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Volumn 53, Issue 10, 1997, Pages 830-841

Psychrophilic enzymes: Molecular basis of cold adaptation

Author keywords

Antarctic; Cold adaptation; Extremophiles; Microbial proteins; Protein stability; Psychrophiles; Weak interactions

Indexed keywords

AMINO TERMINAL SEQUENCE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELL GROWTH; CHEMICAL REACTION; CHEMICAL REACTION KINETICS; COLD ACCLIMATIZATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; NONHUMAN; POINT MUTATION; PROTEIN STABILITY; PSYCHROPHILE; REVIEW; TEMPERATURE SENSITIVITY; THERMODYNAMICS; THERMOSTABILITY;

EID: 0030681366     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050103     Document Type: Review
Times cited : (363)

References (76)
  • 1
    • 0024616108 scopus 로고
    • Inhibition of growth of non-basal planes in ice by fish antifreezes
    • Raymond J. A., Wilson P. and DeVries A. I., (1989) Inhibition of growth of non-basal planes in ice by fish antifreezes. Proc. Natl Acad. Sci. USA 86: 881-885
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 881-885
    • Raymond, J.A.1    Wilson, P.2    Devries, A.I.3
  • 2
    • 0029856558 scopus 로고    scopus 로고
    • Structural basis for the binding of a globulat antifreeze protein to ice
    • Jia Z., DeLuca C. I. Chao II. and Davies P. L. (1996) Structural basis for the binding of a globulat antifreeze protein to ice. Nature 384: 285-288
    • (1996) Nature , vol.384 , pp. 285-288
    • Jia, Z.1    DeLuca, C.I.2    Chao, I.I.3    Davies, P.L.4
  • 3
    • 0000078585 scopus 로고
    • Thermal hysteresis protein activity in bacteria, fungi and phylogenetically diverse plants
    • Duman J. G. and Olsen T. M. (1993) Thermal hysteresis protein activity in bacteria, fungi and phylogenetically diverse plants. Cryobiology 30: 322-328
    • (1993) Cryobiology , vol.30 , pp. 322-328
    • Duman, J.G.1    Olsen, T.M.2
  • 4
    • 0028807747 scopus 로고
    • Low temperature growth, freezing survival and production of antifreeze protein by the plant growth promoting rhizobacterium Pseudomous putida GR 12-2
    • Sun X., Griffith M., Pasternak J. J. and Glick B. (1995) Low temperature growth, freezing survival and production of antifreeze protein by the plant growth promoting rhizobacterium Pseudomous putida GR 12-2. Can, J. Microbiol. 41: 776-784
    • (1995) Can, J. Microbiol. , vol.41 , pp. 776-784
    • Sun, X.1    Griffith, M.2    Pasternak, J.J.3    Glick, B.4
  • 8
    • 0001734325 scopus 로고
    • Physiology and molecular biology of psychrophilic microorganisms
    • Herbert R. A. and Sharp R. J. (eds). Blackie, London
    • Russell N. J. (1992) Physiology and molecular biology of psychrophilic microorganisms. In: Molecular Biology and Biotechnology of Extremophiles. Herbert R. A. and Sharp R. J. (eds). pp. 203-224. Blackie, London
    • (1992) Molecular Biology and Biotechnology of Extremophiles , pp. 203-224
    • Russell, N.J.1
  • 9
    • 0038279773 scopus 로고
    • Endolithic microorganisms in the antaretic cold desert
    • Friedmann E.H. (1982) Endolithic microorganisms in the antaretic cold desert. Science 215: 1045-1053
    • (1982) Science , vol.215 , pp. 1045-1053
    • Friedmann, E.H.1
  • 10
    • 0016189989 scopus 로고
    • Molecular mechanisms of temperature compensation in poikilotherms
    • Hazel J. R. and Prosser C. L. (1974) Molecular mechanisms of temperature compensation in poikilotherms. Biol. Rev. 54: 620-677
    • (1974) Biol. Rev. , vol.54 , pp. 620-677
    • Hazel, J.R.1    Prosser, C.L.2
  • 12
    • 0023841438 scopus 로고
    • Freeze tolerance in animals
    • Storey K. B. and Storey J. M. (1988) Freeze tolerance in animals. Physiol. Rev. 68: 27-84
    • (1988) Physiol. Rev. , vol.68 , pp. 27-84
    • Storey, K.B.1    Storey, J.M.2
  • 14
    • 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
  • 15
    • 0028363836 scopus 로고
    • The cold shock response-a hot topic
