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Volumn 148, Issue 2, 2010, Pages 231-238

Enhanced activity and stability in the presence of organic solvents by increased active site polarity and stabilization of a surface loop in a metalloprotease

Author keywords

activity and stability; organic solvent; site directed mutagenesis; zinc metalloprotease

Indexed keywords

2 PROPANOL; METALLOPROTEINASE; METHANOL; N,N DIMETHYLFORMAMIDE; ORGANIC SOLVENT; PROPANOL;

EID: 77955207297     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvq057     Document Type: Article
Times cited : (29)

References (48)
  • 1
    • 0041152088 scopus 로고    scopus 로고
    • Properties and synthetic applications of enzymes in organic solvents
    • Carrea, G. and Riva, S. (2000) Properties and synthetic applications of enzymes in organic solvents. Angew. Chem. Int. 39, 2226-2254
    • (2000) Angew. Chem. Int. , vol.39 , pp. 2226-2254
    • Carrea, G.1    Riva, S.2
  • 2
    • 33645229314 scopus 로고    scopus 로고
    • The expanding roles of biocatalysis and biotransformation
    • DeSantis, G. and Davis, B.G. (2006) The expanding roles of biocatalysis and biotransformation. Curr. Opin. Chem. Biol. 10, 139-140
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 139-140
    • Desantis, G.1    Davis, B.G.2
  • 3
    • 0032513138 scopus 로고    scopus 로고
    • Stereoselective synthesis of biologically active tetronic acids
    • Effenberger, F. and Syed, J. (1998) Stereoselective synthesis of biologically active tetronic acids. Tetrahedron: Asymmetry 9, 817-825
    • (1998) Tetrahedron: Asymmetry , vol.9 , pp. 817-825
    • Effenberger, F.1    Syed, J.2
  • 4
    • 0033429257 scopus 로고    scopus 로고
    • Application of pig liver esterase catalyzed transesterification in organic media to the kinetic resolution of glycerol derivatives
    • Jungen, M. and Gais, H. (1999) Application of pig liver esterase catalyzed transesterification in organic media to the kinetic resolution of glycerol derivatives. Tetrahedron: Asymmetry. 10, 3747-58
    • (1999) Tetrahedron: Asymmetry. , vol.10 , pp. 3747-3758
    • Jungen, M.1    Gais, H.2
  • 5
    • 0031465724 scopus 로고    scopus 로고
    • Enantioselective synthesis of unsaturated a-hydroxy acids
    • Macritchie, J.A., Silcock, A., and Willis, C.L. (1997) Enantioselective synthesis of unsaturated a-hydroxy acids. Tetrahedron: Asymmetry. 8, 3895-3902
    • (1997) Tetrahedron: Asymmetry , vol.8 , pp. 3895-3902
    • MacRitchie, J.A.1    Silcock, A.2    Willis, C.L.3
  • 6
    • 0030052863 scopus 로고    scopus 로고
    • Probing the abilities of synthetically useful serine proteases to discriminate between the configurations of remote stereocenters using chiral aldehyde inhibitors
    • Lee, T. and Jones, J.B. (1996) Probing the abilities of synthetically useful serine proteases to discriminate between the configurations of remote stereocenters using chiral aldehyde inhibitors. J. Am. Chem. Soc. 118, 502-508
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 502-508
    • Lee, T.1    Jones, J.B.2
  • 7
    • 0034811393 scopus 로고    scopus 로고
    • Structure and activity of a-chymotrypsin and trypsin in aqueous organic media
    • Simon, L.M., Kotorman, M., Garab, G., and Laczko, I. (2001) Structure and Activity of a-Chymotrypsin and Trypsin in Aqueous Organic Media. Biochem. Biophys. Res. Commun. 280, 1367-1371
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 1367-1371
    • Simon, L.M.1    Kotorman, M.2    Garab, G.3    Laczko, I.4
  • 8
    • 0036882398 scopus 로고    scopus 로고
    • Proteases in Organic Synthesis
    • Bordusa, F. (2002) Proteases in Organic Synthesis. Chem. Rev. 102, 4817-4867
    • (2002) Chem. Rev. , vol.102 , pp. 4817-4867
    • Bordusa, F.1
  • 9
    • 0026334373 scopus 로고
    • Enzyme engineering for nonaqueous solvents: Random mutagenesis to enhance activity of subtilisin e in polar organic media
