메뉴 건너뛰기




Volumn 372, Issue 1, 2007, Pages 130-149

Structural and Functional Properties of Isocitrate Dehydrogenase from the Psychrophilic Bacterium Desulfotalea psychrophila Reveal a Cold-active Enzyme with an Unusual High Thermal Stability

Author keywords

cold adaptation; crystal structure; isocitrate dehydrogenase; psychrophilic; thermal stability

Indexed keywords

ENZYME; ISOCITRATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 34547680284     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.06.040     Document Type: Article
Times cited : (68)

References (85)
  • 1
  • 3
    • 0025032116 scopus 로고
    • Regulation of an enzyme by phosphorylation at the active site
    • Hurley J.H., Dean A.M., Sohl J.L., Koshl Jr. D.E., and Stroud R.M. Regulation of an enzyme by phosphorylation at the active site. Science 249 (1990) 1012-1016
    • (1990) Science , vol.249 , pp. 1012-1016
    • Hurley, J.H.1    Dean, A.M.2    Sohl, J.L.3    Koshl Jr., D.E.4    Stroud, R.M.5
  • 6
    • 0031734969 scopus 로고    scopus 로고
    • New results using Laue diffraction and time-resolved crystallography
    • Stoddard B.L. New results using Laue diffraction and time-resolved crystallography. Curr. Opin. Struct. Biol. 8 (1998) 612-618
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 612-618
    • Stoddard, B.L.1
  • 7
    • 0035854744 scopus 로고    scopus 로고
    • Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 Å. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase
    • Singh S.K., Matsuno K., LaPorte D.C., and Banaszak L.J. Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 Å. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase. J. Biol. Chem. 276 (2001) 26154-26163
    • (2001) J. Biol. Chem. , vol.276 , pp. 26154-26163
    • Singh, S.K.1    Matsuno, K.2    LaPorte, D.C.3    Banaszak, L.J.4
  • 9
    • 4043105583 scopus 로고    scopus 로고
    • Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity
    • Xu X., Zhao J., Xu Z., Peng B., Huang Q., Arnold E., and Ding J. Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity. J. Biol. Chem. 279 (2004) 33946-33957
    • (2004) J. Biol. Chem. , vol.279 , pp. 33946-33957
    • Xu, X.1    Zhao, J.2    Xu, Z.3    Peng, B.4    Huang, Q.5    Arnold, E.6    Ding, J.7
  • 10
    • 9644291516 scopus 로고    scopus 로고
    • Isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix: X-ray structure analysis of a ternary enzyme-substrate complex and thermal stability
    • Karlström M., Stokke R., Steen I.H., Birkeland N.K., and Ladenstein R. Isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix: X-ray structure analysis of a ternary enzyme-substrate complex and thermal stability. J. Mol. Biol. 345 (2005) 559-577
    • (2005) J. Mol. Biol. , vol.345 , pp. 559-577
    • Karlström, M.1    Stokke, R.2    Steen, I.H.3    Birkeland, N.K.4    Ladenstein, R.5
  • 11
    • 34248334562 scopus 로고    scopus 로고
    • Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers
    • Stokke R., Karlstrom M., Yang N., Leiros I., Ladenstein R., Birkeland N.K., and Steen I.H. Thermal stability of isocitrate dehydrogenase from Archaeoglobus fulgidus studied by crystal structure analysis and engineering of chimers. Extremophiles 11 (2007) 481-493
    • (2007) Extremophiles , vol.11 , pp. 481-493
    • Stokke, R.1    Karlstrom, M.2    Yang, N.3    Leiros, I.4    Ladenstein, R.5    Birkeland, N.K.6    Steen, I.H.7
  • 12
    • 33745191883 scopus 로고    scopus 로고
    • The crystal structure of a hyperthermostable subfamily II isocitrate dehydrogenase from Thermotoga maritima
    • Karlström M., Steen I.H., Madern D., Fedøy A.E., Birkeland N.K., and Ladenstein R. The crystal structure of a hyperthermostable subfamily II isocitrate dehydrogenase from Thermotoga maritima. FEBS J. 273 (2006) 2851-2868
    • (2006) FEBS J. , vol.273 , pp. 2851-2868
