메뉴 건너뛰기




Volumn 5, Issue APR, 2014, Pages

Protective role of salt in catalysis and maintaining structure of halophilic proteins against denaturation

Author keywords

Denaturants; Haloadaptations; Halophiles; Secondary structure; Structure; Tertiary structure

Indexed keywords

ALCOHOL DEHYDROGENASE; DIHYDROFOLATE REDUCTASE; FERREDOXIN; GLUTAMATE DEHYDROGENASE (NADP); ISOCITRATE DEHYDROGENASE; MALATE DEHYDROGENASE; MICROBIAL ENZYME; NUCLEOSIDE DIPHOSPHATE KINASE; ORGANIC SOLVENT; PROTEINASE; SODIUM CHLORIDE; THERMOLYSIN;

EID: 84899680226     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00165     Document Type: Short Survey
Times cited : (93)

References (56)
  • 1
    • 77954348887 scopus 로고    scopus 로고
    • Catalytic and thermodynamic characterization of protease from Halobacterium sp.SP1(1)
    • doi: 10.1016/j.resmic.2010.04.005
    • Akolkar, A. V., and Desai, A. J. (2010). Catalytic and thermodynamic characterization of protease from Halobacterium sp. SP1(1). Res. Microbiol. 161, 355-362. doi: 10.1016/j.resmic.2010.04.005
    • (2010) Res. Microbiol. , vol.161 , pp. 355-362
    • Akolkar, A.V.1    Desai, A.J.2
  • 2
    • 84871451278 scopus 로고    scopus 로고
    • Effect of organic solvents on the activity and stability of halophilic alcohol dehydrogenase (ADH2) from Haloferax volcanii
    • doi: 10.1007/s00792-012-0498-0
    • Alsafadi, D., and Paradisi, F. (2013). Effect of organic solvents on the activity and stability of halophilic alcohol dehydrogenase (ADH2) from Haloferax volcanii. Extremophiles 17, 115-122. doi: 10.1007/s00792-012-0498-0
    • (2013) Extremophiles , vol.17 , pp. 115-122
    • Alsafadi, D.1    Paradisi, F.2
  • 3
    • 0033916841 scopus 로고    scopus 로고
    • Salt dependent stability and unfolding of [Fe2-S2] ferredoxin of Halobacterium salinarum: spectroscopic investigations
    • doi: 10.1016/S0006-3495(00)76312-0
    • Bandyopadhyay, A. K., and Sonawat, H. M. (2000). Salt dependent stability and unfolding of [Fe2-S2] ferredoxin of Halobacterium salinarum: spectroscopic investigations. Biophys. J. 79, 501-510. doi: 10.1016/S0006-3495(00)76312-0
    • (2000) Biophys. J. , vol.79 , pp. 501-510
    • Bandyopadhyay, A.K.1    Sonawat, H.M.2
  • 4
    • 73649087584 scopus 로고    scopus 로고
    • On the mechanism of SDS-induced protein denaturation
    • doi: 10.1002/bip.21318
    • Bhuyan, A. K. (2010). On the mechanism of SDS-induced protein denaturation. Biopolymers 93, 186-199. doi: 10.1002/bip.21318
    • (2010) Biopolymers , vol.93 , pp. 186-199
    • Bhuyan, A.K.1
  • 5
    • 0028034679 scopus 로고
    • Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions
    • doi: 10.1006/jmbi.1994.1741
    • Bonneté, F., Madern, D., and Zaccai, G. (1994). Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions. J. Mol. Biol. 244, 436-447. doi: 10.1006/jmbi.1994.1741
    • (1994) J. Mol. Biol. , vol.244 , pp. 436-447
    • Bonneté, F.1    Madern, D.2    Zaccai, G.3
  • 6
    • 78349309121 scopus 로고    scopus 로고
    • Gradual adaptive changes of a protein facing high salt concentrations
    • doi: 10.1016/j.jmb.2010.09.055
    • Coquelle, N., Talon, R., Juers, D. H., Girard, É., Kahn, R., and Madern, D. (2010). Gradual adaptive changes of a protein facing high salt concentrations. J. Mol. Biol. 404, 493-505. doi: 10.1016/j.jmb.2010.09.055
