (1989) 291-293
    • (1989) Nature , vol.142 , pp. 291-293
    • Matsumura, M.1    Signor, G.2    Matthews, B.W.3
  • 50
    • 0022538679 scopus 로고
    • Cumulative effect of intragenic amino acid replacements on the thermostability of a protein
    • Matsumura M., Yasumura S., and Aiba S. Cumulative effect of intragenic amino acid replacements on the thermostability of a protein. Nature 323 (1986) 356-358
    • (1986) Nature , vol.323 , pp. 356-358
    • Matsumura, M.1    Yasumura, S.2    Aiba, S.3
  • 51
    • 0023643422 scopus 로고
    • Genetic and structural analysis of the protein stability problem
    • Matthews B.W. Genetic and structural analysis of the protein stability problem. Biochemistry 26 (1987) 6885-6888
    • (1987) Biochemistry , vol.26 , pp. 6885-6888
    • Matthews, B.W.1
  • 52
    • 0001093159 scopus 로고
    • Mutational analysis of protein stability
    • Matthews B.W. Mutational analysis of protein stability. Curr. Opin. Struct. Biol. 1 (1991) 17-21
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 17-21
    • Matthews, B.W.1
  • 53
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Matthews B.W. Structural and genetic analysis of protein stability. Annu. Rev. Biochem. 62 (1993) 139-160
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 54
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site directed mutations that decrease the entropy of unfolding
    • Matthews B.W., Nicholson H., and Becktel W. Enhanced protein thermostability from site directed mutations that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. USA 84 (1987) 6663-6667
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.3
  • 55
    • 0018146009 scopus 로고
    • Is protein turnover thermodynamically controlled?
    • McLendon C., and Radany E. Is protein turnover thermodynamically controlled?. J. Biol. Chem. 253 (1978) 6335-6337
    • (1978) J. Biol. Chem. , vol.253 , pp. 6335-6337
    • McLendon, C.1    Radany, E.2
  • 56
    • 0024974452 scopus 로고
    • Engineering thermal stability: Sequence statistics point to residue substitutions in α-helices
    • Menéndez-Arias L., and Argos P. Engineering thermal stability: Sequence statistics point to residue substitutions in α-helices. J. Mol. Biol. 206 (1989) 397-406
    • (1989) J. Mol. Biol. , vol.206 , pp. 397-406
    • Menéndez-Arias, L.1    Argos, P.2
  • 57
    • 0031406972 scopus 로고    scopus 로고
    • Improving the thermostability of Bacillus stearothermophilus neutral protease by introducing proline into the active site helix
    • Nakamura S., Tanaka T., Yada R.Y., and Nakai S. Improving the thermostability of Bacillus stearothermophilus neutral protease by introducing proline into the active site helix. Protein Eng. 10 (1997) 1263-1269
    • (1997) Protein Eng. , vol.10 , pp. 1263-1269
    • Nakamura, S.1    Tanaka, T.2    Yada, R.Y.3    Nakai, S.4
  • 58
    • 0031415284 scopus 로고    scopus 로고
    • Subtilisin from psychrophilic antarctic bacteria: Characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold
    • Narinx E., Baise E., and Gerday C. Subtilisin from psychrophilic antarctic bacteria: Characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold. Protein Eng. 10 (1997) 1271-1279
    • (1997) Protein Eng. , vol.10 , pp. 1271-1279
    • Narinx, E.1    Baise, E.2    Gerday, C.3
  • 59
    • 0028179634 scopus 로고
    • Predicting calcium-binding sites in proteins
    • Nayal M., and Di Cera E. Predicting calcium-binding sites in proteins. Proc. Natl. Acad. Sci. USA 91 (1994) 817-821
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 817-821
    • Nayal, M.1    Di Cera, E.2
  • 60
    • 0021879452 scopus 로고
    • Effect of single amino acid substitutions on the protease susceptibility of tryptophan synthase alpha subunit
    • Ogasahara K., Tsunasawa S., Soda Y., Yutani K., and Sugino Y. Effect of single amino acid substitutions on the protease susceptibility of tryptophan synthase alpha subunit. Eur. J. Biochem. 150 (1985) 17-21
    • (1985) Eur. J. Biochem. , vol.150 , pp. 17-21
    • Ogasahara, K.1    Tsunasawa, S.2    Soda, Y.3    Yutani, K.4    Sugino, Y.5
  • 61
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil K.T., and De Grado W.F. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science 250 (1990) 646-651
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    De Grado, W.F.2
  • 62
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2
    • Perutz L., and Raidt H. Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2. Nature 255 (1975) 256-259