    • Jones P. G. and Inouye M. (1994) The cold shock response-a hot topic, Mol. Microbiol. 11: 811-818
    • (1994) Mol. Microbiol. , vol.11 , pp. 811-818
    • Jones, P.G.1    Inouye, M.2
  • 16
    • 0028047396 scopus 로고
    • Occurence and expression of CspA. a cold shock gene in antaretic psydirotrophic bacteria
    • Ray M. K., Sitaramamma T., Ghandi S. and Shivagi S. (1994) Occurence and expression of CspA. a cold shock gene in antaretic psydirotrophic bacteria. FEMS Microbiol, Lett. 116: 55-60
    • (1994) FEMS Microbiol, Lett. , vol.116 , pp. 55-60
    • Ray, M.K.1    Sitaramamma, T.2    Ghandi, S.3    Shivagi, S.4
  • 17
    • 0028198927 scopus 로고
    • Effect of growth temperatures on the protein levels in a psychrotrophic bacterium Pseudomonas fragi
    • Hebrand M., Dubois E., Polier P. and Labadie J. (1994) Effect of growth temperatures on the protein levels in a psychrotrophic bacterium Pseudomonas fragi. J. Bacteriol, 176: 4017-4024
    • (1994) J. Bacteriol , vol.176 , pp. 4017-4024
    • Hebrand, M.1    Dubois, E.2    Polier, P.3    Labadie, J.4
  • 18
    • 0029880419 scopus 로고    scopus 로고
    • Identification and purification of a family of dimeric major cold shock protein homologs from the psychrotrophic Bacillus cereus WSB 10201
    • Mayr B., Kaplan T., Lechner S. And Scherer S. (1996) Identification and purification of a family of dimeric major cold shock protein homologs from the psychrotrophic Bacillus cereus WSB 10201. J. Bacteriol, 178: 2916-2925
    • (1996) J. Bacteriol , vol.178 , pp. 2916-2925
    • Mayr, B.1    Kaplan, T.2    Scherer S, L.S.3
  • 19
    • 0030023653 scopus 로고    scopus 로고
    • Cold shock and cold acelimation proteins in the psychrotrophic bacterium Anhrobactes blobiformis 8155
    • Berger F., Morellet N., Menu F. and Potier P. (1996) Cold shock and cold acelimation proteins in the psychrotrophic bacterium Anhrobactes blobiformis 8155. J. Bacteriol. 178: 2999-3007
    • (1996) J. Bacteriol. , vol.178 , pp. 2999-3007
    • Berger, F.1    Morellet, N.2    Menu, F.3    Potier, P.4
  • 20
    • 0029936488 scopus 로고    scopus 로고
    • Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate structure dehydrogenase at 2.5 Å resolution
    • Tanner J. J., Hecht R. M. and Krause K. L. (1996) Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate structure dehydrogenase at 2.5 Å resolution. Biochemistry 35: 2597-2609
    • (1996) Biochemistry , vol.35 , pp. 2597-2609
    • Tanner, J.J.1    Hecht, R.M.2    Krause, K.L.3
  • 21
    • 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
  • 22
    • 0002577666 scopus 로고
    • Optimum temperatures and temperature ranges for growth of snow algae
    • Hohman R. W. (1975) Optimum temperatures and temperature ranges for growth of snow algae. Aretic Alpine Res. 7: 13-24
    • (1975) Aretic Alpine Res. , vol.7 , pp. 13-24
    • Hohman, R.W.1
  • 23
    • 0029739286 scopus 로고    scopus 로고
    • Effect of temperature on two enzymes from a psychrophilic Chloromonas (Chlorophyta)
    • Loppes R., Devos N., Willem S., Barthélemy P. and Matagne R. F. (1996) Effect of temperature on two enzymes from a psychrophilic Chloromonas (Chlorophyta). J. Physcol. 32: 276-278
    • (1996) J. Physcol. , vol.32 , pp. 276-278
    • Loppes, R.1    Devos, N.2    Willem, S.3    Barthélemy, P.4    Matagne, R.F.5
  • 26
  • 27
    • 0001789740 scopus 로고
    • Substrate dependent cold adaptations in some deep-sea sediment bacteria
    • Ruger H. J. (1988) Substrate dependent cold adaptations in some deep-sea sediment bacteria, System, Appl, Microbiol. 11: 90-93
    • (1988) System, Appl, Microbiol. , vol.11 , pp. 90-93
    • Ruger, H.J.1
  • 28
    • 0026615439 scopus 로고
    • Bacterial growth in the cold: Evidence for an enhanced substrate requirement
    • Wiebe W. J., Sheldon W. M. and Pomeroy L., R. (1992) Bacterial growth in the cold: evidence for an enhanced substrate requirement. Appl. Environ. Microbiol. 58: 359-364