    • (2010) J. Mol. Biol. , vol.404 , pp. 493-505
    • Coquelle, N.1    Talon, R.2    Juers, D.H.3    Girard, É.4    Kahn, R.5    Madern, D.6
  • 7
    • 0037027318 scopus 로고    scopus 로고
    • Link between protein-solvent and weak protein-protein interactions gives insight into halophilic adaptation
    • doi: 10.1021/bi025830z
    • Costenaro, L., Zaccai, G., and Ebel, C. (2002). Link between protein-solvent and weak protein-protein interactions gives insight into halophilic adaptation. Biochemistry 41, 13245-13252. doi: 10.1021/bi025830z
    • (2002) Biochemistry , vol.41 , pp. 13245-13252
    • Costenaro, L.1    Zaccai, G.2    Ebel, C.3
  • 8
    • 0031195026 scopus 로고    scopus 로고
    • The structural basis of protein halophilicity
    • doi: 10.1016/S0300-9629(96)00268-X
    • Danson, M. J., and Hough, D. W. (1997). The structural basis of protein halophilicity. Comp. Biochem. Physiol. A Physiol. 117, 307-312. doi: 10.1016/S0300-9629(96)00268-X
    • (1997) Comp. Biochem. Physiol. A Physiol. , vol.117 , pp. 307-312
    • Danson, M.J.1    Hough, D.W.2
  • 9
    • 43849095922 scopus 로고    scopus 로고
    • Salt dependent resistance against chemical denaturation of alkaline protease from a newly isolated haloalkaliphilic Bacillus sp
    • doi: 10.1016/j.biortech.2007.12.020
    • Dodia, M. S., Bhimani, H. G., Rawal, C. M., Joshi, R. H., and Singh, S. P. (2008). Salt dependent resistance against chemical denaturation of alkaline protease from a newly isolated haloalkaliphilic Bacillus sp. Bioresour. Technol. 99, 6223-6227. doi: 10.1016/j.biortech.2007.12.020
    • (2008) Bioresour. Technol. , vol.99 , pp. 6223-6227
    • Dodia, M.S.1    Bhimani, H.G.2    Rawal, C.M.3    Joshi, R.H.4    Singh, S.P.5
  • 10
    • 0037027320 scopus 로고    scopus 로고
    • Solvent interactions of halophilic malate dehydrogenase
    • doi: 10.1021/bi0258290
    • Ebel, C., Costenaro, L., Pascu, M., Faou, P., Kernel, B., Proust-De Martin, F., et al. (2002). Solvent interactions of halophilic malate dehydrogenase. Biochemistry 41, 13234-13244. doi: 10.1021/bi0258290
    • (2002) Biochemistry , vol.41 , pp. 13234-13244
    • Ebel, C.1    Costenaro, L.2    Pascu, M.3    Faou, P.4    Kernel, B.5    Proust-De Martin, F.6
  • 11
    • 0033551441 scopus 로고    scopus 로고
    • Relative role of anions and cations in the stabilization of halophilic malate dehydrogenase
    • doi: 10.1021/bi9900774
    • Ebel, C., Faou, P., Kernel, B., and Zaccai, G. (1999). Relative role of anions and cations in the stabilization of halophilic malate dehydrogenase. Biochemistry 38, 9039-9047. doi: 10.1021/bi9900774
    • (1999) Biochemistry , vol.38 , pp. 9039-9047
    • Ebel, C.1    Faou, P.2    Kernel, B.3    Zaccai, G.4
  • 12
    • 0026646179 scopus 로고
    • Biochemical, structural, and molecular genetic aspects of halophilism
    • doi: 10.1016/S0065-3233(08)60553-7
    • Eisenberg, H., Mevarech, M., and Zaccai, G. (1992). Biochemical, structural, and molecular genetic aspects of halophilism. Adv. Protein. Chem. 43, 1-62. doi: 10.1016/S0065-3233(08)60553-7
    • (1992) Adv. Protein. Chem. , vol.43 , pp. 1-62