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, L.1    Raidt, H.2
  • 63
    • 0029932580 scopus 로고    scopus 로고
    • Analysis of protein conformational characteristics related to thermostability
    • Querol E., Perez-Pons J.A., and Mozo-Villarias A. Analysis of protein conformational characteristics related to thermostability. Protein Eng. 9 (1996) 265-271
    • (1996) Protein Eng. , vol.9 , pp. 265-271
    • Querol, E.1    Perez-Pons, J.A.2    Mozo-Villarias, A.3
  • 64
    • 0029644328 scopus 로고
    • Hyperthermophiles: Taking the heat and loving it
    • Rees D.C., and Adams M.W.W. Hyperthermophiles: Taking the heat and loving it. Structure 3 (1995) 251-254
    • (1995) Structure , vol.3 , pp. 251-254
    • Rees, D.C.1    Adams, M.W.W.2
  • 65
    • 0026648514 scopus 로고
    • Stability and reconstitution of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima
    • Rehaber V., and Jaenicke R. Stability and reconstitution of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima. J. Biol. Chem. 267 (1992) 10999-11006
    • (1992) J. Biol. Chem. , vol.267 , pp. 10999-11006
    • Rehaber, V.1    Jaenicke, R.2
  • 66
    • 84907035182 scopus 로고
    • The structural and funcional roles of metal ions in thermolysin
    • Roche R.S., and Voordouw G. The structural and funcional roles of metal ions in thermolysin. CRC Crit. Rev. Biochem. 5 (1978) 1-23
    • (1978) CRC Crit. Rev. Biochem. , vol.5 , pp. 1-23
    • Roche, R.S.1    Voordouw, G.2
  • 67
    • 0027263501 scopus 로고
    • Regulation of autoproteolysis of the HIV-1 and HIV-2 proteases with engineered amino acid substitution
    • Rosé JR., Salto R., and Craik C.S. Regulation of autoproteolysis of the HIV-1 and HIV-2 proteases with engineered amino acid substitution. J. Biol. Chem. 268 (1993) 11939-11945
    • (1993) J. Biol. Chem. , vol.268 , pp. 11939-11945
    • Rosé, JR.1    Salto, R.2    Craik, C.S.3
  • 68
    • 0029099960 scopus 로고
    • Engineering thermostability: Lessons from thermophilic proteins
    • Russell R.J.M., and Taylor G.L. Engineering thermostability: Lessons from thermophilic proteins. Curr. Opin. Biotechnol. 6 (1995) 370-374
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 370-374
    • Russell, R.J.M.1    Taylor, G.L.2
  • 69
    • 77957061526 scopus 로고
    • Proteolysis as a probe for motility in mutant bacteriophage T4 lysozyme
    • Schellman C. Proteolysis as a probe for motility in mutant bacteriophage T4 lysozyme. Biophys. J. 49 (1986) 4932
    • (1986) Biophys. J. , vol.49 , pp. 4932
    • Schellman, C.1
  • 71
  • 72
    • 0028949615 scopus 로고
    • Proteins and temperature
    • Somero G.N. Proteins and temperature. Annu. Rev. Physiol. 57 (1995) 43-68
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 43-68
    • Somero, G.N.1
  • 73
    • 0020980077 scopus 로고
    • Advantages of using thermophiles in biotechnological processes: Expectations and reality
    • Sonnleitner B., and Fiechter A. Advantages of using thermophiles in biotechnological processes: Expectations and reality. Trends Biotechnol. 1 (1983) 74-80
    • (1983) Trends Biotechnol. , vol.1 , pp. 74-80
    • Sonnleitner, B.1    Fiechter, A.2
  • 74
    • 0016905006 scopus 로고
    • Structural and functional properties of thermophilic enolase
    • Enzymes and proteins from thermophilic microorganisms. Zuber H. (Ed), Birkäuser Verlag, Basel
    • Stellwagen E., and Barnes L.D. Structural and functional properties of thermophilic enolase. In: Zuber H. (Ed). Enzymes and proteins from thermophilic microorganisms. Experientia Suppl. 26 (1976), Birkäuser Verlag, Basel 223-228
    • (1976) Experientia Suppl. , vol.26 , pp. 223-228
    • Stellwagen, E.1    Barnes, L.D.2
  • 75
    • 0015919528 scopus 로고
    • A thermostable enolase from the extreme thermophile Thermus aquaticus YT-1
    • Stellwagen E., Cronlund M.M., and Barnes L.D. A thermostable enolase from the extreme thermophile Thermus aquaticus YT-1. Biochemistry 12 (1973) 1552-1559
    • (1973) Biochemistry , vol.12 , pp. 1552-1559
    • Stellwagen, E.1    Cronlund, M.M.2    Barnes, L.D.3
  • 76
    • 0000163923 scopus 로고
    • The lessons of archaebacteria
    • Early life on hearth. S. B. (Ed), Columbia University Press, New York
    • Early life on hearth. Stetter KO. The lessons of archaebacteria. In: S. B. (Ed). Nobel Symposium 84 (1993), Columbia University Press, New York 101-109
    • (1993) Nobel Symposium 84 , pp. 101-109
    • Stetter, KO.1
  • 78
    • 0019323530 scopus 로고
    • Malate dehydrogenase from thermophilic and mesophilic bacteria: Molecular size, subunit structure, amino acid composition, immunochemical homology and catalytic activity