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 359-364
    • Wiebe, W.J.1    Sheldon, W.M.2    Pomeroy, L.R.3
  • 29
    • 0028151519 scopus 로고
    • Growth temperature regulates the induction of β-lactamase in Psculomonas flaorescens through modification of the outer membrane permeation of a β-lactam inducing antibiotic
    • Orange N. (1994) Growth temperature regulates the induction of β-lactamase in Psculomonas flaorescens through modification of the outer membrane permeation of a β-lactam inducing antibiotic, Microbiology 140: 3125-3130
    • (1994) Microbiology , vol.140 , pp. 3125-3130
    • Orange, N.1
  • 30
    • 0028998469 scopus 로고
    • Growth temperature in involved in the regulation of extracellular lipase at two different levels in Pseudomonas fluorescens strain MF0
    • Guillou C., Merieau A., Trebert B. and Guespin-Michel J. F. (1995) Growth temperature in involved in the regulation of extracellular lipase at two different levels in Pseudomonas fluorescens strain MF0, Biotechnol. Lett. 17: 377-382
    • (1995) Biotechnol. Lett. , vol.17 , pp. 377-382
    • Guillou, C.1    Merieau, A.2    Trebert, B.3    Guespin-Michel, J.F.4
  • 31
    • 0029786675 scopus 로고
    • Evidence for two domains of temperature for the psychrotrophic bacterium Pseudomonas fluorescens MF0
    • Guillou C. And Guespin-Michel J. F. (1995) Evidence for two domains of temperature for the psychrotrophic bacterium Pseudomonas fluorescens MF0. App. Environ. Microbiol. 62: 3319-3324
    • (1995) App. Environ. Microbiol. , vol.62 , pp. 3319-3324
    • Guillou, C.1    Guespin-Michel, J.F.2
  • 32
    • 0040606207 scopus 로고    scopus 로고
    • Growth temperature dependence of channel size of the major outer membrane protein (Oprf) in psychrotrophic Pseudomanas fluorescens strains
    • De E., Orange N., Saint N., Guerillon J., De Mot R. and Molle G. (1997) Growth temperature dependence of channel size of the major outer membrane protein (Oprf) in psychrotrophic Pseudomanas fluorescens strains. Microbiology 143: 1029-1035
    • (1997) Microbiology , vol.143 , pp. 1029-1035
    • De, E.1    Orange, N.2    Saint, N.3    Guerillon, J.4    De Mot, R.5    Molle, G.6
  • 33
    • 0029912086 scopus 로고    scopus 로고
    • Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer
    • 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 homodimer. 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
  • 34
    • 0015578550 scopus 로고
    • Temperature adaptations of enzymes: Roles of the free energy, the enthalpy and the entropy of activation
    • Low P. S., Bada J. L. and Somero G. N. (1973) Temperature adaptations of enzymes: roles of the free energy, the enthalpy and the entropy of activation. Proc. Natl Acad, Sci. USA 70: 430-432
    • (1973) Proc. Natl Acad, Sci. USA , vol.70 , pp. 430-432
    • Low, P.S.1    Bada, J.L.2    Somero, G.N.3
  • 35
    • 0019000671 scopus 로고
    • The causes of sharply bent or discontinuous Arrhenius plots for enzyme-catalysed reactions
    • Londesborough J. (1980) The causes of sharply bent or discontinuous Arrhenius plots for enzyme-catalysed reactions. Eur. J. Biochem, 105: 211-215
    • (1980) Eur. J. Biochem , vol.105 , pp. 211-215
    • Londesborough, J.1
  • 36
    • 0000773373 scopus 로고
    • Life in cold water: The physiological ecology of polar marine ectotherms
    • Clarke A. (1983) Life in cold water: the physiological ecology of polar marine ectotherms. Oceanogr. Mar, Biol. Annu. Rev. 21: 341-453
    • (1983) Oceanogr. Mar, Biol. Annu. Rev. , vol.21 , pp. 341-453
    • Clarke, A.1
  • 37
    • 0019273357 scopus 로고
    • Temperature characteristics and Arrhenius plots for nominal psychrophiles, mesophiles and thermophiles
    • Mohr P. W. and Krawiec S. (1980) Temperature characteristics and Arrhenius plots for nominal psychrophiles, mesophiles and thermophiles. J. Gen. Microbiol. 121: 311-317
    • (1980) J. Gen. Microbiol. , vol.121 , pp. 311-317
