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Volumn 5, Issue 5, 2001, Pages 313-321

Did psychrophilic enzymes really win the challenge?

Author keywords

Biotechnological tools; Cold adaptation; Directed evolution; Enzyme; Flexibility; Microcalorimetry; Psychrophile

Indexed keywords

ENZYME;

EID: 18044401046     PISSN: 14310651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s007920100207     Document Type: Article
Times cited : (59)

References (78)
  • 1
    • 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, Haser R (1998a) 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
  • 2
    • 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, Haser R (1998b) 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
  • 3
    • 0030924747 scopus 로고    scopus 로고
    • Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from Antarctic fish Notothenia neglecta
    • Aittaleb M, Hubner R, Lamotte-Brasseur J, Gerday C (1997) Cold adaptation parameters derived from cDNA sequencing and molecular modelling of elastase from Antarctic 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
  • 4
    • 0031935580 scopus 로고    scopus 로고
    • Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution
    • Akanuma S, Yamagishi A, Tanaka N, Oshima T (1998) Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution. Protein Sci 7:698-705
    • (1998) Protein Sci , vol.7 , pp. 698-705
    • Akanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 5
    • 0033106205 scopus 로고    scopus 로고
    • Further improvement of the thermal stability of a partially stabilized Bacillus subtilis 3-isopropylmalate dehydrogenase variant by random and site-directed mutagenesis
    • Akanuma S, Yamagishi A, Tanaka N, Oshima T (1999) Further improvement of the thermal stability of a partially stabilized Bacillus subtilis 3-isopropylmalate dehydrogenase variant by random and site-directed mutagenesis. Eur J Biochem 260:499-504
    • (1999) Eur J Biochem , vol.260 , pp. 499-504
    • Akanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 8
    • 0342981073 scopus 로고    scopus 로고
    • Molecular adaptation to cold of an Antarctic bacterial lipase
    • Arpigny JL, Lamotte J, Gerday C (1997) Molecular adaptation to cold of an Antarctic bacterial lipase. J Mol Catal B 3:29-35
    • (1997) J Mol Catal B , vol.3 , pp. 29-35
    • Arpigny, J.L.1    Lamotte, J.2    Gerday, C.3
  • 9
    • 0034646605 scopus 로고    scopus 로고
    • Structural kinetic and calorimetric characterization of the cold-active phosphoglycerate kinase from the antarctic Pseudomonassp. TACII18
    • Bentahir M, Feller G, Aittaleb M, Lamotte-Brasseur J, Himri T, Chessa JP, Gerday C (2000) Structural kinetic and calorimetric characterization of the cold-active phosphoglycerate kinase from the antarctic Pseudomonassp. 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    Gerday, C.7
  • 10
    • 0034169822 scopus 로고    scopus 로고
    • Structural analysis of the elongation factor G protein from the low-temperature-adapted bacterium Arthrobacter globiformis SI55
    • Berchet V, Thomas T, Cavicchioli R, Russell NJ, Gounot AM (2000) Structural analysis of the elongation factor G protein from the low-temperature-adapted bacterium Arthrobacter globiformis SI55. Extremophiles 4:123-130
    • (2000) Extremophiles , vol.4 , pp. 123-130
    • Berchet, V.1    Thomas, T.2    Cavicchioli, R.3    Russell, N.J.4    Gounot, A.M.5
  • 11
    • 0029187318 scopus 로고
    • Structure of native pancreatic elastases from North Atlantic salmon at 1.61 Å resolution
    • Berglund GI, Willasen NP, Horvick A, Smalas AO (1995) Structure of native pancreatic elastases from North Atlantic salmon at 1.61 Å resolution. Acta Cryst D51:925-937
    • (1995) Acta Cryst , vol.D51 , pp. 925-937
    • Berglund, G.I.1    Willasen, N.P.2    Horvick, A.3    Smalas, A.O.4
  • 13
    • 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 Ann Rev 21:341-453
    • (1983) Oceanogr Mar Biol Ann Rev , vol.21 , pp. 341-453
    • Clarke, A.1
  • 14
    • 0034713903 scopus 로고    scopus 로고
    • Structural similarities and evolutionary relationships in chloride-dependent alpha-amylases
