메뉴 건너뛰기




Volumn 13, Issue 9, 2012, Pages 11643-11665

Optimization to low temperature activity in psychrophilic enzymes

Author keywords

Biotechnology; Cold adaptation; Enzyme activity; Extremophiles; Psychrophiles

Indexed keywords

INDUSTRIAL ENZYME; MICROBIAL ENZYME;

EID: 84866927713     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms130911643     Document Type: Article
Times cited : (189)

References (114)
  • 2
    • 0036270790 scopus 로고    scopus 로고
    • Psychrophiles and polar regions
    • Deming, J.W. Psychrophiles and polar regions. Curr. Opin. Microbiol. 2002, 5, 301-309
    • (2002) Curr. Opin. Microbiol , vol.5 , pp. 301-309
    • Deming, J.W.1
  • 3
    • 0038279773 scopus 로고
    • Endolithic microorganisms in the Antarctic cold desert
    • Friedmann, E.I. Endolithic microorganisms in the Antarctic cold desert. Science 1982, 215, 1045-1053
    • (1982) Science , vol.215 , pp. 1045-1053
    • Friedmann, E.I.1
  • 6
    • 34548370571 scopus 로고    scopus 로고
    • Ecology and Biodiversity of Cold-adapted Microorganisms
    • Gerday, C., Glansdorff, N., Eds.; ASM Press: Washington, DC, USA
    • Cowan, D.A.; Casanueva, A.; Stafford, W. Ecology and Biodiversity of Cold-adapted Microorganisms. In Physiology and Biochemistry of Extremophiles; Gerday, C., Glansdorff, N., Eds.; ASM Press: Washington, DC, USA, 2007; pp. 119-132
    • (2007) Physiology and Biochemistry of Extremophiles , pp. 119-132
    • Cowan, D.A.1    Casanueva, A.2    Stafford, W.3
  • 8
    • 1842509102 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Hot topics in cold adaptation
    • Feller, G.; Gerday, C. Psychrophilic enzymes: Hot topics in cold adaptation. Nat. Rev. Microbiol. 2003, 1, 200-208
    • (2003) Nat. Rev. Microbiol , vol.1 , pp. 200-208
    • Feller, G.1    Gerday, C.2
  • 10
    • 77956912541 scopus 로고    scopus 로고
    • Protein stability and enzyme activity at extreme biological temperatures
    • doi 10.1088/0953-8984/1022/1032/323101
    • Feller, G. Protein stability and enzyme activity at extreme biological temperatures. J. Phys. Condens. Mat. 2010, 22, doi 10.1088/0953-8984/1022/1032/323101
    • (2010) J. Phys. Condens. Mat , pp. 22
    • Feller, G.1
  • 11
    • 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. Purification, characterization, and nucleotide sequence of the thermolabile α-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23. J. Biol. Chem. 1992, 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
  • 13
    • 0037466287 scopus 로고    scopus 로고
    • Activity, stability and flexibility in glycosidases adapted to extreme thermal environments
    • Collins, T.; Meuwis, M.A.; Gerday, C.; Feller, G. Activity, stability and flexibility in glycosidases adapted to extreme thermal environments. J. Mol. Biol. 2003, 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
  • 14
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • D'Amico, S.; Marx, J.C.; Gerday, C.; Feller, G. Activity-stability relationships in extremophilic enzymes. J. Biol. Chem. 2003, 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
  • 15
    • 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.; Feller, G. Structural and functional adaptations to extreme temperatures in psychrophilic, mesophilic, and thermophilic DNA ligases. J. Biol. Chem. 2003, 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
  • 16
    • 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.; Cavicchioli, R. The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted alpha-amylase. J. Bacteriol. 2005, 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
  • 17
    • 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.; Somero, G.N. 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 1998, 95, 11476-11481
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11476-11481
    • Fields, P.A.1    Somero, G.N.2
  • 19
    • 34547680284 scopus 로고    scopus 로고
    • Structural and functional properties of isocitrate dehydrogenase from the psychrophilic bacterium Desulfotalea psychrophila reveal a cold-active enzyme with an unusual high thermal stability
    • Fedoy, A.E.; Yang, N.; Martinez, A.; Leiros, H.K.; Steen, I.H. Structural and functional properties of isocitrate dehydrogenase from the psychrophilic bacterium Desulfotalea psychrophila reveal a cold-active enzyme with an unusual high thermal stability. J. Mol. Biol. 2007, 372, 130-149
    • (2007) J. Mol. Biol , vol.372 , pp. 130-149
    • Fedoy, A.E.1    Yang, N.2    Martinez, A.3    Leiros, H.K.4    Steen, I.H.5
