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Volumn 60, Issue 4, 2003, Pages 648-662

Molecular adaptations to cold in psychrophilic enzymes

Author keywords

Biophysics; Crystal structure; Enzyme kinetics; Extremophile; Folding; Mutagenesis; Psychrophile

Indexed keywords

ENZYME; PSYCHROPHILIC ENZYME; UNCLASSIFIED DRUG;

EID: 0037688133     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-2155-3     Document Type: Review
Times cited : (182)

References (102)
  • 1
    • 0030681366 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Molecular basis of cold adaptation
    • Feller G. and Gerday C. (1997) Psychrophilic enzymes: molecular basis of cold adaptation. Cell. Mol. Life Sci. 53: 830-841
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 830-841
    • Feller, G.1    Gerday, C.2
  • 5
    • 0031608378 scopus 로고    scopus 로고
    • Molecular adaptations in psychrophilic bacteria: Potential for biotechnological applications
    • Russell N. J. (1998) Molecular adaptations in psychrophilic bacteria: potential for biotechnological applications. Adv. Biochem. Eng. Biotechnol. 61: 1-21
    • (1998) Adv. Biochem. Eng. Biotechnol. , vol.61 , pp. 1-21
    • Russell, N.J.1
  • 7
    • 0037197677 scopus 로고    scopus 로고
    • Maximal stabilities of reversible two-state proteins
    • Kumar S., Tsai C. J. and Nussinov R. (2002) Maximal stabilities of reversible two-state proteins. Biochemistry 41: 5359-5374
    • (2002) Biochemistry , vol.41 , pp. 5359-5374
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 8
    • 0033779402 scopus 로고    scopus 로고
    • Temperature adaptation of enzymes: Lessons from laboratory evolution
    • Wintrode P. L. and Arnold F. H. (2000) Temperature adaptation of enzymes: lessons from laboratory evolution. Adv. Protein Chem. 55: 161-225
    • (2000) Adv. Protein Chem. , vol.55 , pp. 161-225
    • Wintrode, P.L.1    Arnold, F.H.2
  • 9
    • 0032493439 scopus 로고    scopus 로고
    • The stability of the RNA bases: Implications for the origin of life
    • Levy M. and Miller S. L. (1998) The stability of the RNA bases: implications for the origin of life. Proc. Natl. Acad. Sci. USA 95: 7933-7938
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7933-7938
    • Levy, M.1    Miller, S.L.2
  • 10
    • 0000607682 scopus 로고    scopus 로고
    • A habitat for psychrophiles in deep Antarctic ice
    • Price P. B. (2000) A habitat for psychrophiles in deep Antarctic ice. Proc. Natl. Acad. Sci. USA 97: 1247-1251
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1247-1251
    • Price, P.B.1
  • 11
    • 0036270790 scopus 로고    scopus 로고
    • Psychrophiles and polar regions
    • Deming J. W. (2002) Psychrophiles and polar regions. Curr. Opin. Microbiol. 5: 301-309
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 301-309
    • Deming, J.W.1
  • 12
    • 0016516090 scopus 로고
    • Psychrophilic bacteria
    • Morita R. Y. (1975) Psychrophilic bacteria. Bacteriol. Rev. 39: 144-167
    • (1975) Bacteriol. Rev. , vol.39 , pp. 144-167
    • Morita, R.Y.1
  • 13
    • 0035918263 scopus 로고    scopus 로고
    • Influence of moderate temperatures on myristoyl-CoA metabolism and acyl-CoA thioesterase activity in the psychrophilic Antarctic yeast Rhodotorula aurantiaca
    • Sabri A., Bare G., Jacques R, Jabrane A., Ongena M., Van Heugen J. C. et al. (2001) Influence of moderate temperatures on myristoyl-CoA metabolism and acyl-CoA thioesterase activity in the psychrophilic Antarctic yeast Rhodotorula aurantiaca. J. Biol. Chem. 276: 12691-12696
    • (2001) J. Biol. Chem. , vol.276 , pp. 12691-12696
    • Sabri, A.1    Bare, G.2    Jacques, R.3    Jabrane, A.4    Ongena, M.5    Van Heugen, J.C.6
  • 15
    • 0034244561 scopus 로고    scopus 로고
    • Thermolabile xylanase of the Antarctic yeast Cryptococcus adeliae: Production and properties
    • Gomes J., Gomes I. and Steiner W. (2000) Thermolabile xylanase of the Antarctic yeast Cryptococcus adeliae: production and properties. Extremophiles 4: 227-235
    • (2000) Extremophiles , vol.4 , pp. 227-235
    • Gomes, J.1    Gomes, I.2    Steiner, W.3
  • 16
    • 0031668781 scopus 로고    scopus 로고
    • Heat shock response in psychrophilic and psychrotrophic yeast from Antarctica
    • Deegenaars M. L. and Watson K. (1998) Heat shock response in psychrophilic and psychrotrophic yeast from Antarctica. Extremophiles 2: 41-49
    • (1998) Extremophiles , vol.2 , pp. 41-49
    • Deegenaars, M.L.1    Watson, K.2
  • 17
    • 0031684804 scopus 로고    scopus 로고