    • Chen, K. and Arnold, F.H. (1991) Enzyme engineering for nonaqueous solvents: random mutagenesis to enhance activity of subtilisin E in polar organic media. Biotechnology 9, 1073-1077
    • (1991) Biotechnology , vol.9 , pp. 1073-1077
    • Chen, K.1    Arnold, F.H.2
  • 10
    • 0027205210 scopus 로고
    • Tuning the activity of an enzyme for unusual environments: Sequential random mutagenesis of subtilisin e for catalysis in dimethylformamide
    • Chen, K. and Arnold, F.H. (1993) Tuning the activity of an enzyme for unusual environments: sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide. Proc. Natl Acad. Sci. USA, 90, 5618-5622
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5618-5622
    • Chen, K.1    Arnold, F.H.2
  • 11
    • 0026124848 scopus 로고
    • Enzyme engineering for nonaqueous solvents. II. Additive effects of mutations on the stability and activity of subtilisin e in polar organic media
    • Chen, K., Robinson, A.C., Van Dam, M.E., Martinez, P., Economou, C., and Arnold, F.H. (1991) Enzyme engineering for nonaqueous solvents. II. Additive effects of mutations on the stability and activity of subtilisin E in polar organic media. Biotechnol. Prog. 7, 125-129
    • (1991) Biotechnol. Prog. , vol.7 , pp. 125-129
    • Chen, K.1    Robinson, A.C.2    Van Dam, M.E.3    Martinez, P.4    Economou, C.5    Arnold, F.H.6
  • 12
    • 0029670577 scopus 로고    scopus 로고
    • Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents
    • Moore, J.C. and Arnold, F.H. (1996) Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents. Nat. Biotechnol. 14, 458-467
    • (1996) Nat. Biotechnol. , vol.14 , pp. 458-467
    • Moore, J.C.1    Arnold, F.H.2
  • 13
    • 0024962392 scopus 로고
    • Large increases in general stability for subtilisin BPN' through incremental change in the free energy of unfolding
    • Pantoliano, M.W., Whitlow, M., Wood, J.F., Dodd, S.W., Hardman, K.D., Rollence, M.L., and Bryan, P.N. (1989) Large increases in general stability for subtilisin BPN' through incremental change in the free energy of unfolding. Biochemistry 28, 7205-7213
    • (1989) Biochemistry , vol.28 , pp. 7205-7213
    • Pantoliano, M.W.1    Whitlow, M.2    Wood, J.F.3    Dodd, S.W.4    Hardman, K.D.5    Rollence, M.L.6    Bryan, P.N.7
  • 14
    • 0035844691 scopus 로고    scopus 로고
    • Enhancement of stability and activity of phospholipase A1 in organic solvents by directed evolution
    • Song, J.K. and Rhee, J.S. (2001) Enhancement of stability and activity of phospholipase A1 in organic solvents by directed evolution. Biochim. Biophys. Acta. 1547, 370-378
    • (2001) Biochim. Biophys. Acta. , vol.1547 , pp. 370-378
    • Song, J.K.1    Rhee, J.S.2
  • 16
    • 0029969577 scopus 로고    scopus 로고
    • Directed evolution of subtilisin e in Bacillus subtilis to enhance total activity in aqueous dimethylformamide
    • You, L. and Arnold, F.H. (1996) Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide. Protein Eng. 9, 77-83
    • (1996) Protein Eng. , vol.9 , pp. 77-83
    • You, L.1    Arnold, F.H.2
  • 17
    • 40549120904 scopus 로고    scopus 로고
    • A stable serine protease, Wrightin, from the latex of the plant Wrightia tinctoria (Roxb.) R. Br.: Purification and biochemical properties
    • Tomar, R., Kumar, R., and Jagannadham, M.V. (2008) A stable serine protease, Wrightin, from the latex of the plant Wrightia tinctoria (Roxb.) R. Br.: purification and biochemical properties. J. Agric. Food. Chem. 56, 1479-1487
    • (2008) J. Agric. Food. Chem. , vol.56 , pp. 1479-1487
    • Tomar, R.1    Kumar, R.2    Jagannadham, M.V.3
  • 18
    • 33847155508 scopus 로고    scopus 로고
    • Stabilities and conformational transitions of various proteases in the presence of an organic solvent
    • Ogino, H., Gemba, Y., Yutori, Y., Doukyu, N., Ishimi, K., and Ishikawa, H. (2007) Stabilities and conformational transitions of various proteases in the presence of an organic solvent. Biotechnol. Prog. 23, 155-161
    • (2007) Biotechnol. Prog. , vol.23 , pp. 155-161