  • 20
    • 0037711318 scopus 로고    scopus 로고
    • GroEL from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125: Molecular characterization and gene cloning
    • Tosco, A.; Birolo, L.; Madonna, S.; Lolli, G.; Sannia, G.; Marino, G. GroEL from the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC 125: Molecular characterization and gene cloning. Extremophiles 2003, 7, 17-28
    • (2003) Extremophiles , vol.7 , pp. 17-28
    • Tosco, A.1    Birolo, L.2    Madonna, S.3    Lolli, G.4    Sannia, G.5    Marino, G.6
  • 21
    • 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.; Feller, G. Proteomics of life at low temperatures: Trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125. Mol. Microbiol. 2010, 76, 120-132
    • (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
  • 22
    • 84860841914 scopus 로고    scopus 로고
    • Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125
    • Falasca, P.; Evangelista, G.; Cotugno, R.; Marco, S.; Masullo, M.; De Vendittis, E.; Raimo, G. Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125. Extremophiles 2012, 16, 539-552
    • (2012) Extremophiles , vol.16 , pp. 539-552
    • Falasca, P.1    Evangelista, G.2    Cotugno, R.3    Marco, S.4    Masullo, M.5    de Vendittis, E.6    Raimo, G.7
  • 23
    • 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. Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor. Protein Sci. 1998, 7, 564-572
    • (1998) Protein Sci , vol.7 , pp. 564-572
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 24
    • 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. Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level. Structure 1998, 6, 1503-1516
    • (1998) Structure , vol.6 , pp. 1503-1516
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 25
    • 0037007004 scopus 로고    scopus 로고
    • Crystallographic evidence of a transglycosylation reaction: Ternary complexes of a psychrophilic alpha-amylase
    • Aghajari, N.; Roth, M.; Haser, R. Crystallographic evidence of a transglycosylation reaction: Ternary complexes of a psychrophilic alpha-amylase. Biochemistry 2002, 41, 4273-4280
    • (2002) Biochemistry , vol.41 , pp. 4273-4280
    • Aghajari, N.1    Roth, M.2    Haser, R.3
  • 26
    • 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. 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 1994, 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
  • 27
    • 77957203764 scopus 로고    scopus 로고
    • Enzyme Function at Low Temperatures in Psychrophiles
    • Siddiqui, K.S., Thomas, T., Eds.; Nova Science Publishers: New York, NY, USA
    • Feller, G. Enzyme Function at Low Temperatures in Psychrophiles. In Protein Adaptation in Extremophiles; Siddiqui, K.S., Thomas, T., Eds.; Nova Science Publishers: New York, NY, USA, 2008; pp. 35-69
    • (2008) Protein Adaptation In Extremophiles , pp. 35-69
    • Feller, G.1
  • 28
    • 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.; Taylor, G.L. Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium. Structure 1998, 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
  • 29
    • 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.; Van Beeumen, J. Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. Proteins 2003, 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
  • 30
    • 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.; Cho, Y.J. Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum. J. Biol. Chem. 1999, 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
  • 31
    • 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.; Willassen, N.P. The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features. Acta Crystallogr. D Biol. Crystallogr. 2003, 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
  • 33
    • 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.; Smalas, A.O. Electrostatics of mesophilic and psychrophilic trypsin isoenzymes: Qualitative evaluation of electrostatic differences at the substrate binding site. Proteins 2000, 40, 207-217
    • (2000) Proteins , vol.40 , pp. 207-217
    • Gorfe, A.A.1    Brandsdal, B.O.2    Leiros, H.K.3    Helland, R.4    Smalas, A.O.5
  • 34
    • 0035875953 scopus 로고    scopus 로고
    • Electrostatic effects play a central role in cold adaptation of trypsin
    • Brandsdal, B.O.; Smalas, A.O.; Aqvist, J. Electrostatic effects play a central role in cold adaptation of trypsin. FEBS Lett. 2001, 499, 171-175
    • (2001) FEBS Lett , vol.499 , pp. 171-175
    • Brandsdal, B.O.1    Smalas, A.O.2    Aqvist, J.3
  • 35