    • Sundaram T.K., Wright I.P., and Wilkinson A.E. Malate dehydrogenase from thermophilic and mesophilic bacteria: Molecular size, subunit structure, amino acid composition, immunochemical homology and catalytic activity. Biochemistry 19 (1980) 2017-2022
    • (1980) Biochemistry , vol.19 , pp. 2017-2022
    • Sundaram, T.K.1    Wright, I.P.2    Wilkinson, A.E.3
  • 79
    • 0019971766 scopus 로고
    • Abnormally high tolerance against proteolysis of an exo-oligo-1,6-glucosidase from thermophile Bacillus thermoglucosidicus RP 1006, compared with its mesophilic counterpart from Bacillus cereus ATCC 7064
    • Suzuki S., and Imai T. Abnormally high tolerance against proteolysis of an exo-oligo-1,6-glucosidase from thermophile Bacillus thermoglucosidicus RP 1006, compared with its mesophilic counterpart from Bacillus cereus ATCC 7064. Biochim. Biophys. Acta 705 (1982) 124-126
    • (1982) Biochim. Biophys. Acta , vol.705 , pp. 124-126
    • Suzuki, S.1    Imai, T.2
  • 80
    • 77957094495 scopus 로고    scopus 로고
    • Adaptation of a thermophilic isopropylmalate dehydrogenase to mesophilic temperature
    • Commun. TU-137. Budapest, 17-21 August 1997
    • Commun. TU-137. Suzuki S., Yamagishi A., and Oshima T. Adaptation of a thermophilic isopropylmalate dehydrogenase to mesophilic temperature. Proc. 8th Eur. Congress on Biotechnology. Budapest, 17-21 August 1997 (1997)
    • (1997) Proc. 8th Eur. Congress on Biotechnology
    • Suzuki, S.1    Yamagishi, A.2    Oshima, T.3
  • 81
    • 0001767586 scopus 로고
    • A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidases
    • Suzuki Y., Oishi K., Nakano H., and Nagayama T. A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidases. Appl. Microbiol. Biotechnol. 26 (1987) 546-551
    • (1987) Appl. Microbiol. Biotechnol. , vol.26 , pp. 546-551
    • Suzuki, Y.1    Oishi, K.2    Nakano, H.3    Nagayama, T.4
  • 84
    • 77956810106 scopus 로고
    • Structural fluctuation of protein and thermophily
    • M. F. (Ed), Academic Press, New York
    • Tsuboi M., Ohta S., and Nakanishi M. Structural fluctuation of protein and thermophily. In: M. F. (Ed). Biochemistry of thermophily (1978), Academic Press, New York 251-266
    • (1978) Biochemistry of thermophily , pp. 251-266
    • Tsuboi, M.1    Ohta, S.2    Nakanishi, M.3
  • 85
    • 0031922228 scopus 로고    scopus 로고
    • Rendering one autolysis site in Bacillus subtilis neutral protease resistant to cleavage reveals a new fission
    • Van den Burg B., Eijsink V.G.H., Vriend G., Veltman O.R., and Venema G. Rendering one autolysis site in Bacillus subtilis neutral protease resistant to cleavage reveals a new fission. Biotechnol. Appl Biochem. 27 (1998) 125-132
    • (1998) Biotechnol. Appl Biochem. , vol.27 , pp. 125-132
    • Van den Burg, B.1    Eijsink, V.G.H.2    Vriend, G.3    Veltman, O.R.4    Venema, G.5
  • 87
    • 0025822794 scopus 로고
    • Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus
    • Varley P.G., and Pain R.H. Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus. J. Mol Biol. 220 (1991) 531-538
    • (1991) J. Mol Biol. , vol.220 , pp. 531-538
    • Varley, P.G.1    Pain, R.H.2
  • 88
    • 0021376962 scopus 로고
    • General stability of thermophilic enzymes: Studies on 6-phosphogluconate dehydrogenase from B. stearothermophilus and yeast
    • Veronese F.M., Boccù E., Schiavon O., Grandi C., and Fontana A. General stability of thermophilic enzymes: Studies on 6-phosphogluconate dehydrogenase from B. stearothermophilus and yeast. J. Appl Biochem. 6 (1984) 39-47
    • (1984) J. Appl Biochem. , vol.6 , pp. 39-47
    • Veronese, F.M.1    Boccù, E.2    Schiavon, O.3    Grandi, C.4    Fontana, A.5
  • 89
    • 0029893110 scopus 로고    scopus 로고
    • Thermoenzymes: Identifying molecular determinants of protein structural and functional stability
    • Vieille C., and Zeikus J.G. Thermoenzymes: Identifying molecular determinants of protein structural and functional stability. Trends Biotechnol. 14 (1996) 183-191
    • (1996) Trends Biotechnol. , vol.14 , pp. 183-191
    • Vieille, C.1    Zeikus, J.G.2
  • 91
    • 0023557882 scopus 로고
    • Relationship of protein flexibility to thermostability
    • Vihinen M. Relationship of protein flexibility to thermostability. Protein Eng. 1 (1987) 477-480
    • (1987) Protein Eng. , vol.1 , pp. 477-480
    • Vihinen, M.1
  • 93
    • 0011186093 scopus 로고    scopus 로고
    • Protein thermal stability: Hydrogen bonds or internal packing?