    • Ogino, H.1    Gemba, Y.2    Yutori, Y.3    Doukyu, N.4    Ishimi, K.5    Ishikawa, H.6
  • 19
    • 0026489329 scopus 로고
    • Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis
    • Holland, D.R., Tronrud, D.E., Pley, H.W., Flaherty, K.M., Stark, W., Jansonius, J.N., McKay, D.B., and Matthews, B.W. (1992) Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis. Biochemistry 31, 11310-11316
    • (1992) Biochemistry , vol.31 , pp. 11310-11316
    • Holland, D.R.1    Tronrud, D.E.2    Pley, H.W.3    Flaherty, K.M.4    Stark, W.5    Jansonius, J.N.6    McKay, D.B.7    Matthews, B.W.8
  • 20
    • 37549005219 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of a novel zinc-metalloprotease gene from the Salinivibrio sp. strain AF-2004 and its extracellular expression in E. coli
    • Karbalaei-Heidari, H.R., Ziaee, A.A., Amoozegar, M.A., Cheburkin, Y., and Budisa, N. (2008) Molecular cloning and sequence analysis of a novel zinc-metalloprotease gene from the Salinivibrio sp. strain AF-2004 and its extracellular expression in E. coli. Gene. 408, 196-203
    • (2008) Gene. , vol.408 , pp. 196-203
    • Karbalaei-Heidari, H.R.1    Ziaee, A.A.2    Amoozegar, M.A.3    Cheburkin, Y.4    Budisa, N.5
  • 21
    • 0032712358 scopus 로고    scopus 로고
    • Alkaliphiles: Some applications of their products for biotechnology
    • Horikoshi, K. (1999) Alkaliphiles: some applications of their products for biotechnology. Microbiol. Mol. Biol. Rev. 63, 735-750
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 735-750
    • Horikoshi, K.1
  • 22
    • 0343471377 scopus 로고    scopus 로고
    • Modification of a PCR based site-directed mutagenesis method
    • Fisher, C.L. and Pei, G.K. (1997) Modification of a PCR based site-directed mutagenesis method. Biotechniques. 23, 570-574
    • (1997) Biotechniques. , vol.23 , pp. 570-574
    • Fisher, C.L.1    Pei, G.K.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 34748868292 scopus 로고    scopus 로고
    • Effects of site-directed mutagenesis of the the surface residues Gln128 and Gln225 of thermolysin on its catalytic activity
    • Tatsumi, C., Hashida, Y., Yasukawa, K., and Inouye, K. (2007) Effects of site-directed mutagenesis of the the surface residues Gln128 and Gln225 of thermolysin on its catalytic activity. J. Biochem. 141, 835-842
    • (2007) J. Biochem. , vol.141 , pp. 835-842
    • Tatsumi, C.1    Hashida, Y.2    Yasukawa, K.3    Inouye, K.4
  • 26
    • 34748871409 scopus 로고    scopus 로고
    • Improving the activity and stability of thermolysin by site-directed mutagenesis
    • Yasukawa, K. and Inouye, K. (2007) Improving the activity and stability of thermolysin by site-directed mutagenesis. Biochim. Biophys. Acta. 1774, 1281-1288
    • (2007) Biochim. Biophys. Acta. , vol.1774 , pp. 1281-1288
    • Yasukawa, K.1    Inouye, K.2
  • 27
    • 0026799337 scopus 로고
    • Effects of salts on thermolysin: Activation of hydrolysis and synthesis ofN-carbobenzoxyl- aspartyl-l-phenylalanine methyl ester, and a unique change in the absorption spectrum of thermolysin
    • Inouye, K. (1992) Effects of salts on thermolysin: activation of hydrolysis and synthesis ofN-carbobenzoxyl- aspartyl-l-phenylalanine methyl ester, and a unique change in the absorption spectrum of thermolysin. J. Biochem. 112, 335-340
    • (1992) J. Biochem. , vol.112 , pp. 335-340
    • Inouye, K.1
  • 28
    • 0029863639 scopus 로고    scopus 로고
    • Effect of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts
    • Inouye, K., Lee, S.B., and Tonomura, B. (1996) Effect of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts. Biochem. J. 315, 133-138
    • (1996) Biochem. J. , vol.315 , pp. 133-138
    • Inouye, K.1    Lee, S.B.2    Tonomura, B.3
  • 29
    • 33645411423 scopus 로고    scopus 로고
    • Extracellular production of recombinant thermolysin expressed in Escherichia coli, and its purification and enzymatic characterization