    • Mohr, P.W.1    Krawiec, S.2
  • 38
    • 0024389204 scopus 로고
    • Molecular basis of evolutionary adaptation at the lactate dehydrogenasc-B locus in the fish Fundulus heteroclitus
    • Crawford D. L. and Powers D. A. (1989) Molecular basis of evolutionary adaptation at the lactate dehydrogenasc-B locus in the fish Fundulus heteroclitus. Proc. Natl Acad. Sci. USA 86: 9365-9369
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 9365-9369
    • Crawford, D.L.1    Powers, D.A.2
  • 39
    • 0026760697 scopus 로고
    • Evolutionary adaptation to different thermal environments via transcriptional regulation
    • Crawford D. L. and Powers D. A. (1992) Evolutionary adaptation to different thermal environments via transcriptional regulation. Mol. Biol. Evol. 9: 806-813
    • (1992) Mol. Biol. Evol. , vol.9 , pp. 806-813
    • Crawford, D.L.1    Powers, D.A.2
  • 40
    • 0000618105 scopus 로고
    • Trypsin from antaretic fish (Paranotothenia magellanoica Forster) as compared with trout (Salmo gairdneri) trypsin
    • Genicot S., Feller G. and Gerday C. (1988) Trypsin from antaretic fish (Paranotothenia magellanoica Forster) as compared with trout (Salmo gairdneri) trypsin. Comp. Biochem. Physiol. 90B: 601-609
    • (1988) Comp. Biochem. Physiol. , vol.90 B , pp. 601-609
    • Genicot, S.1    Feller, G.2    Gerday, C.3
  • 41
    • 0021707123 scopus 로고
    • Purification and characterization of trypsin from the Greenland cod (Gadusogac). 1. Kinetic and thermodynamic characteristics
    • Simpson B. K. and Haard N. F. (1984) Purification and characterization of trypsin from the Greenland cod (Gadusogac). 1. Kinetic and thermodynamic characteristics. Can. J. Biochem. Cell. Biol. 62: 894-900
    • (1984) Can. J. Biochem. Cell. Biol. , vol.62 , pp. 894-900
    • Simpson, B.K.1    Haard, N.F.2
  • 42
    • 0027194992 scopus 로고
    • Properties of elastase from Atlantic cod. a cold-adapted proteinase
    • Asgeirsson B. and Bjarnason J. B. (1993) Properties of elastase from Atlantic cod. a cold-adapted proteinase. Biochim. Biophys. Acta 1164: 91-100
    • (1993) Biochim. Biophys. Acta , vol.1164 , pp. 91-100
    • Asgeirsson, B.1    Bjarnason, J.B.2
  • 43
    • 0025761645 scopus 로고
    • Structural and kinetic properties of chymotrypsin from atlantic cod (Gadusmorhua). Comparison with bovine chymotrypsin
    • Asgeirsson B. and Bjarnason J. B. (1991) Structural and kinetic properties of chymotrypsin from atlantic cod (Gadusmorhua). Comparison with bovine chymotrypsin. Comp. Biochem. Physiol. 99B: 327-335
    • (1991) Comp. Biochem. Physiol. , vol.99 B , pp. 327-335
    • Asgeirsson, B.1    Bjarnason, J.B.2
  • 44
    • 0026673888 scopus 로고
    • Purification, characterization, and nucleotide sequence of the thermolabile a-amylase from the antarctic psychrotroph. Alteromonas haloplanetis A23
    • Feller G., Lonhienne T., Deroanne C., Libioulle C., Van Becumen J. and Gerday C. (1992) Purification, characterization, and nucleotide sequence of the thermolabile a-amylase from the antarctic psychrotroph. Alteromonas haloplanetis A23. J. Biol. Chem. 267: 5217-5221
    • (1992) J. Biol. Chem. , vol.267 , pp. 5217-5221
    • Feller, G.1    Lonhienne, T.2    Deroanne, C.3    Libioulle, C.4    Van Becumen, J.5    Gerday, C.6
  • 45
    • 0028289989 scopus 로고
    • Stability and structural analysis of a-amylase from the antaretic psychrophile Alteromonas haloplanctis A23
    • Feller G., Payan F., Theys F., Qian M., Haser R. and Gerday C. (1994) Stability and structural analysis of a-amylase from the antaretic 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
  • 47
    • 0024388720 scopus 로고
    • Evolutionary optimization of the catalytic effectiveness of an enzyme
    • Burbaum J. J., Raines R. T., Albery W. J. and Knowles J. R. (1989) Evolutionary optimization of the catalytic effectiveness of an enzyme. Biochemistry 28: 9293-9305
    • (1989) Biochemistry , vol.28 , pp. 9293-9305