    • Eisenberg, H.1    Mevarech, M.2    Zaccai, G.3
  • 13
    • 84896381156 scopus 로고    scopus 로고
    • "Biochemical analysis of halophilic dehydrogenases altered by site-directed mutagenesis," in Genetic Manipulation of DNA and Protein-Examples From Current Research, ed D
    • Figurski (InTech). doi: 10.5772/34565. Available online at
    • Esclapez, J., Camacho, M., Pire, C., and Bonete, M. J. (2013). "Biochemical analysis of halophilic dehydrogenases altered by site-directed mutagenesis," in Genetic Manipulation of DNA and Protein-Examples From Current Research, ed D. Figurski (InTech). doi: 10.5772/34565. Available online at: http://cdn.intechopen.com/pdfs/42535/InTech-Biochemical_analysis_of_halophilic_dehydrogenases_altered_by_site_directed_mutagenesis.pdf
    • (2013)
    • Esclapez, J.1    Camacho, M.2    Pire, C.3    Bonete, M.J.4
  • 14
    • 33847147150 scopus 로고    scopus 로고
    • Analysis of acidic surface of Haloferax mediterranei glucose dehydrogenase by site-directed mutagenesis
    • doi: 10.1016/j.febslet.2007.01.054
    • Esclapez, J., Pire, C., Bautista, V., Martínez-Espinosa, R. M., Ferrer, J., and Bonete, M. J. (2007). Analysis of acidic surface of Haloferax mediterranei glucose dehydrogenase by site-directed mutagenesis. FEBS Lett. 581, 837-842. doi: 10.1016/j.febslet.2007.01.054
    • (2007) FEBS Lett. , vol.581 , pp. 837-842
    • Esclapez, J.1    Pire, C.2    Bautista, V.3    Martínez-Espinosa, R.M.4    Ferrer, J.5    Bonete, M.J.6
  • 15
    • 33744960237 scopus 로고    scopus 로고
    • Acquisition of an insertion peptide for efficient aminoacylation by a halophile tRNA synthetase
    • doi: 10.1021/bi0521386
    • Evilla, C., and Hou, Y. (2006). Acquisition of an insertion peptide for efficient aminoacylation by a halophile tRNA synthetase. Biochemistry 45, 6835-6845. doi: 10.1021/bi0521386
    • (2006) Biochemistry , vol.45 , pp. 6835-6845
    • Evilla, C.1    Hou, Y.2
  • 16
    • 0032466981 scopus 로고    scopus 로고
    • Fluorescence and quenching comparative studies of halophilic and bovine glutamate dehydrogenase
    • doi: 10.1016/S1011-1344(98)00214-0
    • Ferrer, J., Cremades, R., Pire, C., and Bonete, M. J. (1998). Fluorescence and quenching comparative studies of halophilic and bovine glutamate dehydrogenase. J. Photochem. Photobiol. B. 47, 148-154. doi: 10.1016/S1011-1344(98)00214-0
    • (1998) J. Photochem. Photobiol. B. , vol.47 , pp. 148-154
    • Ferrer, J.1    Cremades, R.2    Pire, C.3    Bonete, M.J.4
  • 18
    • 68849108440 scopus 로고    scopus 로고
    • Enzymes from solvent tolerant microbes: useful biocatalysts for non-aqueous enzymology
    • doi: 10.1080/07388550802688797
    • Gupta, A., and Khare, S. K. (2009). Enzymes from solvent tolerant microbes: useful biocatalysts for non-aqueous enzymology. Crit. Rev. Biotechnol. 29, 44-54. doi: 10.1080/07388550802688797
    • (2009) Crit. Rev. Biotechnol. , vol.29 , pp. 44-54
    • Gupta, A.1    Khare, S.K.2
  • 19
    • 29244438994 scopus 로고    scopus 로고
    • Characterisation of a highly stable α-amylase from the halophilic archaeon Haloarcula hispanica
    • doi: 10.1007/s00792-005-0471-2
    • Hutcheon, G. W., Vasisht, N., and Bolhuis, A. (2005). Characterisation of a highly stable α-amylase from the halophilic archaeon Haloarcula hispanica. Extremophiles 9, 487-495. doi: 10.1007/s00792-005-0471-2