    • 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.; Bouriotis, V. Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123. Eur. J. Biochem. 1998, 254, 356-362
    • (1998) Eur. J. Biochem , vol.254 , pp. 356-362
    • Tsigos, I.1    Velonia, K.2    Smonou, I.3    Bouriotis, V.4
  • 36
    • 77958176737 scopus 로고    scopus 로고
    • Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis
    • Merlino, A.; Russo Krauss, I.; Castellano, I.; de Vendittis, E.; Rossi, B.; Conte, M.; Vergara, A.; Sica, F. Structure and flexibility in cold-adapted iron superoxide dismutases: The case of the enzyme isolated from Pseudoalteromonas haloplanktis. J. Struct. Biol. 2010, 172, 343-352
    • (2010) J. Struct. Biol , vol.172 , pp. 343-352
    • Merlino, A.1    Russo, K.I.2    Castellano, I.3    de Vendittis, E.4    Rossi, B.5    Conte, M.6    Vergara, A.7    Sica, F.8
  • 37
    • 66549117516 scopus 로고    scopus 로고
    • Structure and dynamics of cold-adapted enzymes as investigated by FT-IR spectroscopy and MD. The case of an esterase from Pseudoalteromonas haloplanktis
    • Aurilia, V.; Rioux-Dube, J.F.; Marabotti, A.; Pezolet, M.; D'Auria, S. Structure and dynamics of cold-adapted enzymes as investigated by FT-IR spectroscopy and MD. The case of an esterase from Pseudoalteromonas haloplanktis. J. Phys. Chem. B 2009, 113, 7753-7761
    • (2009) J. Phys. Chem. B , vol.113 , pp. 7753-7761
    • Aurilia, V.1    Rioux-Dube, J.F.2    Marabotti, A.3    Pezolet, M.4    D'auria, S.5
  • 38
    • 77953160637 scopus 로고    scopus 로고
    • Near native-state conformational landscape of psychrophilic and mesophilic enzymes: Probing the folding funnel model
    • Mereghetti, P.; Riccardi, L.; Brandsdal, B.O.; Fantucci, P.; de Gioia, L.; Papaleo, E. Near native-state conformational landscape of psychrophilic and mesophilic enzymes: Probing the folding funnel model. J. Phys. Chem. B 2010, 114, 7609-7619
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7609-7619
    • Mereghetti, P.1    Riccardi, L.2    Brandsdal, B.O.3    Fantucci, P.4    de Gioia, L.5    Papaleo, E.6
  • 40
    • 79952455148 scopus 로고    scopus 로고
    • Dynamic properties of extremophilic subtilisin-like serine-proteases
    • Tiberti, M.; Papaleo, E. Dynamic properties of extremophilic subtilisin-like serine-proteases. J. Struct. Biol. 2011, 174, 69-83
    • (2011) J. Struct. Biol , vol.174 , pp. 69-83
    • Tiberti, M.1    Papaleo, E.2
  • 41
    • 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.; Feller, G. Kinetics and energetics of ligand binding determined by microcalorimetry: Insights into active site mobility in a psychrophilic alpha-amylase. J. Mol. Biol. 2006, 358, 1296-1304
    • (2006) J. Mol. Biol , vol.358 , pp. 1296-1304
    • D'amico, S.1    Sohier, J.S.2    Feller, G.3
  • 42
    • 0032528329 scopus 로고    scopus 로고
    • Properties of aspartate transcarbamylase from TAD1, a psychrophilic bacterial strain isolated from Antarctica
    • Sun, K.; Camardella, L.; Di Prisco, G.; Herve, G. Properties of aspartate transcarbamylase from TAD1, a psychrophilic bacterial strain isolated from Antarctica. FEMS Microbiol. Lett. 1998, 164, 375-382
    • (1998) FEMS Microbiol. Lett , vol.164 , pp. 375-382
    • Sun, K.1    Camardella, L.2    Di Prisco, G.3    Herve, G.4
  • 43
    • 0031750455 scopus 로고    scopus 로고
    • Aspartate carbamoyltransferase from a psychrophilic deep-sea bacterium, Vibrio strain 2693: Properties of the enzyme, genetic organization and synthesis in Escherichia coli
    • Xu, Y.; Zhang, Y.; Liang, Z.; van de Casteele, M.; Legrain, C.; Glansdorff, N. Aspartate carbamoyltransferase from a psychrophilic deep-sea bacterium, Vibrio strain 2693: Properties of the enzyme, genetic organization and synthesis in Escherichia coli. Microbiology 1998, 144, 1435-1441
    • (1998) Microbiology , vol.144 , pp. 1435-1441
    • Xu, Y.1    Zhang, Y.2    Liang, Z.3    van de Casteele, M.4    Legrain, C.5    Glansdorff, N.6
  • 45
    • 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. Subtilisin from psychrophilic Antarctic bacteria: Characterization and site-directed mutagenesis of residues possibly involved in the adaptation to cold. Protein Eng. 1997, 10, 1271-1279
    • (1997) Protein Eng , vol.10 , pp. 1271-1279
    • Narinx, E.1    Baise, E.2    Gerday, C.3
  • 46
    • 35548974795 scopus 로고    scopus 로고
    • Activity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments
    • Coquelle, N.; Fioravanti, E.; Weik, M.; Vellieux, F.; Madern, D. Activity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments. J. Mol. Biol. 2007, 374, 547-562