    • Rubisco adaptation to low temperatures: A comparative study in psychrophilic and mesophilic unicellular algae
    • Devos N., Ingouff M., Loppes R. and Matagne R. F. (1998) Rubisco adaptation to low temperatures: a comparative study in psychrophilic and mesophilic unicellular algae. J. Phycol. 34: 655-660
    • (1998) J. Phycol. , vol.34 , pp. 655-660
    • Devos, N.1    Ingouff, M.2    Loppes, R.3    Matagne, R.F.4
  • 18
    • 0029739286 scopus 로고    scopus 로고
    • Effect of temperature on two enzymes from a psychrophilic Chloromonas (chlorophyta)
    • Loppes R., Devos N., Willem S., Bartelemy P. and Matagne R. F. (1996) Effect of temperature on two enzymes from a psychrophilic Chloromonas (chlorophyta). J. Phycol. 32: 276-278
    • (1996) J. Phycol. , vol.32 , pp. 276-278
    • Loppes, R.1    Devos, N.2    Willem, S.3    Bartelemy, P.4    Matagne, R.F.5
  • 19
    • 0033180374 scopus 로고    scopus 로고
    • Protein adaptation to low temperatures: A comparative study of alpha-tubulin sequences in mesophilic and psychrophilic algae
    • Willem S., Srahna M., Devos N., Gerday C., Loppes R. and Matagne R. F. (1999) Protein adaptation to low temperatures: a comparative study of alpha-tubulin sequences in mesophilic and psychrophilic algae. Extremophiles 3: 221-226
    • (1999) Extremophiles , vol.3 , pp. 221-226
    • Willem, S.1    Srahna, M.2    Devos, N.3    Gerday, C.4    Loppes, R.5    Matagne, R.F.6
  • 25
    • 0034736285 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Revisiting the thermodynamic parameters of activation may explain local flexibility
    • Lonhienne T, Gerday C. and Feller G. (2000) Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta. 1543: 1-10
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 1-10
    • Lonhienne, T.1    Gerday, C.2    Feller, G.3
  • 27
    • 0028949615 scopus 로고
    • Proteins and temperature
    • Somero G. N. (1995) Proteins and temperature. Annu. Rev. Physiol. 57: 43-68
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 43-68
    • Somero, G.N.1
  • 29
    • 0034731469 scopus 로고    scopus 로고
    • Approaches for deciphering the structural basis of low temperature enzyme activity
    • Sheridan P. P., Panasik N., Coombs J. M. and Brenchley J. E. (2000) Approaches for deciphering the structural basis of low temperature enzyme activity. Biochim. Biophys. Acta. 1543: 417-433
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 417-433
    • Sheridan, P.P.1    Panasik, N.2    Coombs, J.M.3    Brenchley, J.E.4
  • 30
    • 0034170458 scopus 로고    scopus 로고
    • Toward a molecular understanding of cold activity of enzymes from psychrophiles
    • Russell N. J. (2000) Toward a molecular understanding of cold activity of enzymes from psychrophiles. Extremophiles 4: 83-90
    • (2000) Extremophiles , vol.4 , pp. 83-90
    • Russell, N.J.1
  • 31
    • 0008796214 scopus 로고    scopus 로고
    • Cold-adapted microorganisms: Adaptation strategies and biotechnological potential
    • Bitton G. (ed.), Wiley, New York
    • Margesin R., Feller G., Gerday C. and Russell N. J. (2002) Cold-adapted microorganisms: adaptation strategies and biotechnological potential. In: Encyclopedia of Environmental Microbiology, vol. 2, pp. 871-885, Bitton G. (ed.), Wiley, New York
    • (2002) Encyclopedia of Environmental Microbiology , vol.2 , pp. 871-885
    • Margesin, R.1    Feller, G.2    Gerday, C.3    Russell, N.J.4
  • 32
    • 0034973280 scopus 로고    scopus 로고
    • Protein function at thermal extremes: Balancing stability and flexibility
    • Fields P. A. (2001) Protein function at thermal extremes: balancing stability and flexibility. Comp. Biochem Physiol. A Mol. Integr. Physiol. 129: 417-431
    • (2001) Comp. Biochem Physiol. A Mol. Integr. Physiol. , vol.129 , pp. 417-431
    • Fields, P.A.1
  • 34
    • 0025773328 scopus 로고
    • Cloning and expression in Escherichia coli of three lipase-encoding genes from the psychrotrophic Antarctic strain Moraxella TA 144
    • Feller G., Thiry M., Arpigny J. L. and Gerday C. (1991) Cloning and expression in Escherichia coli of three lipase-encoding genes from the psychrotrophic Antarctic strain Moraxella TA 144. Gene 102: 111-115
    • (1991) Gene , vol.102 , pp. 111-115
    • Feller, G.1    Thiry, M.2    Arpigny, J.L.3    Gerday, C.4
  • 35
    • 0025732362 scopus 로고
    • Nucleotide sequence of the lipase gene lip2 from the Antarctic psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine residues
    • Feller G., Thiry M. and Gerday C. (1991) Nucleotide sequence of the lipase gene lip2 from the Antarctic psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine residues. DNA Cell. Biol. 10: 381-388