    • Burbaum, J.J.1    Raines, R.T.2    Albery, W.J.3    Knowles, J.R.4
  • 48
    • 0031052268 scopus 로고    scopus 로고
    • Enzymes from cold-adapted microorganisms. the class C β-lactamase from the antarctic psychrophile Psychrobacter immobilis A5
    • Feller G., Zekhnini Z., Lamotte-Brasseur J. and Gerday C. (1997) Enzymes from cold-adapted microorganisms. The class C β-lactamase from the antarctic psychrophile Psychrobacter immobilis A5. Fur. J. Biochem. 244: 186-191
    • (1997) Fur. J. Biochem. , vol.244 , pp. 186-191
    • Feller, G.1    Zekhnini, Z.2    Lamotte-Brasseur, J.3    Gerday, C.4
  • 49
    • 0019164846 scopus 로고
    • β-lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitin
    • Fisher J., Belasco J. G., Khosla S. and Knowles J. R. (1980) β-lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitin. Biochemistry 19: 2895-2901
    • (1980) Biochemistry , vol.19 , pp. 2895-2901
    • Fisher, J.1    Belasco, J.G.2    Khosla, S.3    Knowles, J.R.4
  • 50
    • 0029962635 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of α-amylase from the antarctic psychrophile Alteromonas haloplanetis A23
    • Aghajari N., Feller G., Gerday C. and Haser R. (1996) Crystallization and preliminary X-ray diffraction studies of α-amylase from the antarctic psychrophile Alteromonas haloplanetis A23. Protein Sci. 5: 2128-2129
    • (1996) Protein Sci. , vol.5 , pp. 2128-2129
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 52
    • 0029187318 scopus 로고
    • Structure of native pancreatic elastase from North Atlantic salmon at 1.61 A resolution
    • Berglund G. L., Willassen N. P., Hordvik A. and Smalas A. O. (1995) Structure of native pancreatic elastase from North Atlantic salmon at 1.61 A resolution. Acta Cryst. D51: 925-937
    • (1995) Acta Cryst. , vol.D51 , pp. 925-937
    • Berglund, G.L.1    Willassen, N.P.2    Hordvik, A.3    Smalas, A.O.4
  • 53
    • 0028864205 scopus 로고
    • A critical assessment of comparative molecular modeling of tertiary structures of proteins
    • Mosimann S., Meleshko R. and James M. N. G. (1995) A critical assessment of comparative molecular modeling of tertiary structures of proteins. Proteins Stuct. Fund. Genet. 23: 301-317
    • (1995) Proteins Stuct. Fund. Genet. , vol.23 , pp. 301-317
    • Mosimann, S.1    Meleshko, R.2    James, M.N.G.3
  • 54
    • 0028991962 scopus 로고
    • Modelling mutations and homologous proteins
    • Sali A. (1995) Modelling mutations and homologous proteins. Curr. Opin. Biotechnol. 6: 437-451
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 437-451
    • Sali, A.1
  • 55
    • 0028198814 scopus 로고
    • The active center of a mammalian a-amylase with a carbohydrate inhibitor refined to 2.2 Å resolution
    • Qian M., Haser R., Buisson G., Duée E. and Payan F. (1994) The active center of a mammalian a-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    Duée, E.4    Payan, F.5
  • 56
    • 0021715356 scopus 로고
    • Heat-labile alkaline phosphalase from antarctic bacteria: Rapid 5′ endlabelling of nucleic acids
    • Kobori H., Sullivan C. W. and Shizuya H. (1984) Heat-labile alkaline phosphalase from antarctic bacteria: rapid 5′ endlabelling of nucleic acids. Proc. Natl Acad. Sci. USA 81: 6691-6695
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 6691-6695
    • Kobori, H.1    Sullivan, C.W.2    Shizuya, H.3
  • 57
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2
    • Perutz M. F. and Raidt H. (1975) Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2. Nature 255: 256-259
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, M.F.1    Raidt, H.2
  • 58
    • 0029042854 scopus 로고
    • Comparative molecular dynamics simulation studies of salmon and bovine trypsins in aqueous solution
    • Heimstad E. S., Hansen L. K. and Smalas A. O. (1995) Comparative molecular dynamics simulation studies of salmon and bovine trypsins in aqueous solution. Protein Eng. 8: 379-388
