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Volumn , Issue , 2008, Pages 211-227

Fundamentals of cold-adapted enzymes

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EID: 77955557854     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-540-74335-4_13     Document Type: Chapter
Times cited : (40)

References (79)
  • 1
    • 0032534759 scopus 로고    scopus 로고
    • Structures of the psychrophilic Alteromonas haloplanctis ?-amylase give insights into cold adaptation at a molecular level
    • Aghajari N, Feller G, Gerday C, Haser R (1998a) Structures of the psychrophilic Alteromonas haloplanctis ?-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
  • 2
    • 0031910806 scopus 로고    scopus 로고
    • Crystal structures of the psychrophilic ?-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor
    • Aghajari N, Feller G, Gerday C, Haser R (1998b) Crystal structures of the psychrophilic ?-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
  • 3
    • 0037342768 scopus 로고    scopus 로고
    • Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by coldadapted proteases
    • Aghajari N, Van Petegem F, Villeret V, Chessa JP, Gerday C, Haser R, Van Beeumen J (2003) Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by coldadapted proteases. Proteins 50:636-647
    • (2003) Proteins , vol.50 , pp. 636-647
    • Aghajari, N.1    Van Petegem, F.2    Villeret, V.3    Chessa, J.P.4    Gerday, C.5    Haser, R.6    Van Beeumen, J.7
  • 5
    • 13444251072 scopus 로고    scopus 로고
    • Crystal structure of a subtilisin-like serine proteinase from a psychrotrophic Vibrio species reveals structural aspects of cold adaptation
    • Arnorsdottir J, Kristjansson MM, Ficner R (2005) Crystal structure of a subtilisin-like serine proteinase from a psychrotrophic Vibrio species reveals structural aspects of cold adaptation. Febs J 272:832-845
    • (2005) Febs J , vol.272 , pp. 832-845
    • Arnorsdottir, J.1    Kristjansson, M.M.2    Ficner, R.3
  • 6
    • 0000804930 scopus 로고
    • Uber die Reaktionsgeschwindigkeit bei der Inversion von Rohrzucker durch Sauren
    • Arrhenius S (1889) Uber die Reaktionsgeschwindigkeit bei der Inversion von Rohrzucker durch Sauren. Z Physik Chem 4:226-248
    • (1889) Z Physik Chem , vol.4 , pp. 226-248
    • Arrhenius, S.1
  • 7
    • 3142653228 scopus 로고    scopus 로고
    • Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases
    • Bae E, Phillips GN Jr (2004) Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases. J Biol Chem 279:28202-28208
    • (2004) J Biol Chem , vol.279 , pp. 28202-28208
    • Bae, E.1    Phillips Jr., G.N.2
  • 8
    • 0035316876 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a chitinase gene from the Antarctic psychrotolerant bacterium Vibrio sp strain Fi:7
    • Bendt A, Huller H, Kammel U, Helmke E, Schweder T (2001) Cloning, expression, and characterization of a chitinase gene from the Antarctic psychrotolerant bacterium Vibrio sp. strain Fi:7. Extremophiles 5:119-126
    • (2001) Extremophiles , vol.5 , pp. 119-126
    • Bendt, A.1    Huller, H.2    Kammel, U.3    Helmke, E.4    Schweder, T.5
  • 9
    • 0034646605 scopus 로고    scopus 로고
    • Structural, kinetic, and calorimetric characterization of the cold-active phosphoglycerate kinase from the antarctic Pseudomonas sp
    • 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 Pseudomonas sp. TACII18. J Biol Chem 275:11147-11153
    • (2000) TACII18. 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
  • 11
    • 0008298889 scopus 로고    scopus 로고
    • Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125 Cloning, expression, properties, and molecular modelling
    • Birolo L, Tutino ML, Fontanella B, Gerday C, Mainolfi K, Pascarella S, Sannia G, Vinci F, Marino G (2000) Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties, and molecular modelling. Eur J Biochem 267:2790-2802
