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Volumn 104, Issue 9, 2013, Pages 1178-1186

Enzymology: Some paradigm shifts over the years

Author keywords

Catalytic promiscuity; Enzyme catalysis; Intrinsically disordered proteins; Moonlighting proteins; Protein purification

Indexed keywords


EID: 84878360602     PISSN: 00113891     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (15)

References (114)
  • 4
    • 84859002070 scopus 로고    scopus 로고
    • Smart polymer mediated purification and recovery of active proteins from inclusion bodies
    • Gautam, S., Dubey, P., Singh, P., Kesavardana, S., Varadarajan, R. and Gupta, M. N., Smart polymer mediated purification and recovery of active proteins from inclusion bodies. J. Chromatogr. A, 2012, 1235, 10-25.
    • (2012) J. Chromatogr. A , vol.1235 , pp. 10-25
    • Gautam, S.1    Dubey, P.2    Singh, P.3    Kesavardana, S.4    Varadarajan, R.5    Gupta, M.N.6
  • 5
    • 34047168776 scopus 로고    scopus 로고
    • Leveraging protein purification strategies in proteomics
    • Roy, I., Mondal, K. and Gupta, M. N., Leveraging protein purification strategies in proteomics. J. Chromatogr. B, 2007, 849, 32- 42.
    • (2007) J. Chromatogr. B , vol.849 , pp. 32-42
    • Roy, I.1    Mondal, K.2    Gupta, M.N.3
  • 7
    • 0027012660 scopus 로고
    • Linderstrom-Lang and the Carlsberg laboratory: the view of a postdoctoral fellow in 1954
    • Richards, F. M., Linderstrom-Lang and the Carlsberg laboratory: the view of a postdoctoral fellow in 1954. Protein Sci., 1992, 1, 1721-1730.
    • (1992) Protein Sci. , vol.1 , pp. 1721-1730
    • Richards, F.M.1
  • 8
    • 70349139155 scopus 로고    scopus 로고
    • Early events in protein folding
    • Sinha, K. K. and Udgaonkar, J. B., Early events in protein folding. Curr. Sci., 2009, 96, 1053-1070.
    • (2009) Curr. Sci. , vol.96 , pp. 1053-1070
    • Sinha, K.K.1    Udgaonkar, J.B.2
  • 9
    • 23444456924 scopus 로고    scopus 로고
    • How to study proteins by circular dichroism
    • Kelly, S. M., Jess, T. J. and Price, N. C., How to study proteins by circular dichroism. Biochim. Biophys. Acta, 2005, 1751, 119- 139.
    • (2005) Biochim. Biophys. Acta , vol.1751 , pp. 119-139
    • Kelly, S.M.1    Jess, T.J.2    Price, N.C.3
  • 10
    • 84878347561 scopus 로고    scopus 로고
    • Biophotonics
    • Academic Press, San Diego, Part B
    • Marriott, G. and Parker, I. (eds), Biophotonics. In Methods in Enzymology, Academic Press, San Diego, Part A (vol. 360) and Part B (vol. 361), 2003.
    • (2003) Methods in Enzymology , vol.360-361 , Issue.PART A
    • Marriott, G.1    Parker, I.2
  • 11
    • 4344642067 scopus 로고    scopus 로고
    • Protein motions promote catalysis
    • Tousignant, A. and Pelletier, J. N., Protein motions promote catalysis. Chem. Biol., 2004, 11, 1037-1042.
    • (2004) Chem. Biol. , vol.11 , pp. 1037-1042
    • Tousignant, A.1    Pelletier, J.N.2
  • 12
    • 36849048228 scopus 로고    scopus 로고
    • Intrinsic motions along an enzymatic reaction trajectory
    • Henzler-Wildman, K. A. et al., Intrinsic motions along an enzymatic reaction trajectory. Nature, 2007, 450, 838-844.
    • (2007) Nature , vol.450 , pp. 838-844
    • Henzler-Wildman, K.A.1
  • 13
    • 68049085675 scopus 로고    scopus 로고
    • A 21st century revisionist's view at a turning point in enzymology
    • Nagel, Z. D. and Klinman, J. P., A 21st century revisionist's view at a turning point in enzymology. Nature Chem. Biol., 2009, 5, 543-550.
    • (2009) Nature Chem. Biol. , vol.5 , pp. 543-550
    • Nagel, Z.D.1    Klinman, J.P.2
  • 14
    • 0028046098 scopus 로고
    • Enhancement of enzyme activity in aqueous - organic solvents mixtures
    • Batra, R. and Gupta, M. N., Enhancement of enzyme activity in aqueous - organic solvents mixtures. Biotechnol. Lett., 1994, 16, 1059-1064.
    • (1994) Biotechnol. Lett. , vol.16 , pp. 1059-1064
    • Batra, R.1    Gupta, M.N.2
  • 15
    • 0025882622 scopus 로고
    • Denaturation capacity: a new quantitative criterion for selection of organic solvents as reaction media in biocatalysis
    • Khmelnitsky, Y. L., Mozhaev, V. V., Belova, A. B., Sergeeva, M. V. and Martinek, K., Denaturation capacity: a new quantitative criterion for selection of organic solvents as reaction media in biocatalysis. Eur. J. Biochem., 1991, 198, 31-41.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 31-41
    • Khmelnitsky, Y.L.1    Mozhaev, V.V.2    Belova, A.B.3    Sergeeva, M.V.4    Martinek, K.5
  • 16
    • 0024653016 scopus 로고
    • Enzymatic catalysis in anhydrous organic solvents
    • Klibanov, A. M., Enzymatic catalysis in anhydrous organic solvents. Trends Biochem. Sci., 1989, 14, 141-144.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 141-144
    • Klibanov, A.M.1
  • 17
    • 0026517617 scopus 로고
    • Enzyme function in organic solvents
    • Gupta, M. N., Enzyme function in organic solvents. Eur. J. Biochem., 1992, 203, 25-32.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 25-32
    • Gupta, M.N.1
  • 18
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Klibanov, A. M., Improving enzymes by using them in organic solvents. Nature, 2001, 409, 241-246.
