메뉴 건너뛰기




Volumn 22, Issue 32, 2010, Pages

Protein stability and enzyme activity at extreme biological temperatures

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL ACTIVITIES; COLD ENVIRONMENT; HYPERTHERMOPHILES; LOW TEMPERATURES; METABOLIC RATES; MODEL-BASED; MOLECULAR LEVELS; MOLECULAR MOTIONS; PROTEIN STABILITY; PROTEIN STRUCTURES; ROOM TEMPERATURE; STRUCTURAL FACTOR; STRUCTURAL FLEXIBILITIES; SUB-ZERO TEMPERATURES; THERMOPHILIC ENZYMES;

EID: 77956912541     PISSN: 09538984     EISSN: 1361648X     Source Type: Journal    
DOI: 10.1088/0953-8984/22/32/323101     Document Type: Review
Times cited : (239)

References (84)
  • 1
    • 0842303296 scopus 로고    scopus 로고
    • The upper temperature for life-where do we draw the line?
    • Cowan D A 2004 The upper temperature for life-where do we draw the line? Trends Microbiol. 12 58-60
    • (2004) Trends Microbiol. , vol.12 , pp. 58-60
    • Cowan, D.A.1
  • 2
    • 0031061411 scopus 로고    scopus 로고
    • Pyrolobus fumarii, gen. and sp. nov., represents a novel group of archaea, extending the upper temperature limit for life to 113 degrees C
    • Blochl E, Rachel R, Burggraf S, Hafenbradl D, Jannasch H W and Stetter K O 1997 Pyrolobus fumarii, gen. and sp. nov., represents a novel group of archaea, extending the upper temperature limit for life to 113 degrees C Extremophiles 1 14-21
    • (1997) Extremophiles , vol.1 , pp. 14-21
    • Blochl, E.1    Rachel, R.2    Burggraf, S.3    Hafenbradl, D.4    Jannasch, H.W.5    Stetter, K.O.6
  • 8
    • 0036270790 scopus 로고    scopus 로고
    • Psychrophiles and polar regions
    • Deming J W 2002 Psychrophiles and polar regions Curr. Opin. Microbiol. 5 301-9
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 301-309
    • Deming, J.W.1
  • 10
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • D'Amico S, Marx J C, Gerday C and Feller G 2003 Activity-stability relationships in extremophilic enzymes J. Biol. Chem. 278 7891-6
    • (2003) J. Biol. Chem. , vol.278 , pp. 7891-7896
    • D'Amico, S.1    Marx, J.C.2    Gerday, C.3    Feller, G.4
  • 11
    • 0030822593 scopus 로고    scopus 로고
    • Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 degrees C
    • Hiller R, Zhou Z H, Adams M W and Englander S W 1997 Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 degrees C Proc. Natl Acad. Sci. USA 94 11329-32
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11329-11332
    • Hiller, R.1    Zhou, Z.H.2    Adams, M.W.3    Englander, S.W.4
  • 12
    • 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 25791-6
    • (2001) J. Biol. Chem. , vol.276 , pp. 25791-25796
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 13
    • 0037466287 scopus 로고    scopus 로고
    • Activity, stability and flexibility in glycosidases adapted to extreme thermal environments
    • Collins T, Meuwis M A, Gerday C and Feller G 2003 Activity, stability and flexibility in glycosidases adapted to extreme thermal environments J. Mol. Biol. 328 419-28
    • (2003) J. Mol. Biol. , vol.328 , pp. 419-428
    • Collins, T.1    Meuwis, M.A.2    Gerday, C.3    Feller, G.4
  • 14
    • 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 V N, Gerday C and Feller G 2003 Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases J. Biol. Chem. 278 37015-23
    • (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
  • 15
    • 0035960641 scopus 로고    scopus 로고
    • Thermodynamic differences among homologous thermophilic and mesophilic proteins
    • Kumar S, Tsai C J and Nussinov R 2001 Thermodynamic differences among homologous thermophilic and mesophilic proteins Biochemistry 40 14152-65
    • (2001) Biochemistry , vol.40 , pp. 14152-14165
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 17
    • 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
  • 19
    • 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 5359-74
    • (2002) Biochemistry , vol.41 , pp. 5359-5374
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 20
    • 0038333434 scopus 로고    scopus 로고
    • Temperature range of thermodynamic stability for the native state of reversible two-state proteins