    • (2000) Eur J Biochem , vol.267 , pp. 2790-2802
    • Birolo, L.1    Tutino, M.L.2    Fontanella, B.3    Gerday, C.4    Mainolfi, K.5    Pascarella, S.6    Sannia, G.7    Vinci, F.8    Marino, G.9
  • 12
    • 0033426952 scopus 로고    scopus 로고
    • Comparative molecular dynamics of mesophilic and psychrophilic protein homologues studied by 1. 2 ns simulations
    • Brandsdal BO, Heimstad ES, Sylte I, Smalas AO (1999) Comparative molecular dynamics of mesophilic and psychrophilic protein homologues studied by 1.2 ns simulations. J Biomol Struct Dyn 17:493-506
    • (1999) J Biomol Struct Dyn , vol.17 , pp. 493-506
    • Brandsdal, B.O.1    Heimstad, E.S.2    Sylte, I.3    Smalas, A.O.4
  • 13
    • 0034660603 scopus 로고    scopus 로고
    • Purification, physico-chemical characterization and sequence of a heat labile alkaline metalloprotease isolated from a psychrophilic Pseudomonas species
    • Chessa JP, Petrescu I, Bentahir M, Van Beeumen J, Gerday C (2000) Purification, physico-chemical characterization and sequence of a heat labile alkaline metalloprotease isolated from a psychrophilic Pseudomonas species. Biochim Biophys Acta. 1479:265-274
    • (2000) Biochim Biophys Acta , vol.1479 , pp. 265-274
    • Chessa, J.P.1    Petrescu, I.2    Bentahir, M.3    Van Beeumen, J.4    Gerday, C.5
  • 14
    • 1242296224 scopus 로고    scopus 로고
    • The precursor of a psychrophilic alpha-amylase: Structural characterization and insights into cold adaptation
    • Claverie P, Vigano C, Ruysschaert JM, Gerday C, Feller G (2003) The precursor of a psychrophilic alpha-amylase: structural characterization and insights into cold adaptation. Biochim Biophys Acta 1649:119-122
    • (2003) Biochim Biophys Acta , vol.1649 , pp. 119-122
    • Claverie, P.1    Vigano, C.2    Ruysschaert, J.M.3    Gerday, C.4    Feller, G.5
  • 17
    • 0037466287 scopus 로고    scopus 로고
    • Activity, stability and flexibility in glycosidases adapted to extreme thermal environments
    • Collins T, Meuwis MA, Gerday C, Feller G (2003) Activity, stability and flexibility in glycosidases adapted to extreme thermal environments. J Mol Biol 328:419-428
    • (2003) J Mol Biol , vol.328 , pp. 419-428
    • Collins, T.1    Meuwis, M.A.2    Gerday, C.3    Feller, G.4
  • 19
    • 0026760697 scopus 로고
    • Evolutionary adaptation to different thermal environments via transcriptional regulation
    • Crawford DL, Powers DA (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
  • 20
    • 0035854688 scopus 로고    scopus 로고
    • Structural determinants of cold adaptation and stability in a large protein
    • D'Amico S, Gerday C, 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
  • 21
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • D'Amico S, Marx JC, Gerday C, Feller G (2003) Activity-stability relationships in extremophilic enzymes. J Biol Chem 278:7891-7896
    • (2003) J Biol Chem , vol.278 , pp. 7891-7896
    • D'amico, S.1    Marx, J.C.2    Gerday, C.3    Feller, G.4
  • 23
    • 33646087677 scopus 로고    scopus 로고
    • Kinetics and energetics of ligand binding determined by microcalorimetry: Insights into active site mobility in a psychrophilic alpha-amylase
    • D'Amico S, Sohier JS, Feller G (2006b) Kinetics and energetics of ligand binding determined by microcalorimetry: insights into active site mobility in a psychrophilic alpha-amylase. J Mol Biol 358:1296-1304
    • (2006) J Mol Biol , vol.358 , pp. 1296-1304
    • D'amico, S.1    Sohier, J.S.2    Feller, G.3
  • 24
    • 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
  • 26
    • 33751502199 scopus 로고    scopus 로고
    • Structural investigation of cold activity and regulation of aspartate carbamoyltransferase from the extreme psychrophilic bacterium Moritella profunda