    • Karlström, M.1    Steen, I.H.2    Madern, D.3    Fedøy, A.E.4    Birkeland, N.K.5    Ladenstein, R.6
  • 13
    • 0035941275 scopus 로고    scopus 로고
    • Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation
    • Steen I.H., Madern D., Karlström M., Lien T., Ladenstein R., and Birkeland N.K. Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation. J. Biol. Chem. 276 (2001) 43924-43931
    • (2001) J. Biol. Chem. , vol.276 , pp. 43924-43931
    • Steen, I.H.1    Madern, D.2    Karlström, M.3    Lien, T.4    Ladenstein, R.5    Birkeland, N.K.6
  • 14
    • 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. Ion pairs and the thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads. Trends Biochem. Sci. 26 (2001) 550-556
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2
  • 15
    • 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., et al. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure 3 (1995) 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
  • 16
    • 0030681366 scopus 로고    scopus 로고
    • Psychrophilic enzymes: molecular basis of cold adaptation
    • Feller G., and Gerday C. Psychrophilic enzymes: molecular basis of cold adaptation. Cell Mol. Life. Sci. 53 (1997) 830-841
    • (1997) Cell Mol. Life. Sci. , vol.53 , pp. 830-841
    • Feller, G.1    Gerday, C.2
  • 17
    • 0037688133 scopus 로고    scopus 로고
    • Molecular adaptations to cold in psychrophilic enzymes
    • Feller G. Molecular adaptations to cold in psychrophilic enzymes. Cell Mol. Life. Sci. 60 (2003) 648-662
    • (2003) Cell Mol. Life. Sci. , vol.60 , pp. 648-662
    • Feller, G.1
  • 19
    • 33847311388 scopus 로고    scopus 로고
    • Life at low temperatures: is disorder the driving force?
    • Feller G. Life at low temperatures: is disorder the driving force?. Extremophiles 11 (2007) 211-216
    • (2007) Extremophiles , vol.11 , pp. 211-216
    • Feller, G.1
  • 22
    • 0036568335 scopus 로고    scopus 로고
    • Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes
    • Gianese G., Bossa F., and Pascarella S. Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes. Proteins: Struct. Funct. Genet. 47 (2002) 236-249
    • (2002) Proteins: Struct. Funct. Genet. , vol.47 , pp. 236-249
    • Gianese, G.1    Bossa, F.2    Pascarella, S.3
  • 24
    • 0034736285 scopus 로고    scopus 로고
    • Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility
    • Lonhienne T., Gerday C., and Feller G. Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta 1543 (2000) 1-10
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 1-10
    • Lonhienne, T.1    Gerday, C.2    Feller, G.3
  • 25
    • 0027508357 scopus 로고
    • Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic bacterium, Vibrio sp. strain ABE-1
    • Ishii A., Suzuki M., Sahara T., Takada Y., Sasaki S., and Fukunaga N. Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic bacterium, Vibrio sp. strain ABE-1. J. Bacteriol. 175 (1993) 6873-6880
    • (1993) J. Bacteriol. , vol.175 , pp. 6873-6880
    • Ishii, A.1    Suzuki, M.2    Sahara, T.3    Takada, Y.4    Sasaki, S.5    Fukunaga, N.6
  • 26
    • 33745697891 scopus 로고    scopus 로고
    • Two isocitrate dehydrogenases from a psychrophilic bacterium, Colwellia psychrerythraea
    • Maki S., Yoneta M., and Takada Y. Two isocitrate dehydrogenases from a psychrophilic bacterium, Colwellia psychrerythraea. Extremophiles 10 (2006) 237-249
    • (2006) Extremophiles , vol.10 , pp. 237-249
    • Maki, S.1    Yoneta, M.2    Takada, Y.3
  • 27
    • 0028923124 scopus 로고
    • Differential expression in Escherichia coli of the Vibrio sp. strain ABE-1 icdI and icdII genes encoding structurally different isocitrate dehydrogenase isozymes