    • Kumar S, Tsai C J and Nussinov R 2003 Temperature range of thermodynamic stability for the native state of reversible two-state proteins Biochemistry 42 4864-73
    • (2003) Biochemistry , vol.42 , pp. 4864-4873
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 21
    • 6344265180 scopus 로고    scopus 로고
    • Experiment-guided thermodynamic simulations on reversible two-state proteins: Implications for protein thermostability
    • Kumar S and Nussinov R 2004 Experiment-guided thermodynamic simulations on reversible two-state proteins: implications for protein thermostability Biophys. Chem. 111 235-46
    • (2004) Biophys. Chem. , vol.111 , pp. 235-246
    • Kumar, S.1    Nussinov, R.2
  • 22
    • 0037931826 scopus 로고    scopus 로고
    • Genomic correlates of hyperthermostability, an update
    • Suhre K and Claverie J M 2003 Genomic correlates of hyperthermostability, an update J. Biol. Chem. 278 17198-202
    • (2003) J. Biol. Chem. , vol.278 , pp. 17198-17202
    • Suhre, K.1    Claverie, J.M.2
  • 24
    • 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
  • 25
    • 0030834850 scopus 로고    scopus 로고
    • Temperature, stability, and the hydrophobic interaction
    • Schellman J A 1997 Temperature, stability, and the hydrophobic interaction Biophys. J. 73 2960-4
    • (1997) Biophys. J. , vol.73 , pp. 2960-2964
    • Schellman, J.A.1
  • 26
    • 0033528657 scopus 로고    scopus 로고
    • Thermodynamic stability of a cold-active α-amylase from the Antarctic bacterium
    • 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 4613-9
    • (1999) Alteromonas Haloplanctis Biochemistry , vol.38 , pp. 4613-4619
    • Feller, G.1    D'Amico, D.2    Gerday, C.3
  • 28
    • 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 11 211-6
    • (2007) Extremophiles , vol.11 , pp. 211-216
    • Feller, G.1
  • 29
    • 54149091012 scopus 로고    scopus 로고
    • Cold adaptation of enzymes: Structural, kinetic and microcalorimetric characterizations of an aminopeptidase from the Arctic psychrophile Colwellia psychrerythraea and of human leukotriene A) hydrolase
    • Huston A L, Haeggström J Z and Feller G 2008 Cold adaptation of enzymes: structural, kinetic and microcalorimetric characterizations of an aminopeptidase from the Arctic psychrophile Colwellia psychrerythraea and of human leukotriene A(4) hydrolase Biochim. Biophys. Acta 1784 1865-72
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1865-1872
    • Huston, A.L.1    Haeggström, J.Z.2    Feller, G.3
  • 30
    • 70350348011 scopus 로고    scopus 로고
    • NMR spectroscopy brings invisible protein states into focus
    • Baldwin A J and Kay L E 2009 NMR spectroscopy brings invisible protein states into focus Nat. Chem. Biol. 5 808-14
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 808-814
    • Baldwin, A.J.1    Kay, L.E.2
  • 33
    • 0028949615 scopus 로고
    • Proteins and temperature
    • Somero G N 1995 Proteins and temperature Annu. Rev. Phys. 57 43-68
    • (1995) Annu. Rev. Phys. , vol.57 , pp. 43-68
    • Somero, G.N.1
  • 34
    • 0020348367 scopus 로고
    • Stability of proteins. Proteins which do not present a single cooperative system
    • Privalov P L 1982 Stability of proteins. Proteins which do not present a single cooperative system Adv. Protein Chem. 35 1-104
    • (1982) Adv. Protein Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 36
    • 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 47 236-49
    • (2002) Proteins , vol.47 , pp. 236-249
    • Gianese, G.1    Bossa, F.2    Pascarella, S.3
  • 38
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Vieille C and Zeikus G J 2001 Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability Microbiol. Mol. Biol. Rev. 65 1-43
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 39
    • 0034981542 scopus 로고    scopus 로고
    • Structural basis of thermostability in hyperthermophilic proteins, or 'there's more than one way to skin a cat'
    • Petsko G A 2001 Structural basis of thermostability in hyperthermophilic proteins, or 'there's more than one way to skin a cat' Methods Enzymol. 334 469-78
    • (2001) Methods Enzymol. , vol.334 , pp. 469-478
    • Petsko, G.A.1
  • 40
    • 0034855858 scopus 로고    scopus 로고
    • How do thermophilic proteins deal with heat?