    • De Vos D, Xu Y, Hulpiau P, Vergauwen B, Van Beeumen JJ (2007) Structural investigation of cold activity and regulation of aspartate carbamoyltransferase from the extreme psychrophilic bacterium Moritella profunda. J Mol Biol 365:379-395
    • (2007) J Mol Biol , vol.365 , pp. 379-395
    • De Vos, D.1    Xu, Y.2    Hulpiau, P.3    Vergauwen, B.4    Van Beeumen, J.J.5
  • 27
    • 0024463170 scopus 로고
    • Kinetics of the lactate dehydrogenase reaction in high-viscosity media
    • Demchenko AP, Ruskyn OI, Saburova EA (1989) Kinetics of the lactate dehydrogenase reaction in high-viscosity media. Biochim Biophys Acta. 998:196-203
    • (1989) Biochim Biophys Acta. , vol.998 , pp. 196-203
    • Demchenko, A.P.1    Ruskyn, O.I.2    Saburova, E.A.3
  • 28
    • 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, Matagne RF (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
  • 29
    • 0026673888 scopus 로고
    • Purification, characterization, and nucleotide sequence of the thermolabile ?-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 ?-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
  • 30
  • 31
    • 33847311388 scopus 로고    scopus 로고
    • Life at low temperatures: Is disorder the driving force
    • Feller G (2007) Life at low temperatures: is disorder the driving force? Extremophiles 11:211-216
    • (2007) Extremophiles , vol.11 , pp. 211-216
    • Feller, G.1
  • 32
    • 0034973280 scopus 로고    scopus 로고
    • Review: Protein function at thermal extremes: Balancing stability and flexibility
    • Fields PA (2001) Review: 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
  • 33
    • 0034673092 scopus 로고    scopus 로고
    • Hydrogen exchange at the core of Escherichia coli alkaline phosphatase studied by room-temperature tryptophan phosphorescence
    • Fischer CJ, Schauerte JA, Wisser KC, Gafni A, Steel DG (2000) Hydrogen exchange at the core of Escherichia coli alkaline phosphatase studied by room-temperature tryptophan phosphorescence. Biochemistry. 39:1455-1461
    • (2000) Biochemistry , vol.39 , pp. 1455-1461
    • Fischer, C.J.1    Schauerte, J.A.2    Wisser, K.C.3    Gafni, A.4    Steel, D.G.5
  • 34
    • 0346726109 scopus 로고    scopus 로고
    • How enzymes work: Analysis by modern rate theory and computer simulations
    • Garcia-Viloca M, Gao J, Karplus M, Truhlar DG (2004) How enzymes work: analysis by modern rate theory and computer simulations. Science 303:186-195
    • (2004) Science , vol.303 , pp. 186-195
    • Garcia-Viloca, M.1    Gao, J.2    Karplus, M.3    Truhlar, D.G.4
  • 35
    • 0141596172 scopus 로고    scopus 로고
    • Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases
    • Georlette D, Damien B, Blaise V, Depiereux E, Uversky VN, Gerday C, Feller G (2003) Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases. J Biol Chem 278:37015-37023
    • (2003) J Biol Chem , vol.278 , pp. 37015-37023
    • Georlette, D.1    Damien, B.2    Blaise, V.3    Depiereux, E.4    Uversky, V.N.5    Gerday, C.6    Feller, G.7
  • 37
    • 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
  • 38
    • 0031698348 scopus 로고    scopus 로고
    • The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor
    • Helland R, Leiros I, Berglund GI, Willassen NP, Smalas AO (1998) The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor. Eur J Biochem 256:317-324
    • (1998) Eur J Biochem , vol.256 , pp. 317-324
    • Helland, R.1    Leiros, I.2    Berglund, G.I.3    Willassen, N.P.4    Smalas, A.O.5
  • 39
    • 33644875168 scopus 로고    scopus 로고
    • The 1.8 A crystal structure of a proteinase K-like enzyme from a psychrotroph Serratia species
    • Helland R, Larsen AN, Smalas AO, Willassen NP (2006) The 1.8 A crystal structure of a proteinase K-like enzyme from a psychrotroph Serratia species. FEBS J 273:61-71
    • (2006) FEBS J , vol.273 , pp. 61-71
    • Helland, R.1    Larsen, A.N.2    Smalas, A.O.3    Willassen, N.P.4