    • (2005) Extremophiles , vol.9 , pp. 487-495
    • Hutcheon, G.W.1    Vasisht, N.2    Bolhuis, A.3
  • 20
    • 0032517347 scopus 로고    scopus 로고
    • Sodium chloride enhances markedly the thermal stability of thermolysin as well as its catalytic activity
    • doi: 10.1016/S0167-4838(98)00189-7
    • Inouye, K., Kuzuya, K., and Tonomura, B. (1998). Sodium chloride enhances markedly the thermal stability of thermolysin as well as its catalytic activity. Biochim. Biophys. Acta 1388, 209-214. doi: 10.1016/S0167-4838(98)00189-7
    • (1998) Biochim. Biophys. Acta , vol.1388 , pp. 209-214
    • Inouye, K.1    Kuzuya, K.2    Tonomura, B.3
  • 21
    • 0037459095 scopus 로고    scopus 로고
    • The oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies
    • doi: 10.1016/S0022-2836(02)01450-X
    • Irimia, A., Ebel, C., Madern, D., Richard, S. B., Cosenza, L. W., Zaccaï, G., et al. (2003). The oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies. J. Mol. Biol. 326, 859-873. doi: 10.1016/S0022-2836(02)01450-X
    • (2003) J. Mol. Biol. , vol.326 , pp. 859-873
    • Irimia, A.1    Ebel, C.2    Madern, D.3    Richard, S.B.4    Cosenza, L.W.5    Zaccaï, G.6
  • 22
    • 0037027525 scopus 로고    scopus 로고
    • Secondary and quaternary structural transition of the halophilic archaeon nucleoside diphosphate kinase under high-and low-salt conditions
    • doi: 10.1111/j.1574-6968.2002.tb11441.x
    • Ishibashi, M., Arakawa, T., Philo, J. S., Sakashita, K., Yonezawa, Y., Tokunaga, H., et al. (2002). Secondary and quaternary structural transition of the halophilic archaeon nucleoside diphosphate kinase under high-and low-salt conditions. FEMS Microbiol. Lett. 216, 235-241. doi: 10.1111/j.1574-6968.2002.tb11441.x
    • (2002) FEMS Microbiol. Lett. , vol.216 , pp. 235-241
    • Ishibashi, M.1    Arakawa, T.2    Philo, J.S.3    Sakashita, K.4    Yonezawa, Y.5    Tokunaga, H.6
  • 23
    • 79959715897 scopus 로고    scopus 로고
    • Stability of haloalkaliphilic Geomicrobium sp
    • doi: 10.1134/S0006297911060095
    • Karan, R., and Khare, S. K. (2011). Stability of haloalkaliphilic Geomicrobium sp. protease modulated by salt. Biochemistry (Mosc.) 76, 686-693. doi: 10.1134/S0006297911060095
    • (2011) protease modulated by salt. Biochemistry (Mosc.) , vol.76 , pp. 686-693
    • Karan, R.1    Khare, S.K.2
  • 24
    • 84861659828 scopus 로고    scopus 로고
    • Purification and characterization of maltooligosaccharide-forming alpha-amylase from moderately halophilic Marinobacter sp
    • doi: 10.1016/j.biortech.2011.11.109
    • Kumar, S., and Khare, S. K. (2012). Purification and characterization of maltooligosaccharide-forming alpha-amylase from moderately halophilic Marinobacter sp. EMB8. Bioresour. Technol. 116, 247-251. doi: 10.1016/j.biortech.2011.11.109
    • (2012) EMB8. Bioresour. Technol. , vol.116 , pp. 247-251
    • Kumar, S.1    Khare, S.K.2
  • 25
    • 0016139829 scopus 로고
    • Salt-dependent properties of proteins from extremely halophilic bacteria
    • Lanyi, J. K. (1974). Salt-dependent properties of proteins from extremely halophilic bacteria. Bacteriol. Rev. 38, 272-290.