    • Suzuki M., Sahara T., Tsuruha J., Takada Y., and Fukunaga N. Differential expression in Escherichia coli of the Vibrio sp. strain ABE-1 icdI and icdII genes encoding structurally different isocitrate dehydrogenase isozymes. J. Bacteriol. 177 (1995) 2138-2142
    • (1995) J. Bacteriol. , vol.177 , pp. 2138-2142
    • Suzuki, M.1    Sahara, T.2    Tsuruha, J.3    Takada, Y.4    Fukunaga, N.5
  • 28
    • 33645019246 scopus 로고    scopus 로고
    • Substrate-free structure of a monomeric NADP isocitrate dehydrogenase: an open conformation phylogenetic relationship of isocitrate dehydrogenase
    • Imabayashi F., Aich S., Prasad L., and Delbaere L.T. Substrate-free structure of a monomeric NADP isocitrate dehydrogenase: an open conformation phylogenetic relationship of isocitrate dehydrogenase. Proteins: Struct. Funct. Genet. 63 (2006) 100-112
    • (2006) Proteins: Struct. Funct. Genet. , vol.63 , pp. 100-112
    • Imabayashi, F.1    Aich, S.2    Prasad, L.3    Delbaere, L.T.4
  • 30
    • 4344713183 scopus 로고    scopus 로고
    • The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments
    • Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., et al. The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments. Environ. Microbiol. 6 (2004) 887-902
    • (2004) Environ. Microbiol. , vol.6 , pp. 887-902
    • Rabus, R.1    Ruepp, A.2    Frickey, T.3    Rattei, T.4    Fartmann, B.5    Stark, M.6
  • 31
    • 0037129928 scopus 로고    scopus 로고
    • L-Phenylalanine binding and domain organization in human phenylalanine hydroxylase: a differential scanning calorimetry study
    • Thórólfsson M., Ibarra-Molero B., Fojan P., Petersen S.B., Sanchez-Ruiz J.M., and Martinez A. L-Phenylalanine binding and domain organization in human phenylalanine hydroxylase: a differential scanning calorimetry study. Biochemistry 41 (2002) 7573-7585
    • (2002) Biochemistry , vol.41 , pp. 7573-7585
    • Thórólfsson, M.1    Ibarra-Molero, B.2    Fojan, P.3    Petersen, S.B.4    Sanchez-Ruiz, J.M.5    Martinez, A.6
  • 32
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • Sanchez-Ruiz J.M. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61 (1992) 921-935
    • (1992) Biophys. J. , vol.61 , pp. 921-935
    • Sanchez-Ruiz, J.M.1
  • 33
    • 0036432690 scopus 로고    scopus 로고
    • Thermostable aldehyde dehydrogenase from psychrophile, Cytophaga sp. KUC-1: enzymological characteristics and functional properties
    • Yamanaka Y., Kazuoka T., Yoshida M., Yamanaka K., Oikawa T., and Soda K. Thermostable aldehyde dehydrogenase from psychrophile, Cytophaga sp. KUC-1: enzymological characteristics and functional properties. Biochem. Biophys. Res. Commun. 298 (2002) 632-637
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 632-637
    • Yamanaka, Y.1    Kazuoka, T.2    Yoshida, M.3    Yamanaka, K.4    Oikawa, T.5    Soda, K.6
  • 34
    • 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., and Zavodszky P. A better enzyme to cope with cold. Comparative flexibility studies on psychrotrophic, mesophilic, and thermophilic IPMDHs. J. Biol. Chem. 276 (2001) 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
  • 35
    • 0037281464 scopus 로고    scopus 로고
    • Thermostable aspartase from a marine psychrophile, Cytophaga sp. KUC-1: molecular characterization and primary structure
    • Kazuoka T., Masuda Y., Oikawa T., and Soda K. Thermostable aspartase from a marine psychrophile, Cytophaga sp. KUC-1: molecular characterization and primary structure. J. Biochem. (Tokyo) 133 (2003) 51-58
    • (2003) J. Biochem. (Tokyo) , vol.133 , pp. 51-58
    • Kazuoka, T.1    Masuda, Y.2    Oikawa, T.3    Soda, K.4
  • 36
    • 33847302462 scopus 로고    scopus 로고
    • A cold-active and thermostable alcohol dehydrogenase of a psychrotorelant from Antarctic seawater, Flavobacterium frigidimaris KUC-1