    • (1995) Protein Eng. , vol.8 , pp. 379-388
    • Heimstad, E.S.1    Hansen, L.K.2    Smalas, A.O.3
  • 59
    • 0028292010 scopus 로고
    • Cold adaptation of proteins. Purification, characterization and sequence of the heat-labile ubtilisin from the antaretic 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 ubtilisin from the antaretic 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
  • 60
    • 0027397742 scopus 로고
    • Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria
    • 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. 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
  • 61
    • 0342981073 scopus 로고    scopus 로고
    • Molecular adaptation to cold of an antaretic bacterial lipase
    • Arpigny J. L., Lamotte J. and Gerday C. (1997) Molecular adaptation to cold of an antaretic bacterial lipase. J. Mol. Catal. B(3): 29-35
    • (1997) J. Mol. Catal. B , Issue.3 , pp. 29-35
    • Arpigny, J.L.1    Lamotte, J.2    Gerday, C.3
  • 63
    • 0030924747 scopus 로고    scopus 로고
    • Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from antaretic fish Notothenia neglecta
    • Aittaleb M., Hubner R., Lamotte-Brasseur J. and Gerday C. (1997) Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from antaretic fish Notothenia neglecta. Protein Eng. 10: 475-477
    • (1997) Protein Eng. , vol.10 , pp. 475-477
    • Aittaleb, M.1    Hubner, R.2    Lamotte-Brasseur, J.3    Gerday, C.4
  • 65
    • 0031279830 scopus 로고    scopus 로고
    • Molecular adaptations of enzymes from psychrophilic organisms
    • in press
    • Feller G., Arpigny J. L., Narinx. E. and Gerday C. (1997) Molecular adaptations of enzymes from psychrophilic organisms. Comp. Biochem. Physiol. 118A: (in press)
    • (1997) Comp. Biochem. Physiol. , vol.118 A
    • Feller, G.1    Arpigny, J.L.2    Narinx, E.3    Gerday, C.4
  • 66
    • 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. P., 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.P.1    Stillman, T.J.2    Britton, K.L.3    Artymiuk, P.J.4    Baker, P.J.5    Sedelnikova, S.E.6
  • 67
    • 0028268676 scopus 로고
    • A structural role for arginine in proteins: Multiple hydrogen bonds to backbone carbonyl oxygens
    • Borders C. L., Broadwater J. A., Bekeny P. A., Salmon J. A., Lee A. S., Eldridge A. M. et al. (1994) A structural role for arginine in proteins: multiple hydrogen bonds to backbone carbonyl oxygens. Protein Sci. 3: 541-548
    • (1994) Protein Sci. , vol.3 , pp. 541-548
    • Borders, C.L.1    Broadwater, J.A.2    Bekeny, P.A.3    Salmon, J.A.4    Lee, A.S.5    Eldridge, A.M.6
  • 68
  • 71
    • 0024260626 scopus 로고
    • Weakly polar interactions in proteins
    • Burley S. K. and Petsko G. A. (1988) Weakly polar interactions in proteins. Adv. Protein Chem. 39: 125-189
    • (1988) Adv. Protein Chem. , vol.39 , pp. 125-189
    • Burley, S.K.1    Petsko, G.A.2
  • 72
    • 0023122030 scopus 로고
    • Tests of the helix dipole model for the stabilisation of x-helices
    • Shoemaker K. R., Kim P. S., York F. J., Stewart J. M. and Baldwin R.L. (1987) Tests of the helix dipole model for the stabilisation of x-helices. Nature 326: 563-567
    • (1987) Nature , vol.326 , pp. 563-567
    • Shoemaker, K.R.1    Kim, P.S.2    York, F.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 73
    • 0030220170 scopus 로고    scopus 로고
    • The role of protein-solvent interactions in protein unfolding
    • Schiffer C. A. and Dötsch V. (1996) The role of protein-solvent interactions in protein unfolding. Curr. Opin. Biotechnol. 7: 428-432
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 428-432
    • Schiffer, C.A.1    Dötsch, V.2
  • 74
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov P. L. and Gill S. J. (1988) Stability of protein structure and hydrophobic interaction. Adv. Protein Chem. 39: 191-234
    • (1988) Adv. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 75
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.