    • (1974) Bacteriol. Rev. , vol.38 , pp. 272-290
    • Lanyi, J.K.1
  • 26
    • 0033050107 scopus 로고    scopus 로고
    • Spectroscopic characterization of two soluble transducers from the archaeon Halobacterium salinarum
    • doi: 10.1023/A:1021031227197
    • Larsen, R. W., Yang, J., Hou, S., Helms, M. K., Jameson, D. M., and Alam, M. (1999). Spectroscopic characterization of two soluble transducers from the archaeon Halobacterium salinarum. J. Protein Chem. 18, 269-275. doi: 10.1023/A:1021031227197
    • (1999) J. Protein Chem. , vol.18 , pp. 269-275
    • Larsen, R.W.1    Yang, J.2    Hou, S.3    Helms, M.K.4    Jameson, D.M.5    Alam, M.6
  • 27
    • 84864383171 scopus 로고    scopus 로고
    • Purification and characterization of an organic solvent-tolerant alkaline cellulase from a halophilic isolate of Thalassobacillus
    • doi: 10.1007/s10529-012-0938-z
    • Li, X., Wang, H., Li, T., and Yu, H. (2012). Purification and characterization of an organic solvent-tolerant alkaline cellulase from a halophilic isolate of Thalassobacillus. Biotechnol. Lett. 34, 1531-1536. doi: 10.1007/s10529-012-0938-z
    • (2012) Biotechnol. Lett. , vol.34 , pp. 1531-1536
    • Li, X.1    Wang, H.2    Li, T.3    Yu, H.4
  • 28
    • 84862787763 scopus 로고    scopus 로고
    • Purification and characterization of novel organic-solvent-tolerant β-amylase and serine protease from a newly isolated Salimicrobium halophilum strain LY20
    • doi: 10.1111/j.1574-6968.2012.02522.x
    • Li, X., and Yu, H. Y. (2012). Purification and characterization of novel organic-solvent-tolerant β-amylase and serine protease from a newly isolated Salimicrobium halophilum strain LY20. FEMS Microbiol. Lett. 329, 204-211. doi: 10.1111/j.1574-6968.2012.02522.x
    • (2012) FEMS Microbiol. Lett. , vol.329 , pp. 204-211
    • Li, X.1    Yu, H.Y.2
  • 30
    • 8744261915 scopus 로고    scopus 로고
    • Salt-dependent studies of NADP-dependent isocitrate dehydrogenase from the halophilic archaeon Haloferax volcanii
    • doi: 10.1007/s00792-004-0398-z
    • Madern, D., Camacho, M., Rodríguez-Arnedo, A., Bonete, M. J., and Zaccai, G. (2004). Salt-dependent studies of NADP-dependent isocitrate dehydrogenase from the halophilic archaeon Haloferax volcanii. Extremophiles 8, 377-384. doi: 10.1007/s00792-004-0398-z
    • (2004) Extremophiles , vol.8 , pp. 377-384
    • Madern, D.1    Camacho, M.2    Rodríguez-Arnedo, A.3    Bonete, M.J.4    Zaccai, G.5
  • 31
    • 34447268243 scopus 로고    scopus 로고
    • Influence of an anion-binding site in the stabilization of halophilic malate dehydrogenase from Haloarcula marismortui
    • doi: 10.1016/j.biochi.2007.03.008
    • Madern, D., and Ebel, C. (2007). Influence of an anion-binding site in the stabilization of halophilic malate dehydrogenase from Haloarcula marismortui. Biochimie 89, 981-987. doi: 10.1016/j.biochi.2007.03.008
    • (2007) Biochimie , vol.89 , pp. 981-987
    • Madern, D.1    Ebel, C.2
  • 32
    • 0034166764 scopus 로고    scopus 로고
    • Halophilic adaptation of enzymes
    • doi: 10.1007/s007920050142
    • Madern, D., Ebel, C., and Zaccai, G. (2000). Halophilic adaptation of enzymes. Extremophiles 4, 91-98. doi: 10.1007/s007920050142
    • (2000) Extremophiles , vol.4 , pp. 91-98
    • Madern, D.1    Ebel, C.2    Zaccai, G.3
  • 33
    • 0029027430 scopus 로고
    • Mutation at a single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts
    • doi: 10.1111/j.1432-1033.1995.tb20659.x
    • Madern, D., Pfister, C., and Zaccai, G. (1995). Mutation at a single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts. Eur. J. Biochem. 230, 1088-1095. doi: 10.1111/j.1432-1033.1995.tb20659.x
    • (1995) Eur. J. Biochem. , vol.230 , pp. 1088-1095
    • Madern, D.1    Pfister, C.2    Zaccai, G.3
  • 34
    • 0030718555 scopus 로고    scopus 로고
    • Stabilisation of halophilic malate dehydrogenase from Haloarcula marismortui by divalent cations
    • doi: 10.1111/j.1432-1033.1997.00607.x
    • Madern, D., and Zaccai, G. (1997). Stabilisation of halophilic malate dehydrogenase from Haloarcula marismortui by divalent cations. Eur. J. Biochem. 249, 607-611. doi: 10.1111/j.1432-1033.1997.00607.x
    • (1997) Eur. J. Biochem. , vol.249 , pp. 607-611
    • Madern, D.1    Zaccai, G.2
  • 35
    • 2942674796 scopus 로고    scopus 로고
    • Molecular adaptation: the malate dehydrogenase from the extreme halophilic bacterium Salinibacter ruber behaves like a non-halophilic protein
    • doi: 10.1016/j.biochi.2004.04.004