    • Kazuoka T., Oikawa T., Muraoka I., Kuroda S., and Soda K. A cold-active and thermostable alcohol dehydrogenase of a psychrotorelant from Antarctic seawater, Flavobacterium frigidimaris KUC-1. Extremophiles 11 (2007) 257-267
    • (2007) Extremophiles , vol.11 , pp. 257-267
    • Kazuoka, T.1    Oikawa, T.2    Muraoka, I.3    Kuroda, S.4    Soda, K.5
  • 38
    • 0032705302 scopus 로고    scopus 로고
    • Psychrophilic sulfate-reducing bacteria isolated from permanently cold arctic marine sediments: description of Desulfofrigus oceanense gen. nov., sp. nov., Desulfofrigus fragile sp. nov., Desulfofaba gelida gen. nov., sp. nov., Desulfotalea psychrophila gen. nov., sp. nov. and Desulfotalea arctica sp. nov
    • Knoblauch C., Sahm K., and Jørgensen B.B. Psychrophilic sulfate-reducing bacteria isolated from permanently cold arctic marine sediments: description of Desulfofrigus oceanense gen. nov., sp. nov., Desulfofrigus fragile sp. nov., Desulfofaba gelida gen. nov., sp. nov., Desulfotalea psychrophila gen. nov., sp. nov. and Desulfotalea arctica sp. nov. Int. J. Syst. Bacteriol. 49 (1999) 1631-1643
    • (1999) Int. J. Syst. Bacteriol. , vol.49 , pp. 1631-1643
    • Knoblauch, C.1    Sahm, K.2    Jørgensen, B.B.3
  • 39
    • 0029931803 scopus 로고    scopus 로고
    • Desulfitobacterium hafniense sp. nov., an anaerobic, reductively dechlorinating bacterium
    • Christiansen N., and Ahring B.K. Desulfitobacterium hafniense sp. nov., an anaerobic, reductively dechlorinating bacterium. Int. J. Syst. Bacteriol. 46 (1996) 442-448
    • (1996) Int. J. Syst. Bacteriol. , vol.46 , pp. 442-448
    • Christiansen, N.1    Ahring, B.K.2
  • 40
    • 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., and Takada Y. Elucidation of stability determinants of cold-adapted monomeric isocitrate dehydrogenase from a psychrophilic bacterium, Colwellia maris, by construction of chimeric enzymes. Microbiology 151 (2005) 1083-1094
    • (2005) Microbiology , vol.151 , pp. 1083-1094
    • Watanabe, S.1    Yasutake, Y.2    Tanaka, I.3    Takada, Y.4
  • 41
    • 0035108129 scopus 로고    scopus 로고
    • Effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens
    • Thomas T., Kumar N., and Cavicchioli R. Effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens. J. Bacteriol. 183 (2001) 1974-1982
    • (2001) J. Bacteriol. , vol.183 , pp. 1974-1982
    • Thomas, T.1    Kumar, N.2    Cavicchioli, R.3
  • 42
    • 0035830748 scopus 로고    scopus 로고
    • Enzyme activity determination on macromolecular substrates by isothermal titration calorimetry: application to mesophilic and psychrophilic chitinases
    • Lonhienne T., Baise E., Feller G., Bouriotis V., and Gerday C. Enzyme activity determination on macromolecular substrates by isothermal titration calorimetry: application to mesophilic and psychrophilic chitinases. Biochim. Biophys. Acta 1545 (2001) 349-356
    • (2001) Biochim. Biophys. Acta , vol.1545 , pp. 349-356
    • Lonhienne, T.1    Baise, E.2    Feller, G.3    Bouriotis, V.4    Gerday, C.5
  • 43
    • 24044551623 scopus 로고    scopus 로고
    • Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase
    • Huang Y.C., and Colman R.F. Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase. J. Biol. Chem. 280 (2005) 30349-30353
    • (2005) J. Biol. Chem. , vol.280 , pp. 30349-30353
    • Huang, Y.C.1    Colman, R.F.2
  • 44
    • 0032530086 scopus 로고    scopus 로고
    • Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes
    • Fields P.A., and Somero G.N. Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes. Proc. Natl Acad. Sci. USA 95 (1998) 11476-11481
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11476-11481
    • Fields, P.A.1    Somero, G.N.2
  • 45
    • 0034050890 scopus 로고    scopus 로고
    • Identification by mutagenesis of arginines in the substrate binding site of the porcine NADP-dependent isocitrate dehydrogenase