    • Inouye, K., Minoda, M., Takita, T., Sakurama, H., Hashida, Y., Kusano, M., and Yasukawa, K. (2006) Extracellular production of recombinant thermolysin expressed in Escherichia coli, and its purification and enzymatic characterization. Protein Expr. Purif. 46, 248-255
    • (2006) Protein Expr. Purif. , vol.46 , pp. 248-255
    • Inouye, K.1    Minoda, M.2    Takita, T.3    Sakurama, H.4    Hashida, Y.5    Kusano, M.6    Yasukawa, K.7
  • 30
    • 33846251560 scopus 로고    scopus 로고
    • Effects of water-miscible solvents and polyhydroxy compounds on the structure and enzymatic activity of TLN
    • Pazhang, M., Khajeh, Kh., Ranjbar, B., and Hosseinkhani, S. (2006) Effects of water-miscible solvents and polyhydroxy compounds on the structure and enzymatic activity of TLN. J. Biotechnol. 127, 45-53
    • (2006) J. Biotechnol. , vol.127 , pp. 45-53
    • Pazhang, M.1    Khajeh, Kh.2    Ranjbar, B.3    Hosseinkhani, S.4
  • 31
    • 34249731337 scopus 로고    scopus 로고
    • Effect of exchange of amino acid residues of the surface region of the PST-01 protease on its organic solvent-stability
    • Ogino, H., Uchiho, T., Doukyu, N., Yasuda, M., Ishimi, K., and Ishikawa, H. (2007) Effect of exchange of amino acid residues of the surface region of the PST-01 protease on its organic solvent-stability. Biochem. Biophys. Res. Commun. 358, 1028-1033
    • (2007) Biochem. Biophys. Res. Commun. , vol.358 , pp. 1028-1033
    • Ogino, H.1    Uchiho, T.2    Doukyu, N.3    Yasuda, M.4    Ishimi, K.5    Ishikawa, H.6
  • 32
    • 0035140742 scopus 로고    scopus 로고
    • Role of intermolecular disulfide bonds of the organic solvent-stable PST-01 protease in its organic solvent stability
    • Ogino, H., Uchiho, T., Yokoo, J., Kobayashi, R., Ichise, R., and Ishikawa, H. (2001) Role of intermolecular disulfide bonds of the organic solvent-stable PST-01 protease in its organic solvent stability. Appl. Environ. Microbiol. 67, 942-947
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 942-947
    • Ogino, H.1    Uchiho, T.2    Yokoo, J.3    Kobayashi, R.4    Ichise, R.5    Ishikawa, H.6
  • 33
    • 0025906404 scopus 로고
    • Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5A resolution
    • Thayer, M.M., Flaherty, K.M., and McKay, D.B. (1991) Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5A resolution. J. Biol. Chem. 266, 2864-2871
    • (1991) J. Biol. Chem. , vol.266 , pp. 2864-2871
    • Thayer, M.M.1    Flaherty, K.M.2    McKay, D.B.3
  • 34
    • 0035526570 scopus 로고    scopus 로고
    • Environment of tryptophan 57 in porcine fructose-1,6-bisphosphatase studied by time-resolved fluorescence and site-directed mutagenesis
    • Wen, J., Nelson, S.W., Honzatko, R.B., Fromm, H.J., and Petrich, J.W. (2001) Environment of tryptophan 57 in porcine fructose-1,6-bisphosphatase studied by time-resolved fluorescence and site-directed mutagenesis. Photochem. Photobiol. 74, 679-85
    • (2001) Photochem. Photobiol. , vol.74 , pp. 679-685
    • Wen, J.1    Nelson, S.W.2    Honzatko, R.B.3    Fromm, H.J.4    Petrich, J.W.5
  • 35
    • 0024971021 scopus 로고
    • Stability and activity of a thermostable malic enzyme in denaturants and water-miscible organic solvents
    • Guagliardi, A., Manco, G., Rossi, M., and Bartolucci, S. (1989) Stability and activity of a thermostable malic enzyme in denaturants and water-miscible organic solvents. Eur. J. Biochem. 183, 25-30
    • (1989) Eur. J. Biochem. , vol.183 , pp. 25-30
    • Guagliardi, A.1    Manco, G.2    Rossi, M.3    Bartolucci, S.4
  • 36
    • 34447313904 scopus 로고    scopus 로고
    • The stability of engineered thermostable neutral proteases from Bacillus stearothermophilus in organic solvents and detergents
    • Mansfeld, J. and Ulbrich-Hofmann, R. (2007) The stability of engineered thermostable neutral proteases from Bacillus stearothermophilus in organic solvents and detergents. Biotechnol. Bioeng. 97, 672-679
    • (2007) Biotechnol. Bioeng. , vol.97 , pp. 672-679
    • Mansfeld, J.1    Ulbrich-Hofmann, R.2
  • 37