    • (1991) DNA Cell. Biol. , vol.10 , pp. 381-388
    • Feller, G.1    Thiry, M.2    Gerday, C.3
  • 36
    • 0026576411 scopus 로고
    • Nucleotide and derived amino acid sequence of the subtilisin from the Antarctic psychrotroph Bacillus TA39
    • Narinx E., Davail S., Feller G. and Gerday C. (1992) Nucleotide and derived amino acid sequence of the subtilisin from the Antarctic psychrotroph Bacillus TA39. Biochim. Biophys. Acta 1131: 111-113
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 111-113
    • Narinx, E.1    Davail, S.2    Feller, G.3    Gerday, C.4
  • 37
    • 0028292010 scopus 로고
    • Cold adaptation of proteins: Purification, characterization, and sequence of the heat-labile subtilisin from the Antarctic psychrophile Bacillus TA41
    • Davail S., Feller G., Narinx E. and Gerday C. (1994) Cold adaptation of proteins: purification, characterization, and sequence of the heat-labile subtilisin from the Antarctic psychrophile Bacillus TA41. J. Biol. Chem. 269: 17448-17453
    • (1994) J. Biol. Chem. , vol.269 , pp. 17448-17453
    • Davail, S.1    Feller, G.2    Narinx, E.3    Gerday, C.4
  • 38
    • 0027397742 scopus 로고
    • Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria: Structural comparison of the predicted protein sequences
    • Rentier-Delrue F., Mande S. C., Moyens S., Terpstra P., Mainfroid V., Goraj K. et al. (1993) Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria: structural comparison of the predicted protein sequences. J. Mol. Biol. 229: 85-93
    • (1993) J. Mol. Biol. , vol.229 , pp. 85-93
    • Rentier-Delrue, F.1    Mande, S.C.2    Moyens, S.3    Terpstra, P.4    Mainfroid, V.5    Goraj, K.6
  • 39
    • 0036545550 scopus 로고    scopus 로고
    • Thermodynamic activation properties of elongation factor 2 (EF-2) proteins from psychrotolerant and thermophilic Archaea
    • Siddiqui K. S., Cavicchioli R and Thomas T. (2002) Thermodynamic activation properties of elongation factor 2 (EF-2) proteins from psychrotolerant and thermophilic Archaea. Extremophiles 6: 143-150
    • (2002) Extremophiles , vol.6 , pp. 143-150
    • Siddiqui, K.S.1    Cavicchioli, R.2    Thomas, T.3
  • 40
    • 0033982036 scopus 로고    scopus 로고
    • Effect of temperature on stability and activity of elongation factor 2 proteins from Antarctic and thermophilic methanogens
    • Thomas T and Cavicchioli R. (2000) Effect of temperature on stability and activity of elongation factor 2 proteins from Antarctic and thermophilic methanogens. J. Bacteriol. 182: 1328-1332
    • (2000) J. Bacteriol. , vol.182 , pp. 1328-1332
    • Thomas, T.1    Cavicchioli, R.2
  • 41
    • 0035108129 scopus 로고    scopus 로고
    • Effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens
    • Thomas T, Kumar N. and Cavicchioli R. (2001) Effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens. J. Bacteriol. 183: 1974-1982
    • (2001) J. Bacteriol. , vol.183 , pp. 1974-1982
    • Thomas, T.1    Kumar, N.2    Cavicchioli, R.3
  • 42
    • 0034687760 scopus 로고    scopus 로고
    • Psychrophilic elongation factor Tu from the Antarctic Moraxella sp. Tac II 25: Biochemical characterization and cloning of the encoding gene
    • Masullo M., Arcari P., Paola B. de, Parmeggiani A. and Bocchini V. (2000) Psychrophilic elongation factor Tu from the Antarctic Moraxella sp. Tac II 25: biochemical characterization and cloning of the encoding gene. Biochemistry 39: 15531-15539
    • (2000) Biochemistry , vol.39 , pp. 15531-15539
    • Masullo, M.1    Arcari, P.2    De Paola, B.3    Parmeggiani, A.4    Bocchini, V.5
  • 43
    • 0033946342 scopus 로고    scopus 로고
    • A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures
    • Georlette D., Jonsson Z. O., Van Petegem F., Chessa J., Van Beeumen J., Hubscher U. et al. (2000) A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures. Eur. J. Biochem. 267: 3502-3512
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3502-3512
    • Georlette, D.1    Jonsson, Z.O.2    Van Petegem, F.3    Chessa, J.4    Van Beeumen, J.5    Hubscher, U.6
  • 44
    • 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. (1997) Subtilisin from psychrophilic Antarctic bacteria: characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold. Protein. Eng. 10: 1271-1279
    • (1997) Protein. Eng. , vol.10 , pp. 1271-1279
    • Narinx, E.1    Baise, E.2    Gerday, C.3
  • 45
    • 0034644667 scopus 로고    scopus 로고
    • Cold adaptation of a mesophilic subtilisin-like protease by laboratory evolution