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 19
    • 0023788217 scopus 로고
    • The influence of water on protease-catalyzed peptide synthesis in acetonitrile/ water mixtures
    • Reslow, M., Adlercreutz, P. and Mattiasson, B., The influence of water on protease-catalyzed peptide synthesis in acetonitrile/ water mixtures. Eur. J. Biochem., 1988, 177, 313-318.
    • (1988) Eur. J. Biochem. , vol.177 , pp. 313-318
    • Reslow, M.1    Adlercreutz, P.2    Mattiasson, B.3
  • 21
    • 1942472616 scopus 로고    scopus 로고
    • Freeze-drying of proteins: some emerging concerns
    • Roy, I. and Gupta, M. N., Freeze-drying of proteins: some emerging concerns. Biotechnol. Appl. Biochem., 2004, 39, 165-177.
    • (2004) Biotechnol. Appl. Biochem. , vol.39 , pp. 165-177
    • Roy, I.1    Gupta, M.N.2
  • 22
    • 0036669618 scopus 로고    scopus 로고
    • Enzyme activation for nonaqueous media
    • Lee, Y. M. and Dordick, J. S., Enzyme activation for nonaqueous media. Curr. Opin. Biotechnol., 2002, 13, 376-384.
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 376-384
    • Lee, Y.M.1    Dordick, J.S.2
  • 23
    • 27844563238 scopus 로고    scopus 로고
    • Biocatalysis in semi-aqueous and nearly anhydrous conditions
    • Hudson, E. P., Eppler, R. K. and Clark, D. S., Biocatalysis in semi-aqueous and nearly anhydrous conditions. Curr. Opin. Biotechnol., 2005, 16, 637-643.
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 637-643
    • Hudson, E.P.1    Eppler, R.K.2    Clark, D.S.3
  • 24
    • 0842281268 scopus 로고    scopus 로고
    • Obtaining higher transesterification rates with subtilisin Carlsberg in nonaqueous media
    • Roy, I., Sharma, A. and Gupta, M. N., Obtaining higher transesterification rates with subtilisin Carlsberg in nonaqueous media. Bioorg. Med. Chem. Lett., 2004, 14, 887-889.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 887-889
    • Roy, I.1    Sharma, A.2    Gupta, M.N.3
  • 26
    • 1842639623 scopus 로고    scopus 로고
    • Preparation of highly active alphachymotrypsin for catalysis in organic media
    • Roy, I. and Gupta, M. N., Preparation of highly active alphachymotrypsin for catalysis in organic media. Bioorg. Med. Chem. Lett., 2004, 14, 2191-2193.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 2191-2193
    • Roy, I.1    Gupta, M.N.2
  • 27
    • 82355191999 scopus 로고    scopus 로고
    • Increasing catalytic efficiency of Candida rugosa lipase for the synthesis of tert-alkyl butyrates in low-water media
    • Majumder, A. B. and Gupta, M. N., Increasing catalytic efficiency of Candida rugosa lipase for the synthesis of tert-alkyl butyrates in low-water media. Biocatal. Biotransform., 2011, 29, 238-245.
    • (2011) Biocatal. Biotransform. , vol.29 , pp. 238-245
    • Majumder, A.B.1    Gupta, M.N.2
  • 28
    • 33645298457 scopus 로고    scopus 로고
    • Preparation of crosslinked enzyme aggregates by using bovine serum albumin as a proteic feeder
    • Shah, S., Sharma, A. and Gupta, M. N., Preparation of crosslinked enzyme aggregates by using bovine serum albumin as a proteic feeder. Anal. Biochem., 2006, 351, 207-213.
    • (2006) Anal. Biochem. , vol.351 , pp. 207-213
    • Shah, S.1    Sharma, A.2    Gupta, M.N.3
  • 29
    • 0035927926 scopus 로고    scopus 로고
    • Enzyme-coated micro-crystals: a 1-step method for high activity biocatalyst preparation.
    • Kreiner, M., Moore, B. D. and Parker, M. C., Enzyme-coated micro-crystals: a 1-step method for high activity biocatalyst preparation. Chem. Commun., 2001, 1096-1097.
    • (2001) Chem. Commun. , pp. 1096-1097
    • Kreiner, M.1    Moore, B.D.2    Parker, M.C.3
  • 30
    • 34548422290 scopus 로고    scopus 로고
    • A high performance lipase preparation: characterization and atomic force microscopy
    • Shah, S., Sharma, A., Varandani, D., Mehta, B. R. and Gupta, M. N., A high performance lipase preparation: characterization and atomic force microscopy. J. Nanosci. Nanotechnol., 2007, 7, 1-4.
    • (2007) J. Nanosci. Nanotechnol. , vol.7 , pp. 1-4
    • Shah, S.1    Sharma, A.2    Varandani, D.3    Mehta, B.R.4    Gupta, M.N.5
  • 31
    • 45849113968 scopus 로고    scopus 로고
    • Cross-linked protein coated microcrystals as biocatalysts in non-aqueous solvents
    • Shah, S., Sharma, A. and Gupta, M. N., Cross-linked protein coated microcrystals as biocatalysts in non-aqueous solvents. Biocatal. Biotransform., 2008, 26, 266-271.