    • (2007) J. Mol. Biol , vol.374 , pp. 547-562
    • Coquelle, N.1    Fioravanti, E.2    Weik, M.3    Vellieux, F.4    Madern, D.5
  • 47
    • 0033946342 scopus 로고    scopus 로고
    • A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures
    • Georlette, D.; Jonsson, Z.O.; van Petegem, F.; Chessa, J.; van Beeumen, J.; Hubscher, U.; Gerday, C. A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures. Eur. J. Biochem. 2000, 267, 3502-3512
    • (2000) Eur. J. Biochem , vol.267 , pp. 3502-3512
    • Georlette, D.1    Jonsson, Z.O.2    van Petegem, F.3    Chessa, J.4    van Beeumen, J.5    Hubscher, U.6    Gerday, C.7
  • 48
    • 0034687760 scopus 로고    scopus 로고
    • Psychrophilic elongation factor Tu from the antarctic Moraxella sp. Tac II 25: Biochemical characterization and cloning of the encoding gene
    • Masullo, M.; Arcari, P.; de Paola, B.; Parmeggiani, A.; Bocchini, V. Psychrophilic elongation factor Tu from the antarctic Moraxella sp. Tac II 25: Biochemical characterization and cloning of the encoding gene. Biochemistry 2000, 39, 15531-15539
    • (2000) Biochemistry , vol.39 , pp. 15531-15539
    • Masullo, M.1    Arcari, P.2    de Paola, B.3    Parmeggiani, A.4    Bocchini, V.5
  • 49
    • 34548304992 scopus 로고    scopus 로고
    • Molecular and functional properties of the psychrophilic elongation factor G from the Antarctic Eubacterium Pseudoalteromonas haloplanktis TAC 125
    • Ruggiero, I.; Raimo, G.; Palma, M.; Arcari, P.; Masullo, M. Molecular and functional properties of the psychrophilic elongation factor G from the Antarctic Eubacterium Pseudoalteromonas haloplanktis TAC 125. Extremophiles 2007, 11, 699-709
    • (2007) Extremophiles , vol.11 , pp. 699-709
    • Ruggiero, I.1    Raimo, G.2    Palma, M.3    Arcari, P.4    Masullo, M.5
  • 50
    • 0034736288 scopus 로고    scopus 로고
    • L-Glutamate dehydrogenase from the antarctic fish Chaenocephalus aceratus. Primary structure, function and thermodynamic characterisation: Relationship with cold adaptation
    • Ciardiello, M.A.; Camardella, L.; Carratore, V.; di Prisco, G. L-Glutamate dehydrogenase from the antarctic fish Chaenocephalus aceratus. Primary structure, function and thermodynamic characterisation: Relationship with cold adaptation. Biochim. Biophys. Acta 2000, 1543, 11-23
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 11-23
    • Ciardiello, M.A.1    Camardella, L.2    Carratore, V.3    di Prisco, G.4
  • 51
    • 0033962829 scopus 로고    scopus 로고
    • NADP+-dependent glutamate dehydrogenase in the Antarctic psychrotolerant bacterium Psychrobacter sp. TAD1. Characterization, protein and DNA sequence, and relationship to other glutamate dehydrogenases
    • Di Fraia, R.; Wilquet, V.; Ciardiello, M.A.; Carratore, V.; Antignani, A.; Camardella, L.; Glansdorff, N.; Di Prisco, G. NADP+-dependent glutamate dehydrogenase in the Antarctic psychrotolerant bacterium Psychrobacter sp. TAD1. Characterization, protein and DNA sequence, and relationship to other glutamate dehydrogenases. Eur. J. Biochem. 2000, 267, 121-131
    • (2000) Eur. J. Biochem , vol.267 , pp. 121-131
    • Di Fraia, R.1    Wilquet, V.2    Ciardiello, M.A.3    Carratore, V.4    Antignani, A.5    Camardella, L.6    Glansdorff, N.7    Di Prisco, G.8
  • 52
    • 0035854688 scopus 로고    scopus 로고
    • Structural determinants of cold adaptation and stability in a large protein
    • D'Amico, S.; Gerday, C.; Feller, G. Structural determinants of cold adaptation and stability in a large protein. J. Biol. Chem. 2001, 276, 25791-25796
    • (2001) J. Biol. Chem , vol.276 , pp. 25791-25796
    • D'amico, S.1    Gerday, C.2    Feller, G.3
  • 53
    • 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. Moritella cold-active dihydrofolate reductase: Are there natural limits to optimization of catalytic efficiency at low temperature? J. Bacteriol. 2003, 185, 5519-5526
    • (2003) J. Bacteriol , vol.185 , pp. 5519-5526
    • Xu, Y.1    Feller, G.2    Gerday, C.3    Glansdorff, N.4
  • 54
    • 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.; Feller, G. Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis. Biochem. J. 2004, 384, 247-253
    • (2004) Biochem. J , vol.384 , pp. 247-253
    • Garsoux, G.1    Lamotte, J.2    Gerday, C.3    Feller, G.4
  • 55
    • 33845602192 scopus 로고    scopus 로고
    • Comparative studies of endonuclease I from cold-adapted Vibrio salmonicida and mesophilic Vibrio cholerae