    • Wintrode P. L., Miyazaki K. and Arnold F. H. (2000) Cold adaptation of a mesophilic subtilisin-like protease by laboratory evolution. J. Biol. Chem. 275: 31635-31640
    • (2000) J. Biol. Chem. , vol.275 , pp. 31635-31640
    • Wintrode, P.L.1    Miyazaki, K.2    Arnold, F.H.3
  • 46
    • 0031887070 scopus 로고    scopus 로고
    • Expression of psychrophilic genes in mesophilic hosts: Assessment of the folding state of a recombinant alpha-amylase
    • Feller G., Le Bussy O. and Gerday C. (1998) Expression of psychrophilic genes in mesophilic hosts: assessment of the folding state of a recombinant alpha-amylase. Appl. Environ. Microbiol. 64: 1163-1165
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1163-1165
    • Feller, G.1    Le Bussy, O.2    Gerday, C.3
  • 47
    • 0032534759 scopus 로고    scopus 로고
    • Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level
    • Aghajari N., Feller G., Gerday C. and Haser R. (1998) Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level. Structure 6: 1503-1516
    • (1998) Structure , vol.6 , pp. 1503-1516
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 48
    • 0034646605 scopus 로고    scopus 로고
    • Structural, kinetic, and calorimetric characterization of the cold-active phosphoglycerate kinase from the Antarctic Pseudomonas sp. TACII18
    • Bentahir M., Feller G, Aittaleb M., Lamotte-Brasseur J., Himri T., Chessa J. P. et al. (2000) Structural, kinetic, and calorimetric characterization of the cold-active phosphoglycerate kinase from the Antarctic Pseudomonas sp. TACII18. J. Biol. Chem. 275: 11147-11153
    • (2000) J. Biol. Chem. , vol.275 , pp. 11147-11153
    • Bentahir, M.1    Feller, G.2    Aittaleb, M.3    Lamotte-Brasseur, J.4    Himri, T.5    Chessa, J.P.6
  • 49
    • 0035430835 scopus 로고    scopus 로고
    • A novel replication element from an Antarctic plasmid as a tool for the expression of proteins at low temperature
    • Tutino M. L., Duilio A., Parrilli R., Remaut E., Sannia G. and Marino G. (2001) A novel replication element from an Antarctic plasmid as a tool for the expression of proteins at low temperature. Extremophiles 5: 257-264
    • (2001) Extremophiles , vol.5 , pp. 257-264
    • Tutino, M.L.1    Duilio, A.2    Parrilli, R.3    Remaut, E.4    Sannia, G.5    Marino, G.6
  • 50
    • 0031910806 scopus 로고    scopus 로고
    • Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor
    • Aghajari N., Feller G., Gerday C. and Haser R. (1998) Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Protein Sci. 7: 564-572
    • (1998) Protein Sci. , vol.7 , pp. 564-572
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 51
    • 0031941134 scopus 로고    scopus 로고
    • Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus: Kinetic and structural properties
    • Alvarez M., Zeelen J. P., Mainfroid V., Rentier-Delrue F., Martial J. A., Wyns L. et al. (1998) Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus: kinetic and structural properties. J. Biol. Chem. 273: 2199-2206
    • (1998) J. Biol. Chem. , vol.273 , pp. 2199-2206
    • Alvarez, M.1    Zeelen, J.P.2    Mainfroid, V.3    Rentier-Delrue, F.4    Martial, J.A.5    Wyns, L.6
  • 52
    • 0033597205 scopus 로고    scopus 로고
    • Structural basis for cold adaptation: Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum
    • Kim S. Y., Hwang K. Y., Kim S. H., Sung H. C., Han Y. S. and Cho Y. J. (1999) Structural basis for cold adaptation: sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum. J. Biol. Chem. 274: 11761-11767
    • (1999) J. Biol. Chem. , vol.274 , pp. 11761-11767
    • Kim, S.Y.1    Hwang, K.Y.2    Kim, S.H.3    Sung, H.C.4    Han, Y.S.5    Cho, Y.J.6
  • 53
    • 0032521220 scopus 로고    scopus 로고
    • Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium
    • Russell R. J., Gerike U., Danson M. J., Hough D. W. and Taylor G. L. (1998) Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium. Structure 6: 351-361
    • (1998) Structure , vol.6 , pp. 351-361
    • Russell, R.J.1    Gerike, U.2    Danson, M.J.3    Hough, D.W.4    Taylor, G.L.5
  • 54
    • 0028033122 scopus 로고
    • Cold adaptation of enzymes: Structural comparison between salmon and bovine trypsins
    • Smalas A. O., Heimstad E. S., Hordvik A., Willassen N. P. and Male R. (1994) Cold adaptation of enzymes: structural comparison between salmon and bovine trypsins. Proteins 20: 149-166
    • (1994) Proteins , vol.20 , pp. 149-166
    • Smalas, A.O.1    Heimstad, E.S.2    Hordvik, A.3    Willassen, N.P.4    Male, R.5