    • (2008) Biocatal. Biotransform. , vol.26 , pp. 266-271
    • Shah, S.1    Sharma, A.2    Gupta, M.N.3
  • 33
    • 33846642511 scopus 로고    scopus 로고
    • Kinetic resolution of (±)-1-phenylethanol in [Bmim][PF6] using high activity preparations of lipases
    • Shah, S. and Gupta, M. N., Kinetic resolution of (±)-1-phenylethanol in [Bmim][PF6] using high activity preparations of lipases. Bioorg. Med. Chem. Lett., 2007, 17, 921-924.
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 921-924
    • Shah, S.1    Gupta, M.N.2
  • 34
    • 33845452931 scopus 로고    scopus 로고
    • Obtaining high transesterification activity for subtilisin in ionic liquids
    • Shah, S. and Gupta, M. N., Obtaining high transesterification activity for subtilisin in ionic liquids. Biochim. Biophys. Acta, 2007, 1770, 94-98.
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 94-98
    • Shah, S.1    Gupta, M.N.2
  • 36
    • 84878363717 scopus 로고    scopus 로고
    • accessed on 30 December
    • http://murov.info/webercises.htm; accessed on 30 December 2012.
    • (2012)
  • 38
    • 0037415338 scopus 로고    scopus 로고
    • Bioconversion in an aqueous two phase system using a smart biocatalyst: casein hydrolysis by alpha chymotrypsin
    • Sharma, S., Teotia, S. and Gupta, M. N., Bioconversion in an aqueous two phase system using a smart biocatalyst: casein hydrolysis by alpha chymotrypsin. Enzyme Microb. Technol., 2003, 32, 337-339.
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 337-339
    • Sharma, S.1    Teotia, S.2    Gupta, M.N.3
  • 39
    • 0034888428 scopus 로고    scopus 로고
    • Free polymeric bioligands in aqueous two phase affinity extractions of microbial xylanases and pullulanase
    • Teotia, S. and Gupta, M. N., Free polymeric bioligands in aqueous two phase affinity extractions of microbial xylanases and pullulanase. Protein Express. Purif., 2001, 22, 484-488.
    • (2001) Protein Express. Purif. , vol.22 , pp. 484-488
    • Teotia, S.1    Gupta, M.N.2
  • 40
    • 0033388241 scopus 로고    scopus 로고
    • Comparison of batch, packed bed and expanded bed purification of A. niger cellulase using cellulose beads
    • Roy, I., Pai, A., Lali, A. and Gupta, M. N., Comparison of batch, packed bed and expanded bed purification of A. niger cellulase using cellulose beads. Bioseparation, 1999, 8, 317-326.
    • (1999) Bioseparation , vol.8 , pp. 317-326
    • Roy, I.1    Pai, A.2    Lali, A.3    Gupta, M.N.4
  • 41
    • 0033781789 scopus 로고    scopus 로고
    • Purification of alkaline phosphatase from chicken intestine by expanded bed affinity chromatography on dye-linked cellulose
    • Roy, I. and Gupta, M. N., Purification of alkaline phosphatase from chicken intestine by expanded bed affinity chromatography on dye-linked cellulose. Biotechnol. Appl. Biochem., 2000, 32, 81-87.
    • (2000) Biotechnol. Appl. Biochem. , vol.32 , pp. 81-87
    • Roy, I.1    Gupta, M.N.2
  • 42
    • 0034469206 scopus 로고    scopus 로고
    • Purification of a double-headed inhibitor of alpha-amylase/proteinase K from wheat germ by expanded bed chromatography
    • Roy, I. and Gupta, M. N., Purification of a "double-headed" inhibitor of alpha-amylase/proteinase K from wheat germ by expanded bed chromatography. Bioseparation, 2001, 9, 239-245.
    • (2001) Bioseparation , vol.9 , pp. 239-245
    • Roy, I.1    Gupta, M.N.2
  • 44
    • 0028484263 scopus 로고
    • Purification of proteins by adsorption chromatography in expanded beds
    • Chase, H. A., Purification of proteins by adsorption chromatography in expanded beds. Trends Biotechnol., 1994, 12, 296-303.
    • (1994) Trends Biotechnol. , vol.12 , pp. 296-303
    • Chase, H.A.1
  • 45
    • 0034595911 scopus 로고    scopus 로고
    • Perfusion chromatography: an emergent technique for the analysis of food proteins
    • García, M. C., Marina, M. L. and Torre, M., Perfusion chromatography: an emergent technique for the analysis of food proteins. J. Chromatogr. A, 2000, 880, 169-187.
    • (2000) J. Chromatogr. A , vol.880 , pp. 169-187
    • García, M.C.1    Marina, M.L.2    Torre, M.3
  • 46
    • 0026427240 scopus 로고    scopus 로고
    • Perfusion chromatography
    • Regnier, F. E., Perfusion chromatography. Nature, 1999, 350, 634-635.
    • (1999) Nature , vol.350 , pp. 634-635
    • Regnier, F.E.1
  • 47
    • 0034830304 scopus 로고    scopus 로고
    • Three phase partitioning as a largescale separation method for purification of a wheat germ bifunctional protease/amylase inhibitor
    • Sharma, A. and Gupta, M. N., Three phase partitioning as a largescale separation method for purification of a wheat germ bifunctional protease/amylase inhibitor. Process Biochem., 2001, 37, 193-196.
    • (2001) Process Biochem. , vol.37 , pp. 193-196
    • Sharma, A.1    Gupta, M.N.2
  • 48
    • 0031281935 scopus 로고    scopus 로고
    • Three phase partitioning: concentration and purification of proteins
    • Dennison, C. and Lovrein, R., Three phase partitioning: concentration and purification of proteins. Protein Express. Purif., 1997, 11, 149-161.