    • Altermark, B.; Niiranen, L.; Willassen, N.P.; Smalas, A.O.; Moe, E. Comparative studies of endonuclease I from cold-adapted Vibrio salmonicida and mesophilic Vibrio cholerae. FEBS J. 2007, 274, 252-263
    • (2007) FEBS J , vol.274 , pp. 252-263
    • Altermark, B.1    Niiranen, L.2    Willassen, N.P.3    Smalas, A.O.4    Moe, E.5
  • 56
    • 0008298889 scopus 로고    scopus 로고
    • Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties, and molecular modelling
    • Birolo, L.; Tutino, M.L.; Fontanella, B.; Gerday, C.; Mainolfi, K.; Pascarella, S.; Sannia, G.; Vinci, F.; Marino, G. Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125. Cloning, expression, properties, and molecular modelling. Eur. J. Biochem. 2000, 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
  • 57
    • 17644424601 scopus 로고    scopus 로고
    • Elucidation of stability determinants of cold-adapted monomeric isocitrate dehydrogenase from a psychrophilic bacterium, Colwellia maris, by construction of chimeric enzymes
    • Watanabe, S.; Yasutake, Y.; Tanaka, I.; Takada, Y. Elucidation of stability determinants of cold-adapted monomeric isocitrate dehydrogenase from a psychrophilic bacterium, Colwellia maris, by construction of chimeric enzymes. Microbiology 2005, 151, 1083-1094
    • (2005) Microbiology , vol.151 , pp. 1083-1094
    • Watanabe, S.1    Yasutake, Y.2    Tanaka, I.3    Takada, Y.4
  • 58
    • 0037144574 scopus 로고    scopus 로고
    • A novel family 8 xylanase, functional and physicochemical characterization
    • Collins, T.; Meuwis, M.A.; Stals, I.; Claeyssens, M.; Feller, G.; Gerday, C. A novel family 8 xylanase, functional and physicochemical characterization. J. Biol. Chem. 2002, 277, 35133-35139
    • (2002) J. Biol. Chem , vol.277 , pp. 35133-35139
    • Collins, T.1    Meuwis, M.A.2    Stals, I.3    Claeyssens, M.4    Feller, G.5    Gerday, C.6
  • 59
    • 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. Metabolic enzymes from psychrophilic bacteria: Challenge of adaptation to low temperatures in ornithine carbamoyltransferase from Moritella abyssi. J. Bacteriol. 2003, 185, 2161-2168
    • (2003) J. Bacteriol , vol.185 , pp. 2161-2168
    • Xu, Y.1    Feller, G.2    Gerday, C.3    Glansdorff, N.4
  • 60
    • 0030789078 scopus 로고    scopus 로고
    • Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R
    • Gerike, U.; Danson, M.J.; Russell, N.J.; Hough, D.W. Sequencing and expression of the gene encoding a cold-active citrate synthase from an Antarctic bacterium, strain DS2-3R. Eur. J. Biochem. 1997, 248, 49-57
    • (1997) Eur. J. Biochem , vol.248 , pp. 49-57
    • Gerike, U.1    Danson, M.J.2    Russell, N.J.3    Hough, D.W.4
  • 61
    • 43049161350 scopus 로고    scopus 로고
    • Purine nucleoside phosphorylase from Pseudoalteromonas sp. Bsi590: Molecular cloning, gene expression and characterization of the recombinant protein
    • Li, X.; Jiang, X.; Li, H.; Ren, D. Purine nucleoside phosphorylase from Pseudoalteromonas sp. Bsi590: Molecular cloning, gene expression and characterization of the recombinant protein. Extremophiles 2008, 12, 325-333
    • (2008) Extremophiles , vol.12 , pp. 325-333
    • Li, X.1    Jiang, X.2    Li, H.3    Ren, D.4
  • 63
    • 84861093055 scopus 로고    scopus 로고
    • Fluorescence studies on the stability, flexibility and substrate-induced conformational changes of acetate kinases from psychrophilic and mesophilic bacteria
    • Tang, M.A.; Motoshima, H.; Watanabe, K. Fluorescence studies on the stability, flexibility and substrate-induced conformational changes of acetate kinases from psychrophilic and mesophilic bacteria. Protein J. 2012, 31, 337-344
    • (2012) Protein J , vol.31 , pp. 337-344
    • Tang, M.A.1    Motoshima, H.2    Watanabe, K.3
  • 64
    • 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.; Feller, G. Temperature adaptation of proteins: Engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase. J. Mol. Biol. 2003, 332, 981-988
    • (2003) J. Mol. Biol , vol.332 , pp. 981-988
    • D'amico, S.1    Gerday, C.2    Feller, G.3
  • 65
    • 80055096639 scopus 로고    scopus 로고
    • Stepwise adaptations to low temperature as revealed by multiple mutants of psychrophilic alpha-amylase from Antarctic Bacterium
    • Cipolla, A.; D'Amico, S.; Barumandzadeh, R.; Matagne, A.; Feller, G. Stepwise adaptations to low temperature as revealed by multiple mutants of psychrophilic alpha-amylase from Antarctic Bacterium. J. Biol. Chem. 2011, 286, 38348-38355
    • (2011) J. Biol. Chem , vol.286 , pp. 38348-38355