    • Soundar S., Danek B.L., and Colman R.F. Identification by mutagenesis of arginines in the substrate binding site of the porcine NADP-dependent isocitrate dehydrogenase. J. Biol. Chem. 275 (2000) 5606-5612
    • (2000) J. Biol. Chem. , vol.275 , pp. 5606-5612
    • Soundar, S.1    Danek, B.L.2    Colman, R.F.3
  • 46
    • 0037197684 scopus 로고    scopus 로고
    • Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart NADP-dependent isocitrate dehydrogenase
    • Huang Y.C., and Colman R.F. Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart NADP-dependent isocitrate dehydrogenase. Biochemistry 41 (2002) 5637-5643
    • (2002) Biochemistry , vol.41 , pp. 5637-5643
    • Huang, Y.C.1    Colman, R.F.2
  • 47
    • 0036578481 scopus 로고    scopus 로고
    • Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial NADP-dependent isocitrate dehydrogenase
    • Lee P., and Colman R.F. Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial NADP-dependent isocitrate dehydrogenase. Arch. Biochem. Biophys. 401 (2002) 81-90
    • (2002) Arch. Biochem. Biophys. , vol.401 , pp. 81-90
    • Lee, P.1    Colman, R.F.2
  • 48
    • 33744934213 scopus 로고    scopus 로고
    • Thr(373), Asp(375), and Lys(260) are in the coenzyme site of porcine NADP-dependent isocitrate dehydrogenase
    • Lee P., and Colman R.F. Thr(373), Asp(375), and Lys(260) are in the coenzyme site of porcine NADP-dependent isocitrate dehydrogenase. Arch. Biochem. Biophys. 450 (2006) 183-190
    • (2006) Arch. Biochem. Biophys. , vol.450 , pp. 183-190
    • Lee, P.1    Colman, R.F.2
  • 50
    • 0027383273 scopus 로고
    • Kinetic mechanism of Escherichia coli isocitrate dehydrogenase
    • Dean A.M., and Koshl Jr. D.E. Kinetic mechanism of Escherichia coli isocitrate dehydrogenase. Biochemistry 32 (1993) 9302-9309
    • (1993) Biochemistry , vol.32 , pp. 9302-9309
    • Dean, A.M.1    Koshl Jr., D.E.2
  • 51
    • 1542297722 scopus 로고    scopus 로고
    • 2+ bound to porcine mitochondrial NADP-dependent isocitrate dehydrogenase, as assessed by mutagenesis
    • 2+ bound to porcine mitochondrial NADP-dependent isocitrate dehydrogenase, as assessed by mutagenesis. Biochemistry 43 (2004) 2821-2828
    • (2004) Biochemistry , vol.43 , pp. 2821-2828
    • Huang, Y.C.1    Grodsky, N.B.2    Kim, T.K.3    Colman, R.F.4
  • 53
    • 1542361158 scopus 로고    scopus 로고
    • Critical role of Lys212 and Tyr140 in porcine NADP-dependent isocitrate dehydrogenase
    • Kim T.K., Lee P., and Colman R.F. Critical role of Lys212 and Tyr140 in porcine NADP-dependent isocitrate dehydrogenase. J. Biol. Chem. 278 (2003) 49323-49331
    • (2003) J. Biol. Chem. , vol.278 , pp. 49323-49331
    • Kim, T.K.1    Lee, P.2    Colman, R.F.3
  • 54
    • 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 M.M., and Ficner R. Crystal structure of a subtilisin-like serine proteinase from a psychrotrophic Vibrio species reveals structural aspects of cold adaptation. FEBS J 272 (2005) 832-845
    • (2005) FEBS J , vol.272 , pp. 832-845
    • Arnorsdottir, J.1    Kristjansson, M.M.2    Ficner, R.3
  • 55
    • 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., and Gerday C. Cold adaptation of proteins. Purification, characterization, and sequence of the heat-labile subtilisin from the antarctic psychrophile Bacillus TA41. J. Biol. Chem. 269 (1994) 17448-17453
    • (1994) J. Biol. Chem. , vol.269 , pp. 17448-17453
    • Davail, S.1    Feller, G.2    Narinx, E.3    Gerday, C.4
  • 56
    • 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. Kinetic and structural optimization to catalysis at low temperatures in a psychrophilic cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis. Biochem. J. 384 (2004) 247-253
    • (2004) Biochem. J. , vol.384 , pp. 247-253
    • Garsoux, G.1    Lamotte, J.2    Gerday, C.3    Feller, G.4