  • 41
    • 0034548849 scopus 로고    scopus 로고
    • Remarkably low temperature optima for extracellular enzyme activity from Arctic bacteria and sea ice
    • Huston AL, Krieger-Brockett BB, Deming JW (2000) Remarkably low temperature optima for extracellular enzyme activity from Arctic bacteria and sea ice. Environ Microbiol 2:383-388
    • (2000) Environ Microbiol , vol.2 , pp. 383-388
    • Huston, A.L.1    Krieger-Brockett, B.B.2    Deming, J.W.3
  • 42
    • 0031888333 scopus 로고    scopus 로고
    • Structure and proposed amino-acid sequence of a pepsin from atlantic cod (Gadus morhua)
    • Karlsen S, Hough E, Olsen RL (1998) Structure and proposed amino-acid sequence of a pepsin from atlantic cod (Gadus morhua). Acta Crystallogr D Biol Crystallogr 54:32-46
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , pp. 32-46
    • Karlsen, S.1    Hough, E.2    Olsen, R.L.3
  • 43
    • 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 SY, Hwang KY, Kim SH, Sung HC, Han YS, Cho Y (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.6
  • 44
    • 0035960641 scopus 로고    scopus 로고
    • Thermodynamic differences among homologous thermophilic and mesophilic proteins
    • Kumar S, Tsai CJ, Nussinov R (2001) Thermodynamic differences among homologous thermophilic and mesophilic proteins. Biochemistry 40:14152-14165
    • (2001) Biochemistry , vol.40 , pp. 14152-14165
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 45
    • 0042568932 scopus 로고    scopus 로고
    • The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features
    • Leiros I, Moe E, Lanes O, Smalas AO, Willassen NP (2003) The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features. Acta Crystallogr D Biol Crystallogr 59:1357-1365
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 1357-1365
    • Leiros, I.1    Moe, E.2    Lanes, O.3    Smalas, A.O.4    Willassen, N.P.5
  • 46
    • 0029138519 scopus 로고
    • Thermal adaptation of cytoplasmic malate dehydrogenases of eastern Pacific barracuda (Sphyraena spp): The role of differential isoenzyme expression
    • Lin JJ, Somero G (1995) Thermal adaptation of cytoplasmic malate dehydrogenases of eastern Pacific barracuda (Sphyraena spp): the role of differential isoenzyme expression. J Exp Biol 198:551-560
    • (1995) J Exp Biol , vol.198 , pp. 551-560
    • Lin, J.J.1    Somero, G.2
  • 47
    • 0034736285 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Revisiting the thermodynamic parameters of activation may explain local flexibility
    • Lonhienne T, Gerday C, 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
  • 48
    • 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 CE, Feller G, Gerday C, 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
  • 49
    • 0027965116 scopus 로고
    • Hydration effects in protein unfolding
    • Makhatadze GI, Privalov PL (1994) Hydration effects in protein unfolding. Biophys Chem 51:291-309
    • (1994) Biophys Chem , vol.51 , pp. 291-309
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 51
    • 0021228382 scopus 로고
    • Diffusion in the aqueous compartment
    • Mastro AM, Keith AD (1984) Diffusion in the aqueous compartment. J Cell Biol 99:180-187
    • (1984) J Cell Biol , vol.99 , pp. 180-187
    • Mastro, A.M.1    Keith, A.D.2
  • 53
    • 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
  • 54
    • 0033574176 scopus 로고    scopus 로고
    • Characterization of psychrophilic alanine racemase from Bacillus psychrosaccharolyticus
    • Okubo Y, Yokoigawa K, Esaki N, Soda K, Kawai H (1999) Characterization of psychrophilic alanine racemase from Bacillus psychrosaccharolyticus. Biochem Biophys Res Commun 256:333-340
    • (1999) Biochem Biophys Res Commun , vol.256 , pp. 333-340
    • Okubo, Y.1    Yokoigawa, K.2    Esaki, N.3    Soda, K.4    Kawai, H.5
  • 55
    • 23844458318 scopus 로고    scopus 로고