    • Cipolla, A.1    D'amico, S.2    Barumandzadeh, R.3    Matagne, A.4    Feller, G.5
  • 66
    • 33746887076 scopus 로고    scopus 로고
    • Microscopic rate-constants for substrate binding and acylation in cold-adaptation of trypsin I from Atlantic cod
    • Asgeirsson, B.; Cekan, P. Microscopic rate-constants for substrate binding and acylation in cold-adaptation of trypsin I from Atlantic cod. FEBS Lett. 2006, 580, 4639-4644
    • (2006) FEBS Lett , vol.580 , pp. 4639-4644
    • Asgeirsson, B.1    Cekan, P.2
  • 67
    • 0034736285 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Revisiting the thermodynamic parameters of activation may explain local flexibility
    • Lonhienne, T.; Gerday, C.; Feller, G. Psychrophilic enzymes: Revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta 2000, 1543, 1-10
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 1-10
    • Lonhienne, T.1    Gerday, C.2    Feller, G.3
  • 68
    • 52249116531 scopus 로고    scopus 로고
    • Cold adaptation of enzyme reaction rates
    • Bjelic, S.; Brandsdal, B.O.; Aqvist, J. Cold adaptation of enzyme reaction rates. Biochemistry 2008, 47, 10049-10057
    • (2008) Biochemistry , vol.47 , pp. 10049-10057
    • Bjelic, S.1    Brandsdal, B.O.2    Aqvist, J.3
  • 70
    • 0034170458 scopus 로고    scopus 로고
    • Toward a molecular understanding of cold activity of enzymes from psychrophiles
    • Russell, N.J. Toward a molecular understanding of cold activity of enzymes from psychrophiles. Extremophiles 2000, 4, 83-90
    • (2000) Extremophiles , vol.4 , pp. 83-90
    • Russell, N.J.1
  • 71
    • 0036568335 scopus 로고    scopus 로고
    • Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes
    • Gianese, G.; Bossa, F.; Pascarella, S. Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes. Proteins 2002, 47, 236-249
    • (2002) Proteins , vol.47 , pp. 236-249
    • Gianese, G.1    Bossa, F.2    Pascarella, S.3
  • 72
    • 34548383957 scopus 로고    scopus 로고
    • Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: Insights from the quasi-chemical approximation
    • Goldstein, R.A. Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: Insights from the quasi-chemical approximation. Protein Sci. 2007, 16, 1887-1895
    • (2007) Protein Sci , vol.16 , pp. 1887-1895
    • Goldstein, R.A.1
  • 73
    • 1242284208 scopus 로고    scopus 로고
    • Cold-active esterase from Psychrobacter sp. Ant300: Gene cloning, characterization, and the effects of Gly→Pro substitution near the active site on its catalytic activity and stability
    • Kulakova, L.; Galkin, A.; Nakayama, T.; Nishino, T.; Esaki, N. Cold-active esterase from Psychrobacter sp. Ant300: Gene cloning, characterization, and the effects of Gly→Pro substitution near the active site on its catalytic activity and stability. Biochim. Biophys. Acta 2004, 1696, 59-65
    • (2004) Biochim. Biophys. Acta , vol.1696 , pp. 59-65
    • Kulakova, L.1    Galkin, A.2    Nakayama, T.3    Nishino, T.4    Esaki, N.5
  • 74
    • 0036093866 scopus 로고    scopus 로고
    • Exploring the role of a glycine cluster in cold adaptation of an alkaline phosphatase
    • Mavromatis, K.; Tsigos, I.; Tzanodaskalaki, M.; Kokkinidis, M.; Bouriotis, V. Exploring the role of a glycine cluster in cold adaptation of an alkaline phosphatase. Eur. J. Biochem. 2002, 269, 2330-2335
    • (2002) Eur. J. Biochem , vol.269 , pp. 2330-2335
    • Mavromatis, K.1    Tsigos, I.2    Tzanodaskalaki, M.3    Kokkinidis, M.4    Bouriotis, V.5
  • 76
    • 80054703699 scopus 로고    scopus 로고
    • Comparative void-volume analysis of psychrophilic and mesophilic enzymes: Structural bioinformatics of psychrophilic enzymes reveals sources of core flexibility
    • Paredes, D.I.; Watters, K.; Pitman, D.J.; Bystroff, C.; Dordick, J.S. Comparative void-volume analysis of psychrophilic and mesophilic enzymes: Structural bioinformatics of psychrophilic enzymes reveals sources of core flexibility. BMC Struct. Biol. 2011, 11, 42
    • (2011) BMC Struct. Biol , vol.11 , pp. 42
    • Paredes, D.I.1    Watters, K.2    Pitman, D.J.3    Bystroff, C.4    Dordick, J.S.5
  • 77
    • 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. Thermodynamic stability of a cold-active α-amylase from the Antarctic bacterium Alteromonas haloplanctis. Biochemistry 1999, 38, 4613-4619
    • (1999) Biochemistry , vol.38 , pp. 4613-4619
    • Feller, G.1    D'amico, D.2    Gerday, C.3
  • 78
    • 13244249836 scopus 로고
    • The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