    • D'Amico S, Gerday C, Feller G (2000) Structural similarities and evolutionary relationships in chloride-dependent alpha-amylases. Gene 253:95-105
    • (2000) Gene , vol.253 , pp. 95-105
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 15
    • 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, 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
  • 16
    • 0025573876 scopus 로고
    • Relationship between viable and direct bacteriological counts in southern polar marine waters
    • Delille D, Bouvy M (1990) Relationship between viable and direct bacteriological counts in southern polar marine waters. Vie Milieu 40:281-284
    • (1990) Vie Milieu , vol.40 , pp. 281-284
    • Delille, D.1    Bouvy, M.2
  • 17
    • 0029902365 scopus 로고    scopus 로고
    • Determinants of polyreactivity in a large panel of recombinant human antibodies from HIV-I infection
    • Ditzel HJ, Itoh K, Burton DA (1996) Determinants of polyreactivity in a large panel of recombinant human antibodies from HIV-I infection. J Immunol 157:739-749
    • (1996) J Immunol , vol.157 , pp. 739-749
    • Ditzel, H.J.1    Itoh, K.2    Burton, D.A.3
  • 18
    • 0030681366 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Molecular basis of cold adaptation
    • Feller G, 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
  • 19
    • 0026673888 scopus 로고
    • Purification characterization and nucleotide sequence of the thermolabile α-amylase from the Antarctic psychrotroph Alteromonas haloplanctis A23
    • Feller G, Lonhienne T, Deroanne C, Libioulle C, Van Beeumen J, Gerday C (1992) Purification characterization and nucleotide sequence of the thermolabile α-amylase from the Antarctic psychrotroph Alteromonas haloplanctis 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 Beeumen, J.5    Gerday, C.6
  • 20
    • 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, 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
  • 21
  • 22
    • 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, Gerday C (1997b) Enzymes from cold-adapted microorganisms. The class C β-lactamase from the Antarctic psychrophile Psychrobacter immobilis A5. Eur J Biochem 244:186-191
    • (1997) Eur J Biochem , vol.244 , pp. 186-191
    • Feller, G.1    Zekhnini, Z.2    Lamotte-Brasseur, J.3    Gerday, C.4
  • 23
    • 0033528657 scopus 로고    scopus 로고
    • Thermodynamic stability of a cold-active α-amylase from the Antarctic bacterium Alteromonas haloplanctis
    • Feller G, d'Amico D, 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
  • 24
    • 0032530086 scopus 로고    scopus 로고
    • Hot spots in cold adaptation: Localized increases in conformational flexibility in lactate dehydrogenase A(4) orthologs of Antarctic notothenioid fishes
    • Fields PA, Somero GN (1998) Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A(4) orthologs of Antarctic notothenioid fishes. Proc Natl Acad Sci U S A 95:11476-11481
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 11476-11481
    • Fields, P.A.1    Somero, G.N.2
  • 25
    • 0033865067 scopus 로고    scopus 로고
    • Structural equilibrium fluctuations in mesophilic and thermophilic α-amylase
    • Fitter J, Heberle J (2000) Structural equilibrium fluctuations in mesophilic and thermophilic α-amylase. Biophys J 79:1629-1636
    • (2000) Biophys J , vol.79 , pp. 1629-1636
    • Fitter, J.1    Heberle, J.2
  • 27
    • 0006263597 scopus 로고
    • Uber einige Eigenschaften leuchtender Bakterien
    • Forster J (1887) Uber einige Eigenschaften leuchtender Bakterien. Zentz Bacteriol Parasitenk Infekt Hyg 2:337-340
    • (1887) Zentz Bacteriol Parasitenk Infekt Hyg , vol.2 , pp. 337-340
    • Forster, J.1
  • 31
    • 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 ZO, Van Petegem F, Chessa JP, Van Beeumen J, Hubscher U, Gerday C (2000b) 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.P.4    Van Beeumen, J.5    Hubscher, U.6    Gerday, C.7
  • 35
    • 0034712678 scopus 로고    scopus 로고
    • Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases
    • Gershenson A, Schauerte JA, Giver L, Arnold FH (2000) Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases. Biochemistry 39:4658-4665
    • (2000) Biochemistry , vol.39 , pp. 4658-4665