  • 55
    • 0029187318 scopus 로고
    • Structure of native pancreatic elastase from north Atlantic salmon at 1.61 Å resolution
    • Berglund G. I., Willassen N. P., Hordvik A. and Smalas A. O. (1995) Structure of native pancreatic elastase from north Atlantic salmon at 1.61 Å resolution. Acta Cryst. D 51: 925-937
    • (1995) Acta Cryst. D , vol.51 , pp. 925-937
    • Berglund, G.I.1    Willassen, N.P.2    Hordvik, A.3    Smalas, A.O.4
  • 56
    • 0031888333 scopus 로고    scopus 로고
    • Structure and proposed amino-acid sequence of a pepsin from Atlantic cod (Gadus morhua)
    • Karlsen S., Hough E. and Olsen R. (1998) Structure and proposed amino-acid sequence of a pepsin from Atlantic cod (Gadus morhua). Acta Cryst. D 54: 32-46
    • (1998) Acta Cryst. D , vol.54 , pp. 32-46
    • Karlsen, S.1    Hough, E.2    Olsen, R.3
  • 57
    • 0030696497 scopus 로고    scopus 로고
    • Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile Pseudomonas aeruginosa
    • Villeret V., Chessa J. P., Gerday C. and Van Beeumen J. (1997) Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile Pseudomonas aeruginosa. Protein Sci. 6: 2462-2464
    • (1997) Protein Sci. , vol.6 , pp. 2462-2464
    • Villeret, V.1    Chessa, J.P.2    Gerday, C.3    Van Beeumen, J.4
  • 58
    • 0034767605 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase
    • Mandelman D., Bentahir M., Feller G., Gerday C. and Haser R. (2001) Crystallization and preliminary X-ray analysis of a bacterial psychrophilic enzyme, phosphoglycerate kinase. Acta Cryst. D 57: 1666-1668
    • (2001) Acta Cryst. D , vol.57 , pp. 1666-1668
    • Mandelman, D.1    Bentahir, M.2    Feller, G.3    Gerday, C.4    Haser, R.5
  • 59
    • 0034765691 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of a cold-adapted uracil-DNA glycosylase from Atlantic cod (Gadus morhua)
    • Leiros I., Lanes O., Sundheim O., Helland R., Smalas A. O. and Willassen N. P. (2001) Crystallization and preliminary X-ray diffraction analysis of a cold-adapted uracil-DNA glycosylase from Atlantic cod (Gadus morhua). Acta Cryst. D 57: 1706-1708
    • (2001) Acta Cryst. D , vol.57 , pp. 1706-1708
    • Leiros, I.1    Lanes, O.2    Sundheim, O.3    Helland, R.4    Smalas, A.O.5    Willassen, N.P.6
  • 60
    • 0005492283 scopus 로고    scopus 로고
    • Structural comparison of psychrophilic and mesophilic trypsins: Elucidating the molecular basis of cold-adaptation
    • Schroder Leiros H. K., Willassen N. P. and Smalas A. O. (2000) Structural comparison of psychrophilic and mesophilic trypsins: elucidating the molecular basis of cold-adaptation. Eur. J. Biochem. 267: 1039-1049
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1039-1049
    • Schroder Leiros, H.K.1    Willassen, N.P.2    Smalas, A.O.3
  • 61
    • 0344549848 scopus 로고    scopus 로고
    • Residue determinants and sequence analysis of cold-adapted trypsins
    • Leiros H. K., Willassen N. P. and Smalas A. O. (1999) Residue determinants and sequence analysis of cold-adapted trypsins. Extremophiles 3: 205-219
    • (1999) Extremophiles , vol.3 , pp. 205-219
    • Leiros, H.K.1    Willassen, N.P.2    Smalas, A.O.3
  • 62
    • 0036568335 scopus 로고    scopus 로고
    • Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes
    • Gianese G., Bossa F. and Pascarella S. (2002) Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes. Proteins 47: 236-249
    • (2002) Proteins , vol.47 , pp. 236-249
    • Gianese, G.1    Bossa, F.2    Pascarella, S.3
  • 63
    • 0028198814 scopus 로고
    • The active center of a mammalian alpha-amylase: Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2 Å resolution
    • Qian M., Haser R., Buisson G., Duee E. and Payan F. (1994) The active center of a mammalian alpha-amylase: structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2 Å resolution. Biochemistry 33: 6284-6294
    • (1994) Biochemistry , vol.33 , pp. 6284-6294
    • Qian, M.1    Haser, R.2    Buisson, G.3    Duee, E.4    Payan, F.5
  • 64
    • 0037007004 scopus 로고    scopus 로고
    • Crystallographic evidence of a transglycosylation reaction: Ternary complexes of a psychrophilic alpha-amylase
    • Aghajari N., Roth M. and Haser R. (2002) Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic alpha-amylase. Biochemistry 41: 4273-4280
    • (2002) Biochemistry , vol.41 , pp. 4273-4280
    • Aghajari, N.1    Roth, M.2    Haser, R.3
  • 65
    • 0035854688 scopus 로고    scopus 로고
    • Structural determinants of cold adaptation and stability in a large protein