    • Madern, D., and Zaccai, G. (2004). Molecular adaptation: the malate dehydrogenase from the extreme halophilic bacterium Salinibacter ruber behaves like a non-halophilic protein. Biochimie 86, 295-303. doi: 10.1016/j.biochi.2004.04.004
    • (2004) Biochimie , vol.86 , pp. 295-303
    • Madern, D.1    Zaccai, G.2
  • 36
    • 0017408353 scopus 로고
    • Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea.1. Purification and molecular characteristics
    • doi: 10.1021/bi00636a009
    • Mevarech, M., Eisenberg, H., and Neumann, E. (1977). Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characteristics. Biochemistry 16, 3781-3785. doi: 10.1021/bi00636a009
    • (1977) Biochemistry , vol.16 , pp. 3781-3785
    • Mevarech, M.1    Eisenberg, H.2    Neumann, E.3
  • 37
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: proteins with a grain of salt
    • doi: 10.1016/S0301-4622(00)00126-5
    • Mevarech, M., Frolow, F., and Gloss, L. M. (2000). Halophilic enzymes: proteins with a grain of salt. Biophys. Chem. 86, 155-164. doi: 10.1016/S0301-4622(00)00126-5
    • (2000) Biophys. Chem. , vol.86 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 38
    • 67650462243 scopus 로고    scopus 로고
    • First evidence for the salt-dependent folding and activity of an esterase from the halophilic archaea Haloarcula marismortui
    • doi: 10.1016/j.bbalip.2009.03.006
    • Müller-Santos, M., de Souza, E. M., Pedrosa, F. O., Mitchell, D. A., Longhi, S., Carrière, F., et al. (2009). First evidence for the salt-dependent folding and activity of an esterase from the halophilic archaea Haloarcula marismortui. Biochim. Biophys. Acta 1791, 719-729. doi: 10.1016/j.bbalip.2009.03.006
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 719-729
    • Müller-Santos, M.1    de Souza, E.M.2    Pedrosa, F.O.3    Mitchell, D.A.4    Longhi, S.5    Carrière, F.6
  • 39
    • 42949104034 scopus 로고    scopus 로고
    • Microbial life at high salt concentrations: phylogenetic and metabolic diversity
    • doi: 10.1186/1746-1448-4-2
    • Oren, A. (2008). Microbial life at high salt concentrations: phylogenetic and metabolic diversity. Saline Syst. 4, 2. doi: 10.1186/1746-1448-4-2
    • (2008) Saline Syst. , vol.4 , pp. 2
    • Oren, A.1
  • 40
    • 84890305097 scopus 로고    scopus 로고
    • Life at high salt concentrations, intracellular KCl concentrations, and acidic proteomes
    • doi: 10.3389/fmicb.2013.00315
    • Oren, A. (2013). Life at high salt concentrations, intracellular KCl concentrations, and acidic proteomes. Front. Microbiol. 4:315. doi: 10.3389/fmicb.2013.00315
    • (2013) Front. Microbiol. , vol.4 , pp. 315
    • Oren, A.1
  • 41
    • 0036549959 scopus 로고    scopus 로고
    • Stability of Natrialba magadii NDP kinase? comparisons with other halophilic proteins
    • doi: 10.1007/s007920100232
    • Polosina, Y. Y., Zamyatkin, D. F., Kostyukova, A. S., Filimonov, V. V., and Fedorov, O. V. (2002). Stability of Natrialba magadii NDP kinase? comparisons with other halophilic proteins. Extremophiles 6, 135-142. doi: 10.1007/s007920100232
    • (2002) Extremophiles , vol.6 , pp. 135-142
    • Polosina, Y.Y.1    Zamyatkin, D.F.2    Kostyukova, A.S.3    Filimonov, V.V.4    Fedorov, O.V.5
  • 42
    • 0019618128 scopus 로고
    • Structure and activity of malate dehydrogenase of the extreme halophilic bacteria of the Dead Sea.1. Conformation and interaction with water and salt between 5 M and 1 M NaCl concentration
    • doi: 10.1111/j.1432-1033.1981.tb05542.x
    • Pundak, S., and Eisenberg, H. (1981). Structure and activity of malate dehydrogenase of the extreme halophilic bacteria of the Dead Sea. 1. Conformation and interaction with water and salt between 5 M and 1 M NaCl concentration. Eur. J. Biochem. 118, 463-470. doi: 10.1111/j.1432-1033.1981.tb05542.x
    • (1981) Eur. J. Biochem. , vol.118 , pp. 463-470
    • Pundak, S.1    Eisenberg, H.2
  • 43
    • 70349209122 scopus 로고    scopus 로고
    • Solution behavior and activity of a halophilic esterase under high salt concentration
    • doi: 10.1371/journal.pone.0006980
    • Rao, L., Zhao, X., Pan, F., Li, Y., Xue, Y., Ma, Y., et al. (2009). Solution behavior and activity of a halophilic esterase under high salt concentration. PLoS ONE 4:e6980. doi: 10.1371/journal.pone.0006980
    • (2009) PLoS ONE , vol.4
    • Rao, L.1    Zhao, X.2    Pan, F.3    Li, Y.4    Xue, Y.5    Ma, Y.6
  • 44
    • 0034620588 scopus 로고    scopus 로고
    • Halophilic adaptation: novel solvent protein interactions observed in the 2 9 and 2.6 Å resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui.