    • (1997) Protein Express. Purif. , vol.11 , pp. 149-161
    • Dennison, C.1    Lovrein, R.2
  • 49
    • 84871104190 scopus 로고    scopus 로고
    • Activation of alpha chymotrypsin by three phase partitioning is accompanied by aggregation
    • doi:10.1371/journal.pone.0049241
    • Rather, G. M., Mukherjee, J., Halling, P. J. and Gupta, M. N., Activation of alpha chymotrypsin by three phase partitioning is accompanied by aggregation. PLoS One, 2012, 7, e49241; doi:10.1371/journal.pone.0049241.
    • (2012) PLoS One , vol.7
    • Rather, G.M.1    Mukherjee, J.2    Halling, P.J.3    Gupta, M.N.4
  • 50
    • 84877721513 scopus 로고    scopus 로고
    • Role of smart polymers in protein purification and refolding
    • Gautam, S., Dubey, P., Singh, P., Varadarajan, R. and Gupta, M. N., Role of smart polymers in protein purification and refolding. Bioengineered, 2012, 3, 286-288.
    • (2012) Bioengineered , vol.3 , pp. 286-288
    • Gautam, S.1    Dubey, P.2    Singh, P.3    Varadarajan, R.4    Gupta, M.N.5
  • 51
    • 0002423852 scopus 로고
    • Affinity precipitation
    • (ed. Street, G.), Blackie Academic and ProfessionalNew York
    • Gupta, M. N. and Mattiasson, B., Affinity precipitation. In Highly Selective Separations in Biotechnology (ed. Street, G.), Blackie Academic and Professional, New York, 1994, pp. 7-33.
    • (1994) Highly Selective Separations in Biotechnology , pp. 7-33
    • Gupta, M.N.1    Mattiasson, B.2
  • 52
    • 0037145328 scopus 로고    scopus 로고
    • Macro-(affinity ligand) facilitated three phase partitioning (MLFTPP) for purification of xylanase
    • Sharma, A. and Gupta, M. N., Macro-(affinity ligand) facilitated three phase partitioning (MLFTPP) for purification of xylanase. Biotechnol. Bioeng., 2002, 80, 228-232.
    • (2002) Biotechnol. Bioeng. , vol.80 , pp. 228-232
    • Sharma, A.1    Gupta, M.N.2
  • 53
    • 0037358560 scopus 로고    scopus 로고
    • Macro-(affinity ligand) facilitated three phase partitioning (MLFTPP) for purification of glucoamylase and pullulanase using alginate
    • Mondal, K., Sharma, A. and Gupta, M. N., Macro-(affinity ligand) facilitated three phase partitioning (MLFTPP) for purification of glucoamylase and pullulanase using alginate. Protein Express. Purif., 2003, 28, 190-195.
    • (2003) Protein Express. Purif. , vol.28 , pp. 190-195
    • Mondal, K.1    Sharma, A.2    Gupta, M.N.3
  • 54
    • 84865535323 scopus 로고    scopus 로고
    • Simultaneous refolding and purification of recombinant proteins by macro-(affinity ligand) facilitated three-phase partitioning
    • Gautam, S., Dubey, P., Singh, P., Varadarajan, R. and Gupta, M. N., Simultaneous refolding and purification of recombinant proteins by macro-(affinity ligand) facilitated three-phase partitioning. Anal. Biochem., 2012, 430, 56-64.
    • (2012) Anal. Biochem. , vol.430 , pp. 56-64
    • Gautam, S.1    Dubey, P.2    Singh, P.3    Varadarajan, R.4    Gupta, M.N.5
  • 55
    • 0028501437 scopus 로고
    • Reversed micellar extraction of charged fusion proteins
    • Forney, C. E. and Glatz, C. E., Reversed micellar extraction of charged fusion proteins. Biotechnol. Prog., 1994, 10, 499-502.
    • (1994) Biotechnol. Prog. , vol.10 , pp. 499-502
    • Forney, C.E.1    Glatz, C.E.2
  • 56
    • 0030144987 scopus 로고    scopus 로고
    • Liquid- liquid extraction of proteins with reversed micelles
    • Pires, M. J., Aires-Barros, M. R. and Cabral, J. M. S., Liquid- liquid extraction of proteins with reversed micelles. Biotechnol. Prog., 1996, 12, 290-301.
    • (1996) Biotechnol. Prog. , vol.12 , pp. 290-301
    • Pires, M.J.1    Aires-Barros, M.R.2    Cabral, J.M.S.3
  • 57
    • 33751401429 scopus 로고    scopus 로고
    • Magnetic techniques for the isolation and purification of proteins and peptides
    • Safarik, I. and Safarikova, M., Magnetic techniques for the isolation and purification of proteins and peptides. BioMagn. Res. Technol., 2004, 2, 7-21.
    • (2004) BioMagn. Res. Technol. , vol.2 , pp. 7-21
    • Safarik, I.1    Safarikova, M.2
  • 58
    • 0037359159 scopus 로고    scopus 로고
    • Protein separations using colloidal magnetic nanoparticles
    • Bucak, S., Jones, D. A., Laibinis, P. and Hatton, T., Protein separations using colloidal magnetic nanoparticles. Biotechnol. Prog., 2003, 19, 477-484.