    • Increased Flexibility as a Strategy for Cold Adaptation: A comparative molecular dynamics study of cold-and warm-active uracil DNA glycosylase
    • Olufsen M, Smalas AO, Moe E, Brandsdal BO (2005) Increased Flexibility as a Strategy for Cold Adaptation: A comparative molecular dynamics study of cold-and warm-active uracil DNA glycosylase. J Biol Chem 280:18042-18048
    • (2005) J Biol Chem , vol.280 , pp. 18042-18048
    • Olufsen, M.1    Smalas, A.O.2    Moe, E.3    Brandsdal, B.O.4
  • 56
    • 33747756504 scopus 로고    scopus 로고
    • Flexibility and enzymatic coldadaptation: A comparative molecular dynamics investigation of the elastase family
    • Papaleo E, Riccardi L, Villa C, Fantucci P, De Gioia L (2006) Flexibility and enzymatic coldadaptation: A comparative molecular dynamics investigation of the elastase family. Biochim Biophys Acta 1764:1397-1406
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1397-1406
    • Papaleo, E.1    Riccardi, L.2    Villa, C.3    Fantucci, P.4    De Gioia, L.5
  • 58
    • 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
  • 59
    • 9444221967 scopus 로고    scopus 로고
    • A novel thermodynamic relationship based on Kramers Theory for studying enzyme kinetics under high viscosity
    • Siddiqui KS, Bokhari SA, Afzal AJ, Singh S (2004) A novel thermodynamic relationship based on Kramers Theory for studying enzyme kinetics under high viscosity. IUBMB Life 56:403-407
    • (2004) IUBMB Life , vol.56 , pp. 403-407
    • Siddiqui, K.S.1    Bokhari, S.A.2    Afzal, A.J.3    Singh, S.4
  • 60
    • 24344486447 scopus 로고    scopus 로고
    • The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted alphaamylase
    • Siddiqui KS, Feller G, D'Amico S, Gerday C, Giaquinto L, Cavicchioli R (2005) The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted alphaamylase. J Bacteriol 187:6197-6205
    • (2005) J Bacteriol , vol.187 , pp. 6197-6205
    • Siddiqui, K.S.1    Feller, G.2    D'amico, S.3    Gerday, C.4    Giaquinto, L.5    Cavicchioli, R.6
  • 64
    • 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
  • 66
    • 13444309317 scopus 로고    scopus 로고
    • Stabilities and activities of the N-and C-domains of FKBP22 from a psychrotrophic bacterium overproduced in Escherichia coli
    • Suzuki Y, Takano K, Kanaya S (2005) Stabilities and activities of the N-and C-domains of FKBP22 from a psychrotrophic bacterium overproduced in Escherichia coli. FEBS J 272:632-642
    • (2005) FEBS J , vol.272 , pp. 632-642
    • Suzuki, Y.1    Takano, K.2    Kanaya, S.3
  • 67
    • 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, 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
  • 69
    • 18744406984 scopus 로고    scopus 로고
    • Crystal structure and nucleotide sequence of an anionic trypsin from chum salmon (Oncorhynchus keta) in comparison with Atlantic salmon (Salmo salar) and bovine trypsin
    • Toyota E, Ng KK, Kuninaga S, Sekizaki H, Itoh K, Tanizawa K, James MN (2002) Crystal structure and nucleotide sequence of an anionic trypsin from chum salmon (Oncorhynchus keta) in comparison with Atlantic salmon (Salmo salar) and bovine trypsin. J Mol Biol 324:391-397
    • (2002) J Mol Biol , vol.324 , pp. 391-397
    • Toyota, E.1    Ng, K.K.2    Kuninaga, S.3    Sekizaki, H.4    Itoh, K.5    Tanizawa, K.6    James, M.N.7
  • 70
    • 17044370905 scopus 로고    scopus 로고
    • Crystal structure of cold-active protein-tyrosine phosphatase from a psychrophile, Shewanella sp
    • Tokyo
    • Tsuruta H, Mikami B, Aizono Y (2005) Crystal structure of cold-active protein-tyrosine phosphatase from a psychrophile, Shewanella sp. J Biochem (Tokyo) 137:69-77
    • (2005) J Biochem , vol.137 , pp. 69-77
    • Tsuruta, H.1    Mikami, B.2    Aizono, Y.3
  • 71
    • 0028773288 scopus 로고
    • The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