    • Gershenson, A.1    Schauerte, J.A.2    Giver, L.3    Arnold, F.H.4
  • 37
    • 0040735677 scopus 로고    scopus 로고
    • Directed evolution of betaglucosidase a from Paenibacillus polymyxa to thermal resistance
    • Gonzalez-Blasco G, Sanz-Aparicio J, Gonzalez B, Hermoso JA, Polaina J (2000) Directed evolution of betaglucosidase A from Paenibacillus polymyxa to thermal resistance. J Biol Chem 275:13708-13712
    • (2000) J Biol Chem , vol.275 , pp. 13708-13712
    • Gonzalez-Blasco, G.1    Sanz-Aparicio, J.2    Gonzalez, B.3    Hermoso, J.A.4    Polaina, J.5
  • 39
    • 0029823884 scopus 로고    scopus 로고
    • Some like it cold: Response of microorganisms to cold shock
    • Graumann P, Marahiel MA (1996) Some like it cold: response of microorganisms to cold shock. Arch Microbiol 166:293-300
    • (1996) Arch Microbiol , vol.166 , pp. 293-300
    • Graumann, P.1    Marahiel, M.A.2
  • 40
    • 0031113943 scopus 로고    scopus 로고
    • An efficient random mutagenesis technique using an E. coli mutator strain
    • Greener A, Callahan M, Jerpseth B (1997) An efficient random mutagenesis technique using an E. coli mutator strain. Mol Biotechnol 7:189-195
    • (1997) Mol Biotechnol , vol.7 , pp. 189-195
    • Greener, A.1    Callahan, M.2    Jerpseth, B.3
  • 41
    • 0034724392 scopus 로고    scopus 로고
    • Millisecond time scale conformational flexibility in a hyper thermophile protein at ambient temperature
    • Hernandez G, Jenney FE, Adams M, Le Master D (2000) Millisecond time scale conformational flexibility in a hyper thermophile protein at ambient temperature. Proc Natl Acad Sci U S A 97:3166-3170
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 3166-3170
    • Hernandez, G.1    Jenney, F.E.2    Adams, M.3    Le Master, D.4
  • 42
    • 0028913567 scopus 로고
    • The effects of hydrophilic to hydrophobic surface mutations on the denatured state of iso-1-cytochrome c: Investigation of aliphatic residues
    • Herrmann L, Bowler BE, Dong A, Caughey WS (1995) The effects of hydrophilic to hydrophobic surface mutations on the denatured state of iso-1-cytochrome c: investigation of aliphatic residues. Biochemistry 34:3040-3047
    • (1995) Biochemistry , vol.34 , pp. 3040-3047
    • Herrmann, L.1    Bowler, B.E.2    Dong, A.3    Caughey, W.S.4
  • 43
    • 0026320508 scopus 로고
    • Protein stability and molecular adaptation to extreme conditions
    • Jaenicke R (1991) Protein stability and molecular adaptation to extreme conditions. Eur J Biochem 202:715-728
    • (1991) Eur J Biochem , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 44
    • 0016624901 scopus 로고
    • Binding energy specificity and enzymic catalysis: The Circe effect
    • Jenks WP (1975) Binding energy specificity and enzymic catalysis: the Circe effect. Adv Enzymol 43:219-410
    • (1975) Adv Enzymol , vol.43 , pp. 219-410
    • Jenks, W.P.1
  • 45
    • 0028363836 scopus 로고
    • The cold-shock response: A hot topic
    • Jones PG, 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
  • 46
    • 0031888333 scopus 로고    scopus 로고
    • Structure and proposed amino acid sequence of a pepsin from Atlantic cod (Gadus morhua)
    • Karlsen S, Hough E, Olsen R (1998) Structure and proposed amino acid sequence of a pepsin from Atlantic cod (Gadus morhua) Acta Cryst D54:32-46
    • (1998) Acta Cryst , vol.D54 , pp. 32-46
    • Karlsen, S.1    Hough, E.2    Olsen, R.3
  • 47
    • 0033597205 scopus 로고    scopus 로고
    • Structural basis for cold adaptation. Sequence biochemical properties and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillum arcticum
    • Kim SY, Hwang KY, Kim SH, Sung HC, Han YS, Cho YJ (1999) Structural basis for cold adaptation. Sequence biochemical properties and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillum 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
  • 48
    • 0034603740 scopus 로고    scopus 로고
    • Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus beta-glucosidase CelB by directed evolution
    • Lebbink JH, Kaper T, Bron P, van der Oost J, de Vos WM (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
  • 49
    • 0034737312 scopus 로고    scopus 로고
    • Low temperature regulated DEAD-box RNA helicase from the Antarctic Archaeon Methanococcoides bustonii