    • (2003) Biotechnol. Prog. , vol.19 , pp. 477-484
    • Bucak, S.1    Jones, D.A.2    Laibinis, P.3    Hatton, T.4
  • 59
    • 0001189231 scopus 로고    scopus 로고
    • Current trends in affinity-based separation of proteins/enzymes
    • Roy, I. and Gupta, M. N., Current trends in affinity-based separation of proteins/enzymes. Curr. Sci., 2000, 78, 587-591.
    • (2000) Curr. Sci. , vol.78 , pp. 587-591
    • Roy, I.1    Gupta, M.N.2
  • 60
    • 33645420958 scopus 로고    scopus 로고
    • The affinity concept in bioseparation: Evolving paradigms and expanding range of applications
    • Mondal, K. and Gupta, M. N., The affinity concept in bioseparation: Evolving paradigms and expanding range of applications. Biomol. Eng., 2006, 23, 59-76.
    • (2006) Biomol. Eng. , vol.23 , pp. 59-76
    • Mondal, K.1    Gupta, M.N.2
  • 61
    • 4744342353 scopus 로고    scopus 로고
    • Alternative bioseparation operations: life beyond packed-bed chromatography
    • Przybycien, T. M., Pujar, N. S. and Steele, L. M., Alternative bioseparation operations: life beyond packed-bed chromatography. Curr. Opin. Biotechnol., 2004, 15, 469-478.
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 469-478
    • Przybycien, T.M.1    Pujar, N.S.2    Steele, L.M.3
  • 63
    • 0038497542 scopus 로고
    • A structure for deoxyribose nucleic acid
    • Watson, J. D. and Crick, F. H. C., A structure for deoxyribose nucleic acid. Nature, 1953, 171, 737-738.
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.C.2
  • 64
    • 79955420122 scopus 로고    scopus 로고
    • Isozymes, moonlighting proteins and promiscous enzymes
    • Gupta, M. N., Kapoor, M., Majumder, A. B. and Singh, V., Isozymes, moonlighting proteins and promiscous enzymes. Curr. Sci., 2011, 100, 1152-1162.
    • (2011) Curr. Sci. , vol.100 , pp. 1152-1162
    • Gupta, M.N.1    Kapoor, M.2    Majumder, A.B.3    Singh, V.4
  • 65
    • 0003450992 scopus 로고
    • Academic Press, San Diego, California
    • Webb, E. C., Enzyme Nomenclature, Academic Press, San Diego, California, 1992.
    • (1992) Enzyme Nomenclature
    • Webb, E.C.1
  • 66
    • 34247131307 scopus 로고    scopus 로고
    • Enzyme promiscuity: mechanism and applications
    • Hult, K. and Berglund, P., Enzyme promiscuity: mechanism and applications. Trends Biotechnol., 2007, 25, 231-238.
    • (2007) Trends Biotechnol. , vol.25 , pp. 231-238
    • Hult, K.1    Berglund, P.2
  • 67
    • 79955449980 scopus 로고    scopus 로고
    • First bovine serum albumin-promoted synthesis of enones, cinnamic acids and coumarins in ionic liquid: an insight into the role of protein impurities in porcine pancreas lipase for olefinic bond formation
    • Sharma, N., Sharma, U. K., Kumar, R., Katoch, N., Kumar, R. and Sinha, A. K., First bovine serum albumin-promoted synthesis of enones, cinnamic acids and coumarins in ionic liquid: an insight into the role of protein impurities in porcine pancreas lipase for olefinic bond formation. Adv. Synth. Catal., 2011, 353, 871-878.
    • (2011) Adv. Synth. Catal. , vol.353 , pp. 871-878
    • Sharma, N.1    Sharma, U.K.2    Kumar, R.3    Katoch, N.4    Kumar, R.5    Sinha, A.K.6
  • 68
    • 84866897120 scopus 로고    scopus 로고
    • Decarboxylative Aldol reaction catalysed by lipases and a protease in organic co-solvent mixtures and nearly anhydrous organic solvent media
    • Kapoor, M., Majumder, A. B., Mukherjee, J. and Gupta, M. N., Decarboxylative Aldol reaction catalysed by lipases and a protease in organic co-solvent mixtures and nearly anhydrous organic solvent media. Biocatal. Biotransform., 2012, 30, 399-408.
    • (2012) Biocatal. Biotransform. , vol.30 , pp. 399-408
    • Kapoor, M.1    Majumder, A.B.2    Mukherjee, J.3    Gupta, M.N.4
  • 69
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: a mechanistic and evolutionary perspective
    • Khersonsky, O. and Tawfik, D. S., Enzyme promiscuity: a mechanistic and evolutionary perspective. Annu. Rev. Biochem., 2010, 79, 471-505.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.S.2
  • 71
    • 78650268993 scopus 로고    scopus 로고
    • Ostensible enzyme promiscuity: alkene cleavage by peroxidases
    • Mutti, F. G., Lara, M., Kroutil, M. and Kroutil, W., Ostensible enzyme promiscuity: alkene cleavage by peroxidases. Chem. Eur. J., 2010, 16, 14142-14148.
    • (2010) Chem. Eur. J. , vol.16 , pp. 14142-14148
    • Mutti, F.G.1    Lara, M.2    Kroutil, M.3    Kroutil, W.4
  • 73
    • 77958046500 scopus 로고    scopus 로고
    • Hydrolases: catalytically promiscuous enzymes for non-conventional reactions in organic synthesis
    • Busto, E., Gotor-Fernandez, V. and Gotor, V., Hydrolases: catalytically promiscuous enzymes for non-conventional reactions in organic synthesis. Chem. Soc. Rev., 2010, 39, 4504-4523.