    • Vogt G., and Argos P. Protein thermal stability: Hydrogen bonds or internal packing?. Folding &Design 2 (1997) 540-546
    • (1997) Folding &Design , vol.2 , pp. 540-546
    • Vogt, G.1    Argos, P.2
  • 94
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds and ion pairs
    • Vogt G., Woell S., and Argos P. Protein thermal stability, hydrogen bonds and ion pairs. J. Mol. Biol. 269 (1997) 631-643
    • (1997) J. Mol. Biol. , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 95
    • 0028130117 scopus 로고
    • Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC-7064 oligo-1,6-glucosidase
    • Watanabe K., Masuda T., Ohashi H., Mihaya H., and Suzuki Y. Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC-7064 oligo-1,6-glucosidase. Eur. J. Biochem. 226 (1994) 277-283
    • (1994) Eur. J. Biochem. , vol.226 , pp. 277-283
    • Watanabe, K.1    Masuda, T.2    Ohashi, H.3    Mihaya, H.4    Suzuki, Y.5
  • 96
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells J.A. Additivity of mutational effects in proteins. Biochemistry 29 (1990) 8509-8517
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1
  • 97
    • 0025182490 scopus 로고
    • Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima
    • Wraba A., Schweiger A., Schultes V., Jaenicke R., and Závodszky P. Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima. Biochemistry 29 (1990) 7584-7592
    • (1990) Biochemistry , vol.29 , pp. 7584-7592
    • Wraba, A.1    Schweiger, A.2    Schultes, V.3    Jaenicke, R.4    Závodszky, P.5
  • 98
    • 0344540139 scopus 로고
    • Amide proton exchange and stability of proteins
    • Wüthrich K., and Wagner G. Amide proton exchange and stability of proteins. J. Mol. Biol. 130 (1979) 31-37
    • (1979) J. Mol. Biol. , vol.130 , pp. 31-37
    • Wüthrich, K.1    Wagner, G.2
  • 99
    • 77956869116 scopus 로고
    • Internal mobility and unfolding of globular proteins
    • Jaenicke R. (Ed), Elsevier/North Holland Biomedical Press, Amsterdam-New York
    • Wüthrich K., Roder H., and Wagner G. Internal mobility and unfolding of globular proteins. In: Jaenicke R. (Ed). Protein folding (1980), Elsevier/North Holland Biomedical Press, Amsterdam-New York 549-564
    • (1980) Protein folding , pp. 549-564
    • Wüthrich, K.1    Roder, H.2    Wagner, G.3
  • 100
    • 0000390128 scopus 로고    scopus 로고
    • Glycine residues provide flexibility for enzyme active sites
    • Yan B.X., and Sun Y.Q. Glycine residues provide flexibility for enzyme active sites. J. Biol. Chem. 272 (1997) 3190-3194
    • (1997) J. Biol. Chem. , vol.272 , pp. 3190-3194
    • Yan, B.X.1    Sun, Y.Q.2
  • 102
    • 0029585945 scopus 로고
    • Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive
    • Zhang T., Baase W.A., Shoichet B.K., Wilson K.P., and Matthews B.W. Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. Protein Eng. 8 (1995) 1017-1022
    • (1995) Protein Eng. , vol.8 , pp. 1017-1022
    • Zhang, T.1    Baase, W.A.2    Shoichet, B.K.3    Wilson, K.P.4    Matthews, B.W.5
  • 103
    • 5544279995 scopus 로고
    • Structure and function of thermophilic enzymes
    • Eggerer H., and Huber R. (Eds), Springer Verlag, Heidelberg
    • Zuber H. Structure and function of thermophilic enzymes. In: Eggerer H., and Huber R. (Eds). Structural and functional aspects of enzyme catalysis (1981), Springer Verlag, Heidelberg 114-127
    • (1981) Structural and functional aspects of enzyme catalysis , pp. 114-127
    • Zuber, H.1


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