  • 57
    • 0005492283 scopus 로고    scopus 로고
    • Structural comparison of psychrophilic and mesophilic trypsins. Elucidating the molecular basis of cold-adaptation
    • Leiros H.K., Willassen N.P., and Smalås A.O. Structural comparison of psychrophilic and mesophilic trypsins. Elucidating the molecular basis of cold-adaptation. Eur. J. Biochem. 267 (2000) 1039-1049
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1039-1049
    • Leiros, H.K.1    Willassen, N.P.2    Smalås, A.O.3
  • 58
    • 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. Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium. Structure 6 (1998) 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
    • 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., et al. 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 (2005) 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
  • 61
    • 4043175563 scopus 로고    scopus 로고
    • Different roles of electrostatics in heat and in cold: adaptation by citrate synthase
    • Kumar S., and Nussinov R. Different roles of electrostatics in heat and in cold: adaptation by citrate synthase. ChemBioChem 5 (2004) 280-290
    • (2004) ChemBioChem , vol.5 , pp. 280-290
    • Kumar, S.1    Nussinov, R.2
  • 62
    • 0033594989 scopus 로고    scopus 로고
    • Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability
    • Ibarra-Molero B., Loladze V.V., Makhatadze G.I., and Sanchez-Ruiz J.M. Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability. Biochemistry 38 (1999) 8138-8149
    • (1999) Biochemistry , vol.38 , pp. 8138-8149
    • Ibarra-Molero, B.1    Loladze, V.V.2    Makhatadze, G.I.3    Sanchez-Ruiz, J.M.4
  • 63
    • 33846702300 scopus 로고    scopus 로고
    • The first structure of a cold-active catalase from Vibrio salmonicida at 1.96 Å reveals structural aspects of cold adaptation
    • Riise E.K., Lorentzen M.S., Helland R., Smalas A.O., Leiros H.K., and Willassen N.P. The first structure of a cold-active catalase from Vibrio salmonicida at 1.96 Å reveals structural aspects of cold adaptation. Acta Crystallog. sect. D 63 (2007) 135-148
    • (2007) Acta Crystallog. sect. D , vol.63 , pp. 135-148
    • Riise, E.K.1    Lorentzen, M.S.2    Helland, R.3    Smalas, A.O.4    Leiros, H.K.5    Willassen, N.P.6
  • 64
    • 0344549848 scopus 로고    scopus 로고
    • Residue determinants and sequence analysis of cold-adapted trypsins
    • Leiros H.K., Willassen N.P., and Smalås A.O. Residue determinants and sequence analysis of cold-adapted trypsins. Extremophiles 3 (1999) 205-219
    • (1999) Extremophiles , vol.3 , pp. 205-219
    • Leiros, H.K.1    Willassen, N.P.2    Smalås, A.O.3
  • 65
    • 0031762555 scopus 로고    scopus 로고
    • Archaeal cold-adapted proteins: structural and evolutionary analysis of the elongation factor 2 proteins from psychrophilic, mesophilic and thermophilic methanogens
    • Thomas T., and Cavicchioli R. Archaeal cold-adapted proteins: structural and evolutionary analysis of the elongation factor 2 proteins from psychrophilic, mesophilic and thermophilic methanogens. FEBS Letters 439 (1998) 281-286
    • (1998) FEBS Letters , vol.439 , pp. 281-286
    • Thomas, T.1    Cavicchioli, R.2
  • 66
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey
    • Szilagyi A., and Zavodszky P. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Structure 8 (2000) 493-504
    • (2000) Structure , vol.8 , pp. 493-504
    • Szilagyi, A.1    Zavodszky, P.2
  • 68
    • 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. Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum. J. Biol. Chem. 274 (1999) 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
  • 69
    • 0032534759 scopus 로고    scopus 로고
    • Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level