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 4504-4523
    • Busto, E.1    Gotor-Fernandez, V.2    Gotor, V.3
  • 74
    • 84858071530 scopus 로고    scopus 로고
    • Lipase promiscuity and its biochemical applications
    • Kapoor, M. and Gupta, M. N., Lipase promiscuity and its biochemical applications. Process Biochem., 2012, 47, 555- 569.
    • (2012) Process Biochem. , vol.47 , pp. 555-569
    • Kapoor, M.1    Gupta, M.N.2
  • 75
    • 79960820232 scopus 로고    scopus 로고
    • Bacterial degradation of strobilurin fungicides: a role for a promiscuous methyl esterase activity of the subtilisin proteases?
    • Clinton, B. et al., Bacterial degradation of strobilurin fungicides: a role for a promiscuous methyl esterase activity of the subtilisin proteases? Biocatal. Biotransform., 2011, 29, 1-11.
    • (2011) Biocatal. Biotransform. , vol.29 , pp. 1-11
    • Clinton, B.1
  • 76
    • 78651310908 scopus 로고    scopus 로고
    • Nuclease p1: a new biocatalyst for direct asymmetric aldol reaction under solvent-free conditions
    • Li, H., He, Y., Yuan, Y. and Guan, Z., Nuclease p1: a new biocatalyst for direct asymmetric aldol reaction under solvent-free conditions. Green Chem., 2011, 13, 185-189.
    • (2011) Green Chem. , vol.13 , pp. 185-189
    • Li, H.1    He, Y.2    Yuan, Y.3    Guan, Z.4
  • 77
    • 19944395879 scopus 로고    scopus 로고
    • Penicillin G acylase catalyzed Markovnikov addition of allopurinol to vinyl ester.
    • Wu, W. B., Wang, N., Xu, J. M., Wu, Q. and Lin, X. F., Penicillin G acylase catalyzed Markovnikov addition of allopurinol to vinyl ester. Chem. Commun., 2005, 2348-2350.
    • (2005) Chem. Commun. , pp. 2348-2350
    • Wu, W.B.1    Wang, N.2    Xu, J.M.3    Wu, Q.4    Lin, X.F.5
  • 78
    • 34547398555 scopus 로고    scopus 로고
    • Promiscuous acylase-catalysed aza-Mihael additions of aromatic N heterocycles in organic solvent
    • Qian, C., Xu, J. M., Wu, Q., Lv, D. S. and Lin, X. F., Promiscuous acylase-catalysed aza-Mihael additions of aromatic N heterocycles in organic solvent. Tetrahedron Lett., 2007, 48, 6100-6104.
    • (2007) Tetrahedron Lett. , vol.48 , pp. 6100-6104
    • Qian, C.1    Xu, J.M.2    Wu, Q.3    Lv, D.S.4    Lin, X.F.5
  • 80
    • 67649114374 scopus 로고    scopus 로고
    • Lipase catalysed direct Mannich reaction in water: utilization of biocatalytic promiscuity for C-C bond formation in a "one-pot" synthesis
    • Li, K., He, T., Li, Chao, Feng, X. W., Wang, N. and Yu, X. Q., Lipase catalysed direct Mannich reaction in water: utilization of biocatalytic promiscuity for C-C bond formation in a "one-pot" synthesis. Green Chem., 2009, 11, 777-779.
    • (2009) Green Chem. , vol.11 , pp. 777-779
    • Li, K.1    He, T.2    Li, C.3    Feng, X.W.4    Wang, N.5    Yu, X.Q.6
  • 81
    • 62949096122 scopus 로고    scopus 로고
    • Moonlighting proteins - an update
    • Jeffery, C. J., Moonlighting proteins - an update. Mol. BioSyst., 2009, 5, 345-350.
    • (2009) Mol. BioSyst. , vol.5 , pp. 345-350
    • Jeffery, C.J.1
  • 82
    • 0037396292 scopus 로고    scopus 로고
    • Enzymes with extra talents: moonlighting functions and catalytic promiscuity
    • Copley, S. D., Enzymes with extra talents: moonlighting functions and catalytic promiscuity. Curr. Opin. Chem. Biol., 2003, 7, 265-272.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 265-272
    • Copley, S.D.1
  • 83
    • 0002449434 scopus 로고
    • The active site and enzyme action
    • (ed. Nord, F. F.), Interscience Publisher, IncNew York
    • Koshland Jr, D. E., The active site and enzyme action. In Advances in Enzymology (ed. Nord, F. F.), Interscience Publisher, Inc, New York, 1960, Vol. 22, pp. 45-97.
    • (1960) Advances in Enzymology , vol.22 , pp. 45-97
    • Koshland, D.E.Jr.1
  • 84
    • 77950369259 scopus 로고    scopus 로고
    • Moonlighting proteins: An intriguing mode of multitasking
    • Huberts, D. H. E. W. and van der Klei, I. J., Moonlighting proteins: An intriguing mode of multitasking. Biochem. Biophys. Acta, 2010, 1803, 520-525.
    • (2010) Biochem. Biophys. Acta , vol.1803 , pp. 520-525
    • Huberts, D.H.E.W.1    van der Klei, I.J.2
  • 85
    • 0036709869 scopus 로고    scopus 로고
    • Structure to function relationships in cerruloplasmin: a "moonlighting" protein
    • Bielli, P. and Calabrese, L., Structure to function relationships in cerruloplasmin: a "moonlighting" protein. Cell. Mol. Life Sci., 2002, 59, 1413-1427.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1413-1427
    • Bielli, P.1    Calabrese, L.2
  • 86
    • 2442430450 scopus 로고    scopus 로고
    • Bifunctional and moonlighting enzymes: lighting the way to regulatory control
    • Moore, B. D., Bifunctional and moonlighting enzymes: lighting the way to regulatory control. Trends Plant Sci., 2004, 9, 221- 228.