    • D'Amico S., Gerday C. and Feller G. (2001) Structural determinants of cold adaptation and stability in a large protein. J. Biol. Chem. 276: 25791-25796
    • (2001) J. Biol. Chem. , vol.276 , pp. 25791-25796
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 66
    • 0032103265 scopus 로고    scopus 로고
    • Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123
    • Tsigos I., Velonia K., Smonou I. and Bouriotis V. (1998) Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123. Eur. J. Biochem. 254: 356-362
    • (1998) Eur. J. Biochem. , vol.254 , pp. 356-362
    • Tsigos, I.1    Velonia, K.2    Smonou, I.3    Bouriotis, V.4
  • 67
    • 0034257240 scopus 로고    scopus 로고
    • Electrostatics of mesophilic and psychrophilic trypsin isoenzymes: Qualitative evaluation of electrostatic differences at the substrate binding site
    • Gorfe A. A., Brandsdal B. O., Leiros H. K., Helland R. and Smalas A. O. (2000) Electrostatics of mesophilic and psychrophilic trypsin isoenzymes: qualitative evaluation of electrostatic differences at the substrate binding site. Proteins 40: 207-217
    • (2000) Proteins , vol.40 , pp. 207-217
    • Gorfe, A.A.1    Brandsdal, B.O.2    Leiros, H.K.3    Helland, R.4    Smalas, A.O.5
  • 68
    • 0035875953 scopus 로고    scopus 로고
    • Electrostatic effects play a central role in cold adaptation of trypsin
    • Brandsdal B. O., Smalas A. O. and Aqvist J. (2001) Electrostatic effects play a central role in cold adaptation of trypsin. FEBS Lett. 499: 171-175
    • (2001) FEBS Lett. , vol.499 , pp. 171-175
    • Brandsdal, B.O.1    Smalas, A.O.2    Aqvist, J.3
  • 69
    • 0033528657 scopus 로고    scopus 로고
    • Thermodynamic stability of a cold-active α-amylase from the Antarctic bacterium Alteromonas haloplanctis
    • Feller G., d'Amico D. and Gerday C. (1999) Thermodynamic stability of a cold-active α-amylase from the Antarctic bacterium Alteromonas haloplanctis. Biochemistry 38: 4613-4619
    • (1999) Biochemistry , vol.38 , pp. 4613-4619
    • Feller, G.1    D'Amico, D.2    Gerday, C.3
  • 70
    • 13244249836 scopus 로고
    • The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
    • Yip K. S., Stillman T. J., Britton K. L., Artymiuk P. J., Baker P. J., Sedelnikova S. E. et al. (1995) The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure 3: 1147-1158
    • (1995) Structure , vol.3 , pp. 1147-1158
    • Yip, K.S.1    Stillman, T.J.2    Britton, K.L.3    Artymiuk, P.J.4    Baker, P.J.5    Sedelnikova, S.E.6
  • 72
    • 0031554925 scopus 로고    scopus 로고
    • Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: Resilience as a key factor in thermostability
    • Aguilar C. F., Sanderson I., Moracci M., Ciaramella M., Nucci R., Rossi M. et al. (1997) Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability. J. Mol. Biol. 271: 789-802
    • (1997) J. Mol. Biol. , vol.271 , pp. 789-802
    • Aguilar, C.F.1    Sanderson, I.2    Moracci, M.3    Ciaramella, M.4    Nucci, R.5    Rossi, M.6
  • 73
    • 0032530086 scopus 로고    scopus 로고
    • Hot spots in cold adaptation: Localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes
    • Fields P. A. and Somero G. N. (1998) Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes. Proc. Natl. Acad. Sci. USA 95: 11476-11481
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11476-11481
    • Fields, P.A.1    Somero, G.N.2
  • 74
    • 0028289989 scopus 로고
    • Stability and structural analysis of α-amylase from the Antarctic psychrophile Alteromonas haloplanctis A23
    • Feller G., Payan F., Theys F., Qian M., Haser R. and Gerday C. (1994) Stability and structural analysis of α-amylase from the Antarctic psychrophile Alteromonas haloplanctis A23. Eur. J. Biochem. 222: 441-447
    • (1994) Eur. J. Biochem. , vol.222 , pp. 441-447
    • Feller, G.1    Payan, F.2    Theys, F.3    Qian, M.4    Haser, R.5    Gerday, C.6
  • 75
    • 0035816221 scopus 로고    scopus 로고
    • Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic Antarctic bacterium
    • Lonhienne T., Zoidakis J., Vorgias C. E., Feller G., Gerday C. and Bouriotis V. (2001) Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic Antarctic bacterium. J. Mol. Biol. 310: 291-297
    • (2001) J. Mol. Biol. , vol.310 , pp. 291-297
    • Lonhienne, T.1    Zoidakis, J.2    Vorgias, C.E.3    Feller, G.4    Gerday, C.5    Bouriotis, V.6
  • 76
    • 0035183584 scopus 로고    scopus 로고
    • Cold-active citrate synthase: Mutagenesis of active-site residues
    • Gerike U., Danson M. J. and Hough D. W. (2001) Cold-active citrate synthase: mutagenesis of active-site residues. Protein Eng. 14: 655-661