    • Kumar S and Nussinov R 2001 How do thermophilic proteins deal with heat? Cell Mol. Life Sci. 58 1216-33
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 1216-1233
    • Kumar, S.1    Nussinov, R.2
  • 41
    • 0037172796 scopus 로고    scopus 로고
    • Elucidation of factors responsible for enhanced thermal stability of proteins: A structural genomics based study
    • Chakravarty S and Varadarajan R 2002 Elucidation of factors responsible for enhanced thermal stability of proteins: a structural genomics based study Biochemistry 41 8152-61
    • (2002) Biochemistry , vol.41 , pp. 8152-8161
    • Chakravarty, S.1    Varadarajan, R.2
  • 42
    • 0032534759 scopus 로고    scopus 로고
    • Structures of the psychrophilic Alteromonas haloplanctis a-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 a-amylase give insights into cold adaptation at a molecular level Structure 61503-16
    • (1998) Structure , vol.6 , pp. 1503-1516
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 43
    • 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 6 351-61
    • (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
  • 44
    • 77950281429 scopus 로고    scopus 로고
    • Proteomics of life at low temperatures: Trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125
    • Piette F, D'Amico S, Struvay C, Mazzucchelli G, Renaut J, Tutino M L, Danchin A, Leprince P and Feller G 2010 Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 Mol. Microbiol. 76 120-32
    • (2010) Mol. Microbiol. , vol.76 , pp. 120-132
    • Piette, F.1    D'Amico, S.2    Struvay, C.3    Mazzucchelli, G.4    Renaut, J.5    Tutino, M.L.6    Danchin, A.7    Leprince, P.8    Feller, G.9
  • 46
    • 0035448574 scopus 로고    scopus 로고
    • Ion pairs and the thermotolerance of proteins from hyperthermophiles: A 'traffic rule' for hot roads
    • Karshikoff A and Ladenstein R 2001 Ion pairs and the thermotolerance of proteins from hyperthermophiles: a 'traffic rule' for hot roads Trends Biochem. Sci. 26 550-6
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2
  • 47
    • 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 and Pearl L H 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    Pearl, L.H.7
  • 48
    • 18744405663 scopus 로고    scopus 로고
    • Stepwise adaptations of citrate synthase to survival at life's extremes. from psychrophile to hyperthermophile
    • Bell G S, Russell R J, Connaris H, Hough D W, Danson M J and Taylor G L 2002 Stepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophile Eur. J. Biochem. 269 6250-60
    • (2002) Eur. J. Biochem. , vol.269 , pp. 6250-6260
    • Bell, G.S.1    Russell, R.J.2    Connaris, H.3    Hough, D.W.4    Danson, M.J.5    Taylor, G.L.6
  • 49
    • 3142653228 scopus 로고    scopus 로고
    • Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases
    • Bae E and Phillips G N Jr 2004 Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases J. Biol. Chem. 279 28202-8
    • (2004) J. Biol. Chem. , vol.279 , pp. 28202-28208
    • Bae, E.1    Phillips Jr, G.N.2
  • 51
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Hot topics in cold adaptation
    • Feller G and Gerday C 2003 Psychrophilic enzymes: hot topics in cold adaptation Nat. Rev. Microbiol. 1 200-8
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 52
    • 2442677663 scopus 로고    scopus 로고
    • A new intrinsic thermal parameter for enzymes reveals true temperature optima
    • Peterson M E, Eisenthal R, Danson M J, Spence A and Daniel R M 2004 A new intrinsic thermal parameter for enzymes reveals true temperature optima J. Biol. Chem. 279 20717-22
    • (2004) J. Biol. Chem. , vol.279 , pp. 20717-20722
    • Peterson, M.E.1    Eisenthal, R.2    Danson, M.J.3    Spence, A.4    Daniel, R.M.5
  • 53
    • 33847757782 scopus 로고    scopus 로고
    • The dependence of enzyme activity on temperature: Determination and validation of parameters
    • Peterson M E, Daniel R M, Danson M J and Eisenthal R 2007 The dependence of enzyme activity on temperature: determination and validation of parameters Biochem. J. 402 331-7
    • (2007) Biochem. J. , vol.402 , pp. 331-337
    • Peterson, M.E.1    Daniel, R.M.2    Danson, M.J.3    Eisenthal, R.4
  • 54
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodszky P, Kardos J, Svingor A 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 7406-11