    • Yip, K.S.; Stillman, T.J.; Britton, K.L.; Artymiuk, P.J.; Baker, P.J.; Sedelnikova, S.E.; Engel, P.C.; Pasquo, A.; Chiaraluce, R.; Consalvi, V. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure 1995, 3, 1147-1158
    • (1995) Structure , vol.3 , pp. 1147-1158
    • Yip, K.S.1    Stillman, T.J.2    Britton, K.L.3    Artymiuk, P.J.4    Baker, P.J.5    Sedelnikova, S.E.6    Engel, P.C.7    Pasquo, A.8    Chiaraluce, R.9    Consalvi, V.10
  • 80
    • 80055076603 scopus 로고    scopus 로고
    • Molecular determinants of enzyme cold adaptation: Comparative structural and computational studies of cold- and warm-adapted enzymes
    • Papaleo, E.; Tiberti, M.; Invernizzi, G.; Pasi, M.; Ranzani, V. Molecular determinants of enzyme cold adaptation: Comparative structural and computational studies of cold- and warm-adapted enzymes. Curr. Protein Pept. Sci. 2011, 12, 657-683
    • (2011) Curr. Protein Pept. Sci , vol.12 , pp. 657-683
    • Papaleo, E.1    Tiberti, M.2    Invernizzi, G.3    Pasi, M.4    Ranzani, V.5
  • 81
    • 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.; Taylor, G.L. Stepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophile. Eur. J. Biochem. 2002, 269, 6250-6260
    • (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
  • 82
    • 3142653228 scopus 로고    scopus 로고
    • Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases
    • Bae, E.; Phillips, G.N., Jr. Structures and analysis of highly homologous psychrophilic, mesophilic, and thermophilic adenylate kinases. J. Biol. Chem. 2004, 279, 28202-28208
    • (2004) J. Biol. Chem , vol.279 , pp. 28202-28208
    • Bae, E.1    Phillips Jr., G.N.2
  • 84
    • 34548147289 scopus 로고    scopus 로고
    • Structural adaptation to low temperatures-analysis of the subunit interface of oligomeric psychrophilic enzymes
    • Tronelli, D.; Maugini, E.; Bossa, F.; Pascarella, S. Structural adaptation to low temperatures-analysis of the subunit interface of oligomeric psychrophilic enzymes. FEBS J. 2007, 274, 4595-4608
    • (2007) FEBS J , vol.274 , pp. 4595-4608
    • Tronelli, D.1    Maugini, E.2    Bossa, F.3    Pascarella, S.4
  • 85
    • 84863275738 scopus 로고    scopus 로고
    • Crystal structure of hyperthermophilic endo-beta-1,4-glucanase: Implications for catalytic mechanism and thermostability
    • Zheng, B.; Yang, W.; Zhao, X.; Wang, Y.; Lou, Z.; Rao, Z.; Feng, Y. Crystal structure of hyperthermophilic endo-beta-1,4-glucanase: Implications for catalytic mechanism and thermostability. J. Biol. Chem. 2012, 287, 8336-8346
    • (2012) J. Biol. Chem , vol.287 , pp. 8336-8346
    • Zheng, B.1    Yang, W.2    Zhao, X.3    Wang, Y.4    Lou, Z.5    Rao, Z.6    Feng, Y.7
  • 86
    • 36448995059 scopus 로고    scopus 로고
    • Adaptation of model proteins from cold to hot environments involves continuous and small adjustments of average parameters related to amino acid composition
    • De Vendittis, E.; Castellano, I.; Cotugno, R.; Ruocco, M.R.; Raimo, G.; Masullo, M. Adaptation of model proteins from cold to hot environments involves continuous and small adjustments of average parameters related to amino acid composition. J. Theor. Biol. 2008, 250, 156-171
    • (2008) J. Theor. Biol , vol.250 , pp. 156-171
    • de Vendittis, E.1    Castellano, I.2    Cotugno, R.3    Ruocco, M.R.4    Raimo, G.5    Masullo, M.6
  • 87
    • 34347361558 scopus 로고    scopus 로고
    • Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins
    • Saelensminde, G.; Halskau, O., Jr.; Helland, R.; Willassen, N.P.; Jonassen, I. Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins. Extremophiles 2007, 11, 585-596
    • (2007) Extremophiles , vol.11 , pp. 585-596
    • Saelensminde, G.1    Halskau Jr., O.2    Helland, R.3    Willassen, N.P.4    Jonassen, I.5
  • 88
    • 0038824870 scopus 로고    scopus 로고
    • Mechanisms of thermal adaptation revealed from the genomes of the Antarctic Archaea Methanogenium frigidum and Methanococcoides burtonii
    • Saunders, N.F.; Thomas, T.; Curmi, P.M.; Mattick, J.S.; Kuczek, E.; Slade, R.; Davis, J.; Franzmann, P.D.; Boone, D.; Rusterholtz, K.; et al. Mechanisms of thermal adaptation revealed from the genomes of the Antarctic Archaea Methanogenium frigidum and Methanococcoides burtonii. Genome Res. 2003, 13, 1580-1588
    • (2003) Genome Res , vol.13 , pp. 1580-1588
    • Saunders, N.F.1    Thomas, T.2    Curmi, P.M.3    Mattick, J.S.4    Kuczek, E.5    Slade, R.6    Davis, J.7    Franzmann, P.D.8    Boone, D.9    Rusterholtz, K.10
  • 90
    • 62349120035 scopus 로고    scopus 로고