    • Uppenberg J, Hansen MT, Patkar S, Jones TA (1994) The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure. 2:293-308
    • (1994) Structure , vol.2 , pp. 293-308
    • Uppenberg, J.1    Hansen, M.T.2    Patkar, S.3    Jones, T.A.4
  • 72
    • 0037470085 scopus 로고    scopus 로고
    • The structure of a cold-adapted family 8 xylanase at 1. 3 A resolution. Structural adaptations to cold and investigation of the active site
    • Van Petegem F, Collins T, Meuwis MA, Gerday C, Feller G, Van Beeumen J (2003) The structure of a cold-adapted family 8 xylanase at 1.3 A resolution. Structural adaptations to cold and investigation of the active site. J Biol Chem 278:7531-7539
    • (2003) J Biol Chem , vol.278 , pp. 7531-7539
    • Van Petegem, F.1    Collins, T.2    Meuwis, M.A.3    Gerday, C.4    Feller, G.5    Van Beeumen, J.6
  • 73
    • 18044372844 scopus 로고    scopus 로고
    • Structure of a full length psychrophilic cellulase from Pseudoalteromonas haloplanktis revealed by X-ray diffraction and small angle X-ray scattering
    • Violot S, Aghajari N, Czjzek M, Feller G, Sonan GK, Gouet P, Gerday C, Haser R, Receveur-Brechot V (2005) Structure of a full length psychrophilic cellulase from Pseudoalteromonas haloplanktis revealed by X-ray diffraction and small angle X-ray scattering. J Mol Biol 348:1211-1224
    • (2005) J Mol Biol , vol.348 , pp. 1211-1224
    • Violot, S.1    Aghajari, N.2    Czjzek, M.3    Feller, G.4    Sonan, G.K.5    Gouet, P.6    Gerday, C.7    Haser, R.8    Receveur-Brechot, V.9
  • 75
    • 0035840105 scopus 로고    scopus 로고
    • Patterns of adaptation in a laboratory evolved thermophilic enzyme
    • Wintrode PL, Miyazaki K, Arnold FH (2001) Patterns of adaptation in a laboratory evolved thermophilic enzyme. Biochim Biophys Acta. 1549:1-8
    • (2001) Biochim Biophys Acta , vol.1549 , pp. 1-8
    • Wintrode, P.L.1    Miyazaki, K.2    Arnold, F.H.3
  • 76
    • 0037377799 scopus 로고    scopus 로고
    • Metabolic enzymes from psychrophilic bacteria: Challenge of adaptation to low temperatures in ornithine carbamoyltransferase from Moritella abyssi
    • Xu Y, Feller G, Gerday C, Glansdorff N (2003a) Metabolic enzymes from psychrophilic bacteria: challenge of adaptation to low temperatures in ornithine carbamoyltransferase from Moritella abyssi. J Bacteriol 185:2161-2168
    • (2003) J Bacteriol , vol.185 , pp. 2161-2168
    • Xu, Y.1    Feller, G.2    Gerday, C.3    Glansdorff, N.4
  • 77
    • 0042337202 scopus 로고    scopus 로고
    • Moritella cold-active dihydrofolate reductase: Are there natural limits to optimization of catalytic efficiency at low temperature
    • Xu Y, Feller G, Gerday C, Glansdorff N (2003b) Moritella cold-active dihydrofolate reductase: are there natural limits to optimization of catalytic efficiency at low temperature? J Bacteriol 185:5519-5526
    • (2003) J Bacteriol , vol.185 , pp. 5519-5526
    • Xu, Y.1    Feller, G.2    Gerday, C.3    Glansdorff, N.4
  • 78
    • 0037360652 scopus 로고    scopus 로고
    • Moritella profunda sp nov. and Moritella abyssi sp. nov., two psychropiezophilic organisms isolated from deep Atlantic sediments
    • Xu Y, Nogi Y, Kato C, Liang Z, Ruger HJ, De Kegel D, Glansdorff N (2003c) Moritella profunda sp. nov. and Moritella abyssi sp. nov., two psychropiezophilic organisms isolated from deep Atlantic sediments. Int J Syst Evol Microbiol 53:533-538
    • (2003) Int J Syst Evol Microbiol , vol.53 , pp. 533-538
    • Xu, Y.1    Nogi, Y.2    Kato, C.3    Liang, Z.4    Ruger, H.J.5    De Kegel, D.6    Glansdorff, N.7
  • 79
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • USA
    • Zavodszky P, Kardos J, Svingor, Petsko GA (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 , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor3    Petsko, G.A.4


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