    • 2442551096 scopus 로고    scopus 로고
    • Polar organic solvent added to an aqueous solution changes hydrolytic property of lipase
    • Tsuzki, W., Ue, A., and Nagao, A. (2003) Polar organic solvent added to an aqueous solution changes hydrolytic property of lipase. Biosci. Biotechnol. Biochem. 67, 1660-1666
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 1660-1666
    • Tsuzki, W.1    Ue, A.2    Nagao, A.3
  • 39
    • 54249164978 scopus 로고    scopus 로고
    • Thermostable variants constructed via the structureguided consensus method also show increased stability in salts solutions and homogenous aqueous-organic media
    • Vazquez-Figueroa, E., Yeh, V., Broering, J.M., Chaparro-Riggers, J.F., and Bommarius, A.S. (2008) Thermostable variants constructed via the structureguided consensus method also show increased stability in salts solutions and homogenous aqueous-organic media. Protein Eng. Des. Selection 21, 673-680
    • (2008) Protein Eng. Des. Selection , vol.21 , pp. 673-680
    • Vazquez-Figueroa, E.1    Yeh, V.2    Broering, J.M.3    Chaparro-Riggers, J.F.4    Bommarius, A.S.5
  • 40
    • 0017230665 scopus 로고
    • Role of Calcium in the thermal stability of thermolysin
    • Dahlquist, F.W., Long, J.W., and Bigbee, W.L. (1976) Role of Calcium in the thermal stability of thermolysin. Biochemistry 15, 1103-1111
    • (1976) Biochemistry , vol.15 , pp. 1103-1111
    • Dahlquist, F.W.1    Long, J.W.2    Bigbee, W.L.3
  • 41
    • 0023038088 scopus 로고
    • A new way of enhancing the thermostability of proteases
    • Imanaka, T., Shibazaki, M., and Takagi, M. (1986) A new way of enhancing the thermostability of proteases. Nature 324, 695-697
    • (1986) Nature , vol.324 , pp. 695-697
    • Imanaka, T.1    Shibazaki, M.2    Takagi, M.3
  • 42
    • 0023830955 scopus 로고
    • Structure and stability of thermophilic enzymes. Studies on thermolysin
    • Fontana, A. (1988) Structure and stability of thermophilic enzymes. Studies on thermolysin. Biophys. Chem. 29, 181-193
    • (1988) Biophys. Chem. , vol.29 , pp. 181-193
    • Fontana, A.1
  • 43
    • 0027645554 scopus 로고
    • Prediction and analysis of structure, stability and unfolding of thermolysin-like proteases
    • Vriend, G. and Eijsink, V.G.H. (1993) Prediction and analysis of structure, stability and unfolding of thermolysin-like proteases. J. Comput. Aided. Mol. Des. 7, 367-396
    • (1993) J. Comput. Aided. Mol. Des. , vol.7 , pp. 367-396
    • Vriend, G.1    Eijsink, V.G.H.2
  • 45
    • 0035108407 scopus 로고    scopus 로고
    • Enzymes which are stable in the presence of organic solvents
    • Ogino, H. and Ishikawa, H. (2001) Enzymes which are stable in the presence of organic solvents. J. Biosci. Bioeng. 91, 109-116
    • (2001) J. Biosci. Bioeng. , vol.91 , pp. 109-116
    • Ogino, H.1    Ishikawa, H.2
  • 46
    • 33847653796 scopus 로고    scopus 로고
    • An engineered mutant, L307V of phenylalanine dehydrogenase from Bacillus sphaericus: High activity and stability in organic-aqueous solvent mixtures and utility for synthesis of non-natural L-amino acids
    • Chen, S. and Engel, P.C. (2007) An engineered mutant, L307V of phenylalanine dehydrogenase from Bacillus sphaericus: high activity and stability in organic-aqueous solvent mixtures and utility for synthesis of non-natural L-amino acids. Enzyme. Microb. Technol. 40, 1407-1411
    • (2007) Enzyme. Microb. Technol. , vol.40 , pp. 1407-1411
    • Chen, S.1    Engel, P.C.2
  • 47
    • 0006688434 scopus 로고    scopus 로고
    • Simultaneous enhancement of thermostability and catalytic activity of phospholipase A1 by evolutionary molecular engineering
    • Song, J.K. and Rhee, J.S. (2000) Simultaneous enhancement of thermostability and catalytic activity of phospholipase A1 by evolutionary molecular engineering. Appl. Environ. Microbiol. 66, 890-894
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 890-894
    • Song, J.K.1    Rhee, J.S.2


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