    • Comparative proteome analysis of psychrophilic versus mesophilic bacterial species: Insights into the molecular basis of cold adaptation of proteins
    • doi:10.1186/1471-2164-10-11
    • Metpally, R.P.; Reddy, B.V. Comparative proteome analysis of psychrophilic versus mesophilic bacterial species: Insights into the molecular basis of cold adaptation of proteins. BMC Genomics 2009, 10, doi:10.1186/1471-2164-10-11
    • (2009) BMC Genomics , pp. 10
    • Metpally, R.P.1    Reddy, B.V.2
  • 91
    • 0031608378 scopus 로고    scopus 로고
    • Molecular adaptations in psychrophilic bacteria: Potential for biotechnological applications
    • Russell, N.J. Molecular adaptations in psychrophilic bacteria: Potential for biotechnological applications. Adv. Biochem. Eng. Biotechnol. 1998, 61, 1-21
    • (1998) Adv. Biochem. Eng. Biotechnol , vol.61 , pp. 1-21
    • Russell, N.J.1
  • 98
    • 84878074250 scopus 로고    scopus 로고
    • Bioprospecting Information Resource, United Nations University: Tokyo, Japan. Available online, accessed on 14 September
    • Bioprospecting Information Resource, United Nations University: Tokyo, Japan. Available online: http://www.bioprospector.org/bioprospector/ (accessed on 14 September 2012).
    • (2012)
  • 99
    • 0021715356 scopus 로고
    • Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5' end labelling of nucleic acids
    • Kobori, H.; Sullivan, C.W.; Shizuya, H. Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5' end labelling of nucleic acids. Proc. Natl. Acad. Sci. USA 1984, 81, 6691-6695
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6691-6695
    • Kobori, H.1    Sullivan, C.W.2    Shizuya, H.3
  • 103
    • 46849092215 scopus 로고    scopus 로고
    • Cold active microbial lipases: Some hot issues and recent developments
    • Babu, J.; Ramteke, P.W.; Thomas, G. Cold active microbial lipases: Some hot issues and recent developments. Biotechnol. Adv. 2008, 26, 457-470
    • (2008) Biotechnol. Adv , vol.26 , pp. 457-470
    • Babu, J.1    Ramteke, P.W.2    Thomas, G.3
  • 105
    • 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. Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the Antarctic psychrophile Bacillus TA41. J. Biol. Chem. 1994, 269, 17448-17453
    • (1994) J. Biol. Chem , vol.269 , pp. 17448-17453
    • Davail, S.1    Feller, G.2    Narinx, E.3    Gerday, C.4
  • 106
    • 0037470085 scopus 로고    scopus 로고
    • The structure of a cold-adapted family 8 xylanase at 1.3 Å resolution. Structural adaptations to cold and investigation of the active site
    • Van Petegem, F.; Collins, T.; Meuwis, M.A.; Gerday, C.; Feller, G.; Van Beeumen, J. The structure of a cold-adapted family 8 xylanase at 1.3 Å resolution. Structural adaptations to cold and investigation of the active site. J. Biol. Chem. 2003, 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
  • 108
    • 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.; Van Beeumen, J. 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 2006, 45, 4797-4807
    • (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
  • 111
    • 0033779402 scopus 로고    scopus 로고
    • Temperature adaptation of enzymes: Lessons from laboratory evolution
    • Wintrode, P.L.; Arnold, F.H. Temperature adaptation of enzymes: Lessons from laboratory evolution. Adv. Protein Chem. 2000, 55, 161-225
    • (2000) Adv. Protein Chem , vol.55 , pp. 161-225
    • Wintrode, P.L.1    Arnold, F.H.2
  • 112
    • 29244491455 scopus 로고    scopus 로고
    • Improved thermal stability and activity in the cold-adapted lipase B from Candida antarctica following chemical modification with oxidized polysaccharides
    • Siddiqui, K.S.; Cavicchioli, R. Improved thermal stability and activity in the cold-adapted lipase B from Candida antarctica following chemical modification with oxidized polysaccharides. Extremophiles 2005, 9, 471-476
    • (2005) Extremophiles , vol.9 , pp. 471-476
    • Siddiqui, K.S.1    Cavicchioli, R.2
  • 114
    • 16644372513 scopus 로고    scopus 로고
    • Improved activity and stability of alkaline phosphatases from psychrophilic and mesophilic organisms by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives
    • Siddiqui, K.S.; Poljak, A.; Cavicchioli, R. Improved activity and stability of alkaline phosphatases from psychrophilic and mesophilic organisms by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives. Cell. Mol. Biol. 2004, 50, 657-667.
    • (2004) Cell. Mol. Biol , vol.50 , pp. 657-667
    • Siddiqui, K.S.1    Poljak, A.2    Cavicchioli, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.