    • (2004) Trends Plant Sci. , vol.9 , pp. 221-228
    • Moore, B.D.1
  • 87
    • 27844471239 scopus 로고    scopus 로고
    • Mass spectrometry and the search for moonlighting proteins
    • Jeffery, C. J., Mass spectrometry and the search for moonlighting proteins. Mass Spectrom. Rev., 2005, 24, 772-782.
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 772-782
    • Jeffery, C.J.1
  • 89
    • 79960376932 scopus 로고    scopus 로고
    • Do protein-protein interaction databases identify moonlighting proteins? Mol
    • Gomez, A., Hernandez, S., Amela, I., Pinol, J., Cedano, J. and Querol, E., Do protein-protein interaction databases identify moonlighting proteins? Mol. BioSyst., 2011, 7, 2379-2382.
    • (2011) BioSyst. , vol.7 , pp. 2379-2382
    • Gomez, A.1    Hernandez, S.2    Amela, I.3    Pinol, J.4    Cedano, J.5    Querol, E.6
  • 90
    • 79959619604 scopus 로고    scopus 로고
    • Proteins with neomorphic moonlighting functions in disease
    • Jeffery, C. J., Proteins with neomorphic moonlighting functions in disease. IUBMB Life, 2011, 63, 489-494.
    • (2011) IUBMB Life , vol.63 , pp. 489-494
    • Jeffery, C.J.1
  • 91
    • 79958741408 scopus 로고    scopus 로고
    • Intrinsically disordered proteins from A to Z
    • Uversky, V. N., Intrinsically disordered proteins from A to Z. Int. J. Biochem. Cell Biol., 2011, 43, 1090-1103.
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 1090-1103
    • Uversky, V.N.1
  • 92
    • 84965093921 scopus 로고
    • The preparation of subtilisin- modified ribonuclease and the separation of the peptide and protein components
    • Richards, F. M. and Vithayathil, P. J., The preparation of subtilisin- modified ribonuclease and the separation of the peptide and protein components. J. Biol. Chem., 1959, 234, 1459- 1465.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1459-1465
    • Richards, F.M.1    Vithayathil, P.J.2
  • 93
  • 94
    • 70349503591 scopus 로고    scopus 로고
    • Biophysics of Parkinson"s disease: structure and aggregation of alpha-synuclein
    • Uversky, V. N. and Eliezer, D., Biophysics of Parkinson"s disease: structure and aggregation of alpha-synuclein. Curr. Protein Pept. Sci., 2009, 10, 483-499.
    • (2009) Curr. Protein Pept. Sci. , vol.10 , pp. 483-499
    • Uversky, V.N.1    Eliezer, D.2
  • 95
    • 76649114676 scopus 로고    scopus 로고
    • Protein dynamics and conformational disorder in molecular recognition
    • Mittag, T., Kay, L. E. and Forman-Kay, J. D., Protein dynamics and conformational disorder in molecular recognition. J. Mol. Recognit., 2010, 23, 105-116.
    • (2010) J. Mol. Recognit. , vol.23 , pp. 105-116
    • Mittag, T.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 96
    • 33750639677 scopus 로고
    • The key-lock theory and the induced fit theory
    • Koshland, D. E., The key-lock theory and the induced fit theory. Angew. Chem., Int. Ed. Engl., 1994, 33, 2375-2378.
    • (1994) Angew. Chem. Int. Ed. Engl. , vol.33 , pp. 2375-2378
    • Koshland, D.E.1
  • 97
    • 84878373702 scopus 로고    scopus 로고
    • accessed on 30 December
    • http://www.grc.org/programs.aspx?year=2010&program=intrinsic #, accessed on 30 December 2012.
    • (2012)
  • 98
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa, P., Szasz, C. and Buday, L., Structural disorder throws new light on moonlighting. Trends Biochem. Sci., 2005, 30, 484- 489.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 484-489
    • Tompa, P.1    Szasz, C.2    Buday, L.3
  • 99
    • 0035022941 scopus 로고    scopus 로고
    • Intrinsically disordered protein
    • Dunker, A. K. et al., Intrinsically disordered protein. J. Mol. Graphica Model., 2001, 19, 26-59.
    • (2001) J. Mol. Graphica Model. , vol.19 , pp. 26-59
    • Dunker, A.K.1
  • 100
    • 84873194008 scopus 로고    scopus 로고
    • Protein flexibility, not disorder, is intrinsic to molecular recognition
    • Janin, J. and Sternberg, M. J. E., Protein flexibility, not disorder, is intrinsic to molecular recognition. F1000 Biol. Rep., 2013, 5:2.
    • (2013) F1000 Biol. Rep. , vol.5 , pp. 2
    • Janin, J.1    Sternberg, M.J.E.2
  • 101
    • 84873198878 scopus 로고    scopus 로고
    • The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure
    • Uversky, V. N. and Dunker, A. K., The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure. F1000 Biol. Rep., 2013, 5:1.
    • (2013) F1000 Biol. Rep. , vol.5 , pp. 1
    • Uversky, V.N.1    Dunker, A.K.2
  • 102
    • 0029584688 scopus 로고
    • What makes a binding site a binding site? Curr
    • Ringe, D., What makes a binding site a binding site? Curr. Opin. Struct. Biol., 1995, 5, 825-829.
    • (1995) Opin. Struct. Biol. , vol.5 , pp. 825-829
    • Ringe, D.1
  • 103
    • 70350347721 scopus 로고    scopus 로고
    • Q&A: what are pharmacological chaperones and why are they interesting?