    • (2001) Protein Eng. , vol.14 , pp. 655-661
    • Gerike, U.1    Danson, M.J.2    Hough, D.W.3
  • 79
    • 0035712765 scopus 로고    scopus 로고
    • Heat labile ribonuclease HI from a psychrotrophic bacterium: Gene cloning, characterization and site-directed mutagenesis
    • Ohtani N., Haruki M., Morikawa M. and Kanaya S. (2001) Heat labile ribonuclease HI from a psychrotrophic bacterium: gene cloning, characterization and site-directed mutagenesis. Protein Eng. 14: 975-982
    • (2001) Protein Eng. , vol.14 , pp. 975-982
    • Ohtani, N.1    Haruki, M.2    Morikawa, M.3    Kanaya, S.4
  • 80
    • 0034736288 scopus 로고    scopus 로고
    • L-Glutamate dehydrogenase from the Antarctic fish Chaenocephalus aceratus: Primary structure, function and thermodynamic characterisation - Relationship with cold adaptation
    • Ciardiello M. A., Camardella L., Carratore V. and Prisco G. di (2000) L-Glutamate dehydrogenase from the Antarctic fish Chaenocephalus aceratus: primary structure, function and thermodynamic characterisation: relationship with cold adaptation. Biochim. Biophys. Acta 1543: 11-23
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 11-23
    • Ciardiello, M.A.1    Camardella, L.2    Carratore, V.3    Di Prisco, G.4
  • 81
    • 0034825983 scopus 로고    scopus 로고
    • Intrinsic versus extrinsic stabilization of enzymes: The interaction of solutes and temperature on A4-lactate dehydrogenase orthologs from warm-adapted and cold-adapted marine fishes
    • Fields P. A., Wahlstrand B. D. and Somero G. N. (2001) Intrinsic versus extrinsic stabilization of enzymes: the interaction of solutes and temperature on A4-lactate dehydrogenase orthologs from warm-adapted and cold-adapted marine fishes. Eur. J. Biochem. 268: 4497-4505
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4497-4505
    • Fields, P.A.1    Wahlstrand, B.D.2    Somero, G.N.3
  • 82
    • 0032524655 scopus 로고    scopus 로고
    • Characterization of the C-terminal propeptide involved in bacterial wall spanning of alpha-amylase from the psychrophile Alteromonas haloplanctis
    • Feller G., D'Amico S., Benotmane A. M., Joly F., Van Beeumen J. and Gerday C. (1998) Characterization of the C-terminal propeptide involved in bacterial wall spanning of alpha-amylase from the psychrophile Alteromonas haloplanctis. J. Biol. Chem. 273: 12109-12115
    • (1998) J. Biol. Chem. , vol.273 , pp. 12109-12115
    • Feller, G.1    D'Amico, S.2    Benotmane, A.M.3    Joly, F.4    Van Beeumen, J.5    Gerday, C.6
  • 83
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov P. L. (1979) Stability of proteins: small globular proteins. Adv. Protein Chem. 33: 167-241
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 84
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel W. J. and Schellman J. A. (1987) Protein stability curves. Biopolymers 26: 1859-1877
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 86
    • 0033908030 scopus 로고    scopus 로고
    • Designed evolution of enzymatic properties
    • Petrounia I. P. and Arnold F. H. (2000) Designed evolution of enzymatic properties. Curr. Opin. Biotechnol. 11: 325-330
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 325-330
    • Petrounia, I.P.1    Arnold, F.H.2
  • 87
    • 0033928844 scopus 로고    scopus 로고
    • Directed evolution: The 'rational' basis for 'irrational' design
    • Tobin M. B., Gustafsson C. and Huisman G. W. (2000) Directed evolution: the 'rational' basis for 'irrational' design. Curr. Opin. Struct. Biol. 10: 421-427
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 421-427
    • Tobin, M.B.1    Gustafsson, C.2    Huisman, G.W.3
  • 90
    • 0029912086 scopus 로고    scopus 로고
    • Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimen
    • Sterner R., Kleemann G. R., Szadkowski H., Lustig A., Hennig M. and Kirschner K. (1996) Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimen. Protein Sci. 5: 2000-2008
    • (1996) Protein Sci. , vol.5 , pp. 2000-2008
    • Sterner, R.1    Kleemann, G.R.2    Szadkowski, H.3    Lustig, A.4    Hennig, M.5    Kirschner, K.6
  • 91
    • 0031938211 scopus 로고    scopus 로고
    • Engineering of a cold-adapted protease by sequential random mutagenesis and a screening system
    • Taguchi S., Ozaki A. and Momose H. (1998) Engineering of a cold-adapted protease by sequential random mutagenesis and a screening system. Appl. Environ. Microbiol. 64: 492-495
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 492-495
    • Taguchi, S.1    Ozaki, A.2    Momose, H.3