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor, A.3    Petsko, G.A.4
  • 55
    • 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 399 496-9
    • (1999) Nature , vol.399 , pp. 496-499
    • Kohen, A.1    Cannio, R.2    Bartolucci, S.3    Klinman, J.P.4
  • 56
    • 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. 7 564-72
    • (1998) Protein Sci. , vol.7 , pp. 564-572
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 57
    • 0037342768 scopus 로고    scopus 로고
    • Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases
    • Aghajari N, Van Petegem F, Villeret V, Chessa J P, Gerday C, Haser R and Van Beeumen J 2003 Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases Proteins 50 636-47
    • (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
  • 58
    • 33645943709 scopus 로고    scopus 로고
    • Oligosaccharide binding in family 8 glycosidases: Crystal structures of active-site mutants of the beta-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product
    • De Vos D, Collins T, Nerinckx W, Savvides S N, Claeyssens M, Gerday C, Feller G and Van Beeumen J 2006 Oligosaccharide binding in family 8 glycosidases: crystal structures of active-site mutants of the beta-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product Biochemistry 45 4797-807
    • (2006) Biochemistry , vol.45 , pp. 4797-4807
    • De Vos, D.1    Collins, T.2    Nerinckx, W.3    Savvides, S.N.4    Claeyssens, M.5    Gerday, C.6    Feller, G.7    Van Beeumen, J.8
  • 59
    • 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 11761-7
    • (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
  • 60
    • 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 A O and Willassen N P 2003 The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features Acta Crystallogr. D 59 1357-65
    • (2003) Acta Crystallogr. D , vol.59 , pp. 1357-1365
    • Leiros, I.1    Moe, E.2    Lanes, O.3    Smalas, A.O.4    Willassen, N.P.5
  • 61
    • 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 40 207-17
    • (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
  • 62
    • 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. 499 171-5
    • (2001) FEBS Lett. , vol.499 , pp. 171-175
    • Brandsdal, B.O.1    Smalas, A.O.2    Aqvist, J.3
  • 64
    • 10644264362 scopus 로고    scopus 로고
    • Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis
    • Garsoux G, Lamotte J, Gerday C and Feller G 2004 Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis Biochem. J. 384 247-53
    • (2004) Biochem. J. , vol.384 , pp. 247-253
    • Garsoux, G.1    Lamotte, J.2    Gerday, C.3    Feller, G.4
  • 65
    • 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 G K, Gouet P, Gerday C, Haser R and 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 1211-24
    • (2005) J. Mol. Biol. , vol.348 , pp. 121-124
    • 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
  • 66
    • 24344486447 scopus 로고    scopus 로고
    • The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted alpha-amylase
    • Siddiqui K S, Feller G, D'Amico S, Gerday C, Giaquinto L and Cavicchioli R 2005 The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted alpha-amylase J. Bacteriol. 187 6197-205
    • (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
  • 67
    • 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 P A and Somero G N 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. USA 95 11476-81
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11476-11481
    • Fields, P.A.1    Somero, G.N.2
  • 69
    • 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. 254 356-62
    • (1998) Eur. J. Biochem. , vol.254 , pp. 356-362
    • Tsigos, I.1    Velonia, K.2    Smonou, I.3    Bouriotis, V.4
  • 70
    • 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 J S and Feller G 2006 Kinetics and energetics of ligand binding determined by microcalorimetry: insights into active site mobility in a psychrophilic alpha-amylase J. Mol. Biol. 358 1296-304
    • (2006) J. Mol. Biol. , vol.358 , pp. 1296-1304
    • D'Amico, S.1    Sohier, J.S.2    Feller, G.3
  • 71
    • 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 and Glansdorff N 2003 Metabolic enzymes from psychrophilic bacteria: challenge of adaptation to low temperatures in ornithine carbamoyltransferase from Moritella abyssi J. Bacteriol. 185 2161-8