    • Ringe, D. and Petsko, D. A., Q&A: what are pharmacological chaperones and why are they interesting?. J. Biol., 2009, 8, 80-85.
    • (2009) J. Biol. , vol.8 , pp. 80-85
    • Ringe, D.1    Petsko, D.A.2
  • 104
  • 105
    • 58149477054 scopus 로고    scopus 로고
    • Effect of trehalose on protein structure
    • Jain, N. K. and Roy, I., Effect of trehalose on protein structure. Protein Sci., 2009, 18, 24-36.
    • (2009) Protein Sci. , vol.18 , pp. 24-36
    • Jain, N.K.1    Roy, I.2
  • 106
    • 79960080783 scopus 로고    scopus 로고
    • Effect of chemical chaperones in improving the solubility of recombinant proteins in Escherichia coli
    • Prasad, S., Khadatre, P. B. and Roy, I., Effect of chemical chaperones in improving the solubility of recombinant proteins in Escherichia coli. Appl. Environ. Microbiol., 2011, 77, 4603- 4609.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 4603-4609
    • Prasad, S.1    Khadatre, P.B.2    Roy, I.3
  • 107
    • 33846020543 scopus 로고    scopus 로고
    • Small molecule pharmacological chaperones: From thermodynamic stabilization to pharmaceutical drugs
    • Arakawa, T., Ejima, D., Kita, Y. and Tsumoto, K., Small molecule pharmacological chaperones: From thermodynamic stabilization to pharmaceutical drugs. Biochim. Biophys. Acta, 2006, 1764, 1677-1687.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1677-1687
    • Arakawa, T.1    Ejima, D.2    Kita, Y.3    Tsumoto, K.4
  • 108
    • 33745091537 scopus 로고    scopus 로고
    • Therapy through chaperones: sense or anti-sense? Cystic fibrosis as a model disease
    • Amaral, M. D., Therapy through chaperones: sense or anti-sense? Cystic fibrosis as a model disease. J. Inherit. Metab. Dis., 2006, 29, 477-487.
    • (2006) J. Inherit. Metab. Dis. , vol.29 , pp. 477-487
    • Amaral, M.D.1
  • 109
    • 34547105186 scopus 로고    scopus 로고
    • Chemical and pharmacological chaperones as new therapeutic agents
    • Loo, T. W. and Clarke, D. M., Chemical and pharmacological chaperones as new therapeutic agents. Expert Rev. Mol. Med., 2007, 9, 1-18.
    • (2007) Expert Rev. Mol. Med. , vol.9 , pp. 1-18
    • Loo, T.W.1    Clarke, D.M.2
  • 110
    • 28244502156 scopus 로고    scopus 로고
    • Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses
    • Johnson, S. M., Wiseman, R. L., Sekijima, Y., Green, N. S., Adamski-Werner, S. L. and Kelly, J. W., Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses. Acc. Chem. Res., 2005, 38, 911-921.
    • (2005) Acc. Chem. Res. , vol.38 , pp. 911-921
    • Johnson, S.M.1    Wiseman, R.L.2    Sekijima, Y.3    Green, N.S.4    Adamski-Werner, S.L.5    Kelly, J.W.6
  • 111
    • 33748801230 scopus 로고    scopus 로고
    • The iminosugar isofagomine increases the activity of N370S mutant acid beta-glucosidase in Gaucher fibroblasts by several mechanisms
    • Steet, R. A., Chung, S., Wustman, B., Powe, A., Do, H. and Kornfeld, S. A., The iminosugar isofagomine increases the activity of N370S mutant acid beta-glucosidase in Gaucher fibroblasts by several mechanisms. Proc. Natl. Acad. Sci. USA, 2006, 103, 13813-13818.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13813-13818
    • Steet, R.A.1    Chung, S.2    Wustman, B.3    Powe, A.4    Do, H.5    Kornfeld, S.A.6
  • 112
    • 34748866532 scopus 로고    scopus 로고
    • Active-site-specific chaperone therapy for Fabry disease
    • Fan, J. Q. and Ishii, S., Active-site-specific chaperone therapy for Fabry disease. Yin and Yang of enzyme inhibitors. FEBS J., 2007, 274, 4962-4971.
    • (2007) Yin and Yang of enzyme inhibitors. FEBS J. , vol.274 , pp. 4962-4971
    • Fan, J.Q.1    Ishii, S.2
  • 113
    • 70350336920 scopus 로고    scopus 로고
    • Correlation of clinical outcomes and disease burden in patients with transthyretin (TTR) amyloid polyneuropathy: study Fx-005, a landmark clinical trail of Fx-1006A, a novel small molecule TTR stabilizer
    • Coelho, T., Waddington-Cruz, M., Planté-Bordeneuve, V., Cros, D., Roy Grogan, D. and Packman, J., Correlation of clinical outcomes and disease burden in patients with transthyretin (TTR) amyloid polyneuropathy: study Fx-005, a landmark clinical trail of Fx-1006A, a novel small molecule TTR stabilizer. J. Neurol., 2008, 255, 78-85.
    • (2008) J. Neurol. , vol.255 , pp. 78-85
    • Coelho, T.1    Waddington-Cruz, M.2    Planté-Bordeneuve, V.3    Cros, D.4    Roy Grogan, D.5    Packman, J.6
  • 114
    • 41349085850 scopus 로고    scopus 로고
    • Treatment perspectives for the lysosomal storage diseases
    • Grabowski, G. A., Treatment perspectives for the lysosomal storage diseases. Expert Opin. Emerg. Drugs, 2008, 13, 197-211.
    • (2008) Expert Opin. Emerg. Drugs , vol.13 , pp. 197-211
    • Grabowski, G.A.1


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