    • doi: 10.1021/bi991001a
    • Richard, S. B., Madern, D., Garcin, E., and Zaccai, G. (2000). Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 Å resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui. Biochemistry 39, 992-1000. doi: 10.1021/bi991001a
    • (2000) Biochemistry , vol.39 , pp. 992-1000
    • Richard, S.B.1    Madern, D.2    Garcin, E.3    Zaccai, G.4
  • 45
    • 79951674162 scopus 로고    scopus 로고
    • Purification and characterization of an organic-solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp
    • doi: 10.1007/s10295-010-0770-1
    • Shafiei, M., Ziaee, A. A., and Amoozegar, M. A. (2011). Purification and characterization of an organic-solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp. strain F. J. Ind. Microbiol. Biotechnol. 38, 275-281. doi: 10.1007/s10295-010-0770-1
    • (2011) strain F. J. Ind. Microbiol. Biotechnol. , vol.38 , pp. 275-281
    • Shafiei, M.1    Ziaee, A.A.2    Amoozegar, M.A.3
  • 47
    • 84956498793 scopus 로고    scopus 로고
    • Thermostable proteases
    • in Thermophilic Microbes in Environmental and Industrial Biotechnology, eds T. Satyanarayana, J. Littlechild, and Y. Kawarabayasi (Dordrecht: Springer), doi: 10.1007/978-94-007-5899-5_32
    • Sinha, R., and Khare, S. K. (2013b). "Thermostable proteases," in Thermophilic Microbes in Environmental and Industrial Biotechnology, eds T. Satyanarayana, J. Littlechild, and Y. Kawarabayasi (Dordrecht: Springer), 859-880. doi: 10.1007/978-94-007-5899-5_32
    • (2013) , pp. 859-880
    • Sinha, R.1    Khare, S.K.2
  • 48
    • 84857050838 scopus 로고    scopus 로고
    • Correlation between catalysis and tertiary structure arrangement in an archaeal halophilic subtilase
    • doi: 10.1016/j.biochi.2011.11.011
    • Souza, T. A., Okamoto, D. N., Ruiz, D. M., Oliveira, L. C., Kondo, M. Y., Tersario, I. L., et al. (2012). Correlation between catalysis and tertiary structure arrangement in an archaeal halophilic subtilase. Biochimie 94, 798-805. doi: 10.1016/j.biochi.2011.11.011
    • (2012) Biochimie , vol.94 , pp. 798-805
    • Souza, T.A.1    Okamoto, D.N.2    Ruiz, D.M.3    Oliveira, L.C.4    Kondo, M.Y.5    Tersario, I.L.6
  • 49
    • 73949105836 scopus 로고    scopus 로고
    • Structural basis for the aminoacid composition of proteins from halophilic archea
    • doi: 10.1371/journal.pbio.1000257
    • Tadeo, X., López-Méndez, B., Trigueros, T., Laín, A., Castaño, D., and Millet, O. (2009). Structural basis for the aminoacid composition of proteins from halophilic archea. PLoS Biol. 7:e1000257. doi: 10.1371/journal.pbio.1000257
    • (2009) PLoS Biol. , vol.7
    • Tadeo, X.1    López-Méndez, B.2    Trigueros, T.3    Laín, A.4    Castaño, D.5    Millet, O.6
  • 50
    • 43049141115 scopus 로고    scopus 로고
    • Effects of introducing negative charges into the molecular surface of thermolysin by site-directed mutagenesis on its activity and stability
    • doi: 10.1016/j.bbapap.2007.12.004
    • Takita, T., Aono, T., Sakurama, H., Itoh, T., Wada, T., Minoda, M., et al. (2008). Effects of introducing negative charges into the molecular surface of thermolysin by site-directed mutagenesis on its activity and stability. Biochim. Biophys. Acta 1784, 481-488. doi: 10.1016/j.bbapap.2007.12.004
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 481-488