    • (2003) J. Bacteriol. , vol.185 , pp. 2161-2168
    • Xu, Y.1    Feller, G.2    Gerday, C.3    Glansdorff, N.4
  • 72
    • 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. 310 291-7
    • (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
  • 73
    • 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
  • 74
    • 0037195912 scopus 로고    scopus 로고
    • Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted alpha-amylase
    • D'Amico S, Gerday C and Feller G 2002 Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted alpha-amylase J. Biol. Chem. 277 46110-5
    • (2002) J. Biol. Chem. , vol.277 , pp. 46110-46115
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 75
    • 0041384407 scopus 로고    scopus 로고
    • Temperature adaptation of proteins: Engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase
    • D'Amico S, Gerday C and Feller G 2003 Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase J. Mol. Biol. 332 981-8
    • (2003) J. Mol. Biol. , vol.332 , pp. 981-988
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 76
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via free-energy surfaces from theory and experiment
    • Dinner A R, Sali A, Smith L J, Dobson C M and Karplus M 2000 Understanding protein folding via free-energy surfaces from theory and experiment Trends Biochem. Sci. 25 331-9
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 331-339
    • Dinner, A.R.1    Sali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 77
    • 0033989157 scopus 로고    scopus 로고
    • Illuminating folding intermediates
    • Schultz C P 2000 Illuminating folding intermediates Nat. Struct. Biol. 7 7-10
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 7-10
    • Schultz, C.P.1
  • 78
    • 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
  • 79
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai C J, Kumar S, Ma B and Nussinov R 1999 Folding funnels, binding funnels, and protein function Protein Sci. 8 1181-90
    • (1999) Protein Sci. , vol.8 , pp. 1181-1190
    • Tsai, C.J.1    Kumar, S.2    Ma, B.3    Nussinov, R.4
  • 80
    • 0033970020 scopus 로고    scopus 로고
    • Folding and binding cascades: Dynamic landscapes and population shifts
    • Kumar S, Ma B, Tsai C J, Sinha N and Nussinov R 2000 Folding and binding cascades: dynamic landscapes and population shifts Protein Sci. 9 10-9
    • (2000) Protein Sci. , vol.9 , pp. 10-19
    • Kumar, S.1    Ma, B.2    Tsai, C.J.3    Sinha, N.4    Nussinov, R.5
  • 81
    • 0034696766 scopus 로고    scopus 로고
    • Transition-state ensemble in enzyme catalysis: Possibility, reality, or necessity?
    • Ma B, Kumar S, Tsai C J, Hu Z and Nussinov R 2000 Transition-state ensemble in enzyme catalysis: possibility, reality, or necessity? J. Theor. Biol. 203 383-97
    • (2000) J. Theor. Biol. , vol.203 , pp. 383-397
    • Ma, B.1    Kumar, S.2    Tsai, C.J.3    Hu, Z.4    Nussinov, R.5
  • 83
    • 52249116531 scopus 로고    scopus 로고
    • Cold adaptation of enzyme reaction rates
    • Bjelic S, Brandsdal B O and Aqvist J 2008 Cold adaptation of enzyme reaction rates Biochemistry 47 10049-57
    • (2008) Biochemistry , vol.47 , pp. 10049-10057
    • Bjelic, S.1    Brandsdal, B.O.2    Aqvist, J.3
  • 84
    • 66149121843 scopus 로고    scopus 로고
    • Cold adaptation of zinc metalloproteases in the thermolysin family from deep sea and arctic sea ice bacteria revealed by catalytic and structural properties and molecular dynamics: New insights into relationship between conformational flexibility and hydrogen bonding
    • Xie B B, Bian F, Chen X L, He H L, Guo J, Gao X, Zeng Y X, Chen B, Zhou B C and Zhang Y Z 2009 Cold adaptation of zinc metalloproteases in the thermolysin family from deep sea and arctic sea ice bacteria revealed by catalytic and structural properties and molecular dynamics: new insights into relationship between conformational flexibility and hydrogen bonding J. Biol. Chem. 284 9257-69
    • (2009) J. Biol. Chem. , vol.284 , pp. 9257-9269
    • Xie, B.B.1    Bian, F.2    Chen, X.L.3    He, H.L.4    Guo, J.5    Gao, X.6    Zeng, Y.X.7    Chen, B.8    Zhou, B.C.9    Zhang, Y.Z.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.