  • 92
    • 0034603740 scopus 로고    scopus 로고
    • Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus beta-glucosidase CelB by directed evolution
    • Lebbink J. H., Kaper T., Bron P., Oost J. van der and Vos W. M. de (2000) Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus beta-glucosidase CelB by directed evolution. Biochemistry 39: 3656-3665
    • (2000) Biochemistry , vol.39 , pp. 3656-3665
    • Lebbink, J.H.1    Kaper, T.2    Bron, P.3    Van Der Oost, J.4    De Vos, W.M.5
  • 94
    • 0035155348 scopus 로고    scopus 로고
    • Experimental evolution of enzyme temperature activity profile: Selection in vivo and characterization of low-temperature-adapted mutants of Pyrococcus furiosus ornithine carbamoyltransferase
    • Roovers M., Sanchez R., Legrain C. and Glansdorff N. (2001) Experimental evolution of enzyme temperature activity profile: selection in vivo and characterization of low-temperature-adapted mutants of Pyrococcus furiosus ornithine carbamoyltransferase. J. Bacteriol. 183: 1101-1105
    • (2001) J. Bacteriol. , vol.183 , pp. 1101-1105
    • Roovers, M.1    Sanchez, R.2    Legrain, C.3    Glansdorff, N.4
  • 95
    • 0035053960 scopus 로고    scopus 로고
    • Cold adaptation of the thermophilic enzyme 3-isopropylmalate dehydrogenase
    • Yasugi M., Amino M., Suzuki T., Oshima T and Yamagishi A. (2001) Cold adaptation of the thermophilic enzyme 3-isopropylmalate dehydrogenase. J. Biochem. (Tokyo) 129: 477-484
    • (2001) J. Biochem. (Tokyo) , vol.129 , pp. 477-484
    • Yasugi, M.1    Amino, M.2    Suzuki, T.3    Oshima, T.4    Yamagishi, A.5
  • 96
    • 0036150978 scopus 로고    scopus 로고
    • Cold adaptation of xylose isomerase from Thermus thermophilus through random PCR mutagenesis: Gene cloning and protein characterization
    • Lonn A., Gardonyi M., Zyl W. van, Hahn-Hagerdal B. and Otero R. C. (2002) Cold adaptation of xylose isomerase from Thermus thermophilus through random PCR mutagenesis: gene cloning and protein characterization. Eur. J. Biochem. 269: 157-163
    • (2002) Eur. J. Biochem. , vol.269 , pp. 157-163
    • Lonn, A.1    Gardonyi, M.2    Van Zyl, W.3    Hahn-Hagerdal, B.4    Otero, R.C.5
  • 97
    • 0033519723 scopus 로고    scopus 로고
    • Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase
    • Kohen A., Cannio R., Bartolucci S. and Klinman J. P. (1999) Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase. Nature 399: 496-499
    • (1999) Nature , vol.399 , pp. 496-499
    • Kohen, A.1    Cannio, R.2    Bartolucci, S.3    Klinman, J.P.4
  • 98
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodszky P., Kardos J., Svingor and Petsko G. A. (1998) Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc. Natl. Acad. Sci. USA 95: 7406-7411
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor3    Petsko, G.A.4
  • 99
    • 0025182490 scopus 로고
    • Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima
    • Wrba A., Schweiger A., Schultes V., Jaenicke R. and Zavodsky P. (1990) Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima. Biochemistry 29: 7584-7592
    • (1990) Biochemistry , vol.29 , pp. 7584-7592
    • Wrba, A.1    Schweiger, A.2    Schultes, V.3    Jaenicke, R.4    Zavodsky, P.5
  • 100
    • 0035958914 scopus 로고    scopus 로고
    • A better enzyme to cope with cold: Comparative flexibility studies on psychrotrophic, mesophilic, and thermophilic IPMDHs
    • Svingor A., Kardos J., Hajdu I., Nemeth A. and Zavodszky P. (2001) A better enzyme to cope with cold: comparative flexibility studies on psychrotrophic, mesophilic, and thermophilic IPMDHs. J. Biol. Chem. 276: 28121-28125
    • (2001) J. Biol. Chem. , vol.276 , pp. 28121-28125
    • Svingor, A.1    Kardos, J.2    Hajdu, I.3    Nemeth, A.4    Zavodszky, P.5
  • 101
    • 0034724271 scopus 로고    scopus 로고
    • Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity?
    • Jaenicke R. (2000) Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity? Proc. Natl. Acad. Sci. USA 97: 2962-2964
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2962-2964
    • Jaenicke, R.1
  • 102
    • 0034724392 scopus 로고    scopus 로고
    • Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature
    • Hernandez G., Jenney F. E. Jr, Adams M. W. and LeMaster D. M. (2000) Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature. Proc. Natl. Acad. Sci. USA 97: 3166-3170
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3166-3170
    • Hernandez, G.1    Jenney F.E., Jr.2    Adams, M.W.3    LeMaster, D.M.4


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