메뉴 건너뛰기




Volumn 109, Issue 4, 2012, Pages 867-876

Development of thermostable Candida antarctica lipase B through novel in silico design of disulfide bridge

Author keywords

B factor of residue pairs; Candida antarctica lipase b; Disulfide bridge; Disulfide by design; Flexibility of residue pairs; MODIP; Thermal stability

Indexed keywords

B-FACTOR OF RESIDUE PAIRS; CANDIDA ANTARCTICA LIPASE B; DISULFIDE BRIDGE; FLEXIBILITY OF RESIDUE PAIRS; MODIP;

EID: 84857440017     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.24371     Document Type: Article
Times cited : (131)

References (41)
  • 1
    • 0000589822 scopus 로고    scopus 로고
    • Identification of the tliDEF ABC transporter specific for lipase in pseudomonas fluorescens SIK W1
    • Ahn JH, Pan JG, Rhee JS. 1999. Identification of the tliDEF ABC transporter specific for lipase in pseudomonas fluorescens SIK W1. J Bacteril 181(6): 1847-1852.
    • (1999) J Bacteril , vol.181 , Issue.6 , pp. 1847-1852
    • Ahn, J.H.1    Pan, J.G.2    Rhee, J.S.3
  • 2
    • 0141506109 scopus 로고    scopus 로고
    • TM: A computational method for the rational design of disulfide bonds in proteins
    • TM: A computational method for the rational design of disulfide bonds in proteins. Bioinformatics 19(14): 1852-1853.
    • (2003) Bioinformatics , vol.19 , Issue.14 , pp. 1852-1853
    • Dombkowski, A.A.1
  • 3
    • 0031795317 scopus 로고    scopus 로고
    • One biocatalyst-many applications: The use of Candida antarctica B-lipase in organic synthesis
    • Anderson EM, Larsson KM, Kirk O. 1998. One biocatalyst-many applications: The use of Candida antarctica B-lipase in organic synthesis. Biocatal Biotransform 16: 181-204.
    • (1998) Biocatal Biotransform , vol.16 , pp. 181-204
    • Anderson, E.M.1    Larsson, K.M.2    Kirk, O.3
  • 4
    • 0016411482 scopus 로고
    • Experimental and theoretical aspects of protein folding
    • Anfinsen CB, Scheraga HA. 1975. Experimental and theoretical aspects of protein folding. Adv Protein Chem 29: 205-300.
    • (1975) Adv Protein Chem , vol.29 , pp. 205-300
    • Anfinsen, C.B.1    Scheraga, H.A.2
  • 5
    • 0027155577 scopus 로고
    • Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
    • Clarke J, Fersht AR. 1993. Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation. Biochemistry 32: 4322-4329.
    • (1993) Biochemistry , vol.32 , pp. 4322-4329
    • Clarke, J.1    Fersht, A.R.2
  • 6
    • 0037880487 scopus 로고    scopus 로고
    • MODIP revisited: Re-evaluation and refinement of an automated procedure for modeling of disulfide bonds in proteins
    • Dani VS, Ramakrishnan C, Varadarajan R. 2003. MODIP revisited: Re-evaluation and refinement of an automated procedure for modeling of disulfide bonds in proteins. Protein Eng 16(3): 187-193.
    • (2003) Protein Eng , vol.16 , Issue.3 , pp. 187-193
    • Dani, V.S.1    Ramakrishnan, C.2    Varadarajan, R.3
  • 8
    • 77957948190 scopus 로고    scopus 로고
    • Generating stereochemically acceptable protein pathways
    • Farrell DW, Speranskiy K, Thorpe MF. 2010. Generating stereochemically acceptable protein pathways. Proteins 78: 2908-2921.
    • (2010) Proteins , vol.78 , pp. 2908-2921
    • Farrell, D.W.1    Speranskiy, K.2    Thorpe, M.F.3