    • Lim J, Thomas T, Cavicchioli R (2000) Low temperature regulated DEAD-box RNA helicase from the Antarctic Archaeon Methanococcoides bustonii. J Mol Biol 297:553-557
    • (2000) J Mol Biol , vol.297 , pp. 553-557
    • Lim, J.1    Thomas, T.2    Cavicchioli, R.3
  • 51
    • 0034736285 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Revisiting the thermodynamic parameters of activation may explain local flexibility
    • 36284
    • Lonhienne T, Gerday C, Feller G, (2000) Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim Biophys Acta 36284:1-10
    • (2000) Biochim Biophys Acta , pp. 1-10
    • Lonhienne, T.1    Gerday, C.2    Feller, G.3
  • 55
    • 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, 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
  • 57
    • 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, 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
  • 58
    • 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 SC, Moyens S, Terpstra P, Mainfroid V, Goraj K, Lion M, Hol WG, Martial JA (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    Lion, M.7    Hol, W.G.8    Martial, J.A.9
  • 59
    • 0001734325 scopus 로고
    • Physiology and molecular biology of psychrophilic micro-organisms
    • Herbert RA and Sharp RJ (eds) Blackie and Son, London
    • Russell NJ (1992) Physiology and molecular biology of psychrophilic micro-organisms. In: Herbert RA and Sharp RJ (eds) Molecular biology and biotechnology of extremophiles.. Blackie and Son, London, pp. 203-224
    • (1992) Molecular Biology and Biotechnology of Extremophiles , pp. 203-224
    • Russell, N.J.1
  • 60
    • 0034170458 scopus 로고    scopus 로고
    • Toward a molecular understanding of cold activity of enzymes from psychrophiles
    • Russell NJ (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
  • 61
    • 0032521220 scopus 로고    scopus 로고
    • Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium
    • Russell RJ, Gerike U, Danson MJ, Hough DW, Taylor GL (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
  • 62
    • 0027050824 scopus 로고
    • Modeling the effects of mutations on the denatured states of proteins
    • Shortle D, Chan HS, Dill KA (1992) Modeling the effects of mutations on the denatured states of proteins. Protein Sci 1:201-215
    • (1992) Protein Sci , vol.1 , pp. 201-215
    • Shortle, D.1    Chan, H.S.2    Dill, K.A.3
  • 63
    • 0000528385 scopus 로고
    • Structure determination and refinement of benzamidine inhibited trypsin from the North Atlantic salmon (Salmo salar) at 1.82 Å resolution
    • Smalas AO, Horvick A (1993) Structure determination and refinement of benzamidine inhibited trypsin from the North Atlantic salmon (Salmo salar) at 1.82 Å resolution. Acta Cryst D49:318-330
    • (1993) Acta Cryst , vol.D49 , pp. 318-330
    • Smalas, A.O.1    Horvick, A.2
  • 65
    • 0028949615 scopus 로고
    • Proteins and temperature
    • Somero GN (1995) Proteins and temperature. Annu Rev Physiol 57:43-68
    • (1995) Annu Rev Physiol , vol.57 , pp. 43-68
    • Somero, G.N.1
  • 67
    • 0031938211 scopus 로고    scopus 로고
    • Engineering of a cold-adapted protease by sequential random mutagenesis and a screening system
    • Taguchi S, Ozaki A, 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
  • 68
    • 0034033848 scopus 로고    scopus 로고
    • The complete amino acid substitutions at position 131 that are positively involved in cold adaptation of subtilisin BPN′
    • Taguchi S, Komada S, Momose H (2000) The complete amino acid substitutions at position 131 that are positively involved in cold adaptation of subtilisin BPN′. Appl Environ Microbiol 66:1410-1415
    • (2000) Appl Environ Microbiol , vol.66 , pp. 1410-1415
    • Taguchi, S.1    Komada, S.2    Momose, H.3
  • 69
    • 0031758464 scopus 로고    scopus 로고
    • Native protein fluctuations: The conformational-motion temperature and the inverse correlation of protein flexibility with protein stability
    • Tang KE, Dill KA (1998) Native protein fluctuations: the conformational-motion temperature and the inverse correlation of protein flexibility with protein stability. J Biomol Struct Dyn 16:397-411.