    • Aghajari N., Feller G., Gerday C., and Haser R. Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level. Structure 6 (1998) 1503-1516
    • (1998) Structure , vol.6 , pp. 1503-1516
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 70
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: a mechanism of protein structure stabilization
    • Burley S.K., and Petsko G.A. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science 229 (1985) 23-28
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 71
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: a determinant of thermal stability of thermophilic proteins
    • Kannan N., and Vishveshwara S. Aromatic clusters: a determinant of thermal stability of thermophilic proteins. Protein Eng. 13 (2000) 753-761
    • (2000) Protein Eng. , vol.13 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2
  • 72
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 73
    • 0016167076 scopus 로고
    • The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters
    • Eisenthal R., and Cornish-Bowden A. The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters. Biochem. J. 139 (1974) 715-720
    • (1974) Biochem. J. , vol.139 , pp. 715-720
    • Eisenthal, R.1    Cornish-Bowden, A.2
  • 74
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms. Lysozyme and insulin
    • Shrake A., and Rupley J.A. Environment and exposure to solvent of protein atoms. Lysozyme and insulin. J. Mol. Biol. 79 (1973) 351-371
    • (1973) J. Mol. Biol. , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2
  • 75
    • 0029957505 scopus 로고    scopus 로고
    • The enthalpy change in protein folding and binding: refinement of parameters for structure-based calculations
    • Hilser V.J., Gomez J., and Freire E. The enthalpy change in protein folding and binding: refinement of parameters for structure-based calculations. Proteins: Struct. Funct. Genet. 26 (1996) 123-133
    • (1996) Proteins: Struct. Funct. Genet. , vol.26 , pp. 123-133
    • Hilser, V.J.1    Gomez, J.2    Freire, E.3
  • 76
    • 0031984455 scopus 로고    scopus 로고
    • Structure-based thermodynamic design of peptide ligands: application to peptide inhibitors of the aspartic protease endothiapepsin
    • Luque I., Gomez J., Semo N., and Freire E. Structure-based thermodynamic design of peptide ligands: application to peptide inhibitors of the aspartic protease endothiapepsin. Proteins: Struct. Funct. Genet. 30 (1998) 74-85
    • (1998) Proteins: Struct. Funct. Genet. , vol.30 , pp. 74-85
    • Luque, I.1    Gomez, J.2    Semo, N.3    Freire, E.4
  • 79
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallog. 24 (1993) 795-800
    • (1993) J. Appl. Crystallog. , vol.24 , pp. 795-800
    • Kabsch, W.1
  • 81
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 82
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 83
    • 0037080244 scopus 로고    scopus 로고
    • Rapid grid-based construction of the molecular surface and the use of induced surface charge to calculate reaction field energies: applications to the molecular systems and geometric objects
    • Rocchia W., Sridharan S., Nicholls A., Alexov E., Chiabrera A., and Honig B. Rapid grid-based construction of the molecular surface and the use of induced surface charge to calculate reaction field energies: applications to the molecular systems and geometric objects. J. Comput. Chem. 23 (2002) 128-137
    • (2002) J. Comput. Chem. , vol.23 , pp. 128-137
    • Rocchia, W.1    Sridharan, S.2    Nicholls, A.3    Alexov, E.4    Chiabrera, A.5    Honig, B.6
  • 84
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald I.K., and Thornton J.M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238 (1994) 777-793
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 85
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.