    • Takita, T.1    Aono, T.2    Sakurama, H.3    Itoh, T.4    Wada, T.5    Minoda, M.6
  • 51
    • 84897652756 scopus 로고    scopus 로고
    • An eperimental point of view on hydration/ solvation in halophilic proteins
    • doi: 10.3389/fmicb.2014.00066
    • Talon, R., Coquelle, N., Madern, D., and Girard, E. (2014). An eperimental point of view on hydration/ solvation in halophilic proteins. Front. Microbiol. 5:66. doi: 10.3389/fmicb.2014.00066
    • (2014) Front. Microbiol. , vol.5 , pp. 66
    • Talon, R.1    Coquelle, N.2    Madern, D.3    Girard, E.4
  • 52
    • 84868347674 scopus 로고    scopus 로고
    • A dual role of divalent metal ions in catalysis and folding of RNase H1 from extreme halophilic archaeon Halobacterium sp.NRC-1
    • doi: 10.1016/j.fob.2012.10.003
    • Tannous, E., Yokoyama, K., You, D. J., Koga, Y., and Kanaya, S. (2012). A dual role of divalent metal ions in catalysis and folding of RNase H1 from extreme halophilic archaeon Halobacterium sp. NRC-1. FEBS Open Bio. 2, 345-352. doi: 10.1016/j.fob.2012.10.003
    • (2012) FEBS Open Bio. , vol.2 , pp. 345-352
    • Tannous, E.1    Yokoyama, K.2    You, D.J.3    Koga, Y.4    Kanaya, S.5
  • 53
    • 50049123899 scopus 로고    scopus 로고
    • Engineering of halophilic enzymes: two acidic amino acid residues at the carboxy-terminal region confer halophilic characteristics to Halomonas and Pseudomonas nucleoside diphosphate kinases
    • doi: 10.1110/ps.035725.108
    • Tokunaga, H., Arakwa, T., and Tokunaga, M. (2008). Engineering of halophilic enzymes: two acidic amino acid residues at the carboxy-terminal region confer halophilic characteristics to Halomonas and Pseudomonas nucleoside diphosphate kinases. Protein Sci. 17, 1603-1610. doi: 10.1110/ps.035725.108
    • (2008) Protein Sci. , vol.17 , pp. 1603-1610
    • Tokunaga, H.1    Arakwa, T.2    Tokunaga, M.3
  • 54
    • 0842303216 scopus 로고    scopus 로고
    • Highly efficient renaturation of β-lactamase isolated from moderately halophilic bacteria
    • doi: 10.1016/S0014-5793(03)01508-4
    • Tokunaga, H., Ishibashi, M., Arakawa, T., and Tokunaga, M. (2004). Highly efficient renaturation of β-lactamase isolated from moderately halophilic bacteria. FEBS Lett. 558, 7-12. doi: 10.1016/S0014-5793(03)01508-4
    • (2004) FEBS Lett. , vol.558 , pp. 7-12
    • Tokunaga, H.1    Ishibashi, M.2    Arakawa, T.3    Tokunaga, M.4
  • 55
    • 0036408309 scopus 로고    scopus 로고
    • The effect of salts on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases
    • doi: 10.1016/S0022-2836(02)00916-6
    • Wright, D. B., Banks, D. D., Lohman, J. R., Hilsenbeck, J. L., and Gloss, L. M. (2002). The effect of salts on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases. J. Mol. Biol. 323, 327-344. doi: 10.1016/S0022-2836(02)00916-6
    • (2002) J. Mol. Biol. , vol.323 , pp. 327-344
    • Wright, D.B.1    Banks, D.D.2    Lohman, J.R.3    Hilsenbeck, J.L.4    Gloss, L.M.5
  • 56
    • 84872954522 scopus 로고    scopus 로고
    • Hydration shells with a pinch of salt
    • doi: 10.1002/bip.22154
    • Zaccai, G. (2013). Hydration shells with a pinch of salt. Biopolymers 99, 233-238. doi: 10.1002/bip.22154
    • (2013) Biopolymers , vol.99 , pp. 233-238
    • Zaccai, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.