    • (1998) J Biomol Struct Dyn , vol.16 , pp. 397-411
    • Tang, K.E.1    Dill, K.A.2
  • 70
    • 0031762555 scopus 로고    scopus 로고
    • Archaeal cold-adapted proteins: Structural and evolutionary analysis of the elongation factor 2 proteins from psychrophilic mesophilic and thermophilic methanogens
    • Thomas T, Cavicchioli R (1998) Archaeal cold-adapted proteins: structural and evolutionary analysis of the elongation factor 2 proteins from psychrophilic mesophilic and thermophilic methanogens. FEBS Lett 439:281-286
    • (1998) FEBS Lett , vol.439 , pp. 281-286
    • Thomas, T.1    Cavicchioli, R.2
  • 71
    • 0025822794 scopus 로고
    • Relation between stability dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus
    • Varley PG, Pain RH (1991) Relation between stability dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus. J Mol Biol 220:531-538
    • (1991) J Mol Biol , vol.220 , pp. 531-538
    • Varley, P.G.1    Pain, R.H.2
  • 72
    • 0030696497 scopus 로고    scopus 로고
    • Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile Pseudomonas aeruginosa
    • Villeret V, Chessa JP, Gerday C, 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
  • 73
    • 0030860701 scopus 로고    scopus 로고
    • Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp. 15 suggest reasons for thermal instability
    • Wallon G, Lovett ST, Magyar C, Svingor A, Szilagyi A, Zavodszky P, Ringe D, Petsko GA (1997) Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp. 15 suggest reasons for thermal instability. Protein Eng 10:665-672
    • (1997) Protein Eng , vol.10 , pp. 665-672
    • Wallon, G.1    Lovett, S.T.2    Magyar, C.3    Svingor, A.4    Szilagyi, A.5    Zavodszky, P.6    Ringe, D.7    Petsko, G.A.8
  • 74
    • 0034644667 scopus 로고    scopus 로고
    • Cold adaptation of a mesophilic subtilisin-like protease by laboratory evolution
    • Wintrode PL, Miyazaki K, Arnold FH (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
  • 75
    • 0025182490 scopus 로고
    • Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima
    • Wrba A, Schweiger A, Schultes V, Jaenicke R, 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
  • 77
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodszky P, Kardos J, Svingor, Petsko GA (1998) Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. ProcNatl Acad Sci U S A 95:7406-7411
    • (1998) ProcNatl Acad Sci U S A , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor3    Petsko, G.A.4
  • 78
    • 0032973026 scopus 로고    scopus 로고
    • Directed evolution converts subtilisin e into a functional equivalent of thermitase
    • Zhao H, Arnold FH (1999) Directed evolution converts subtilisin E into a functional equivalent of thermitase. Protein Eng 12:47-53
    • (1999) Protein Eng , vol.12 , pp. 47-53
    • Zhao, H.1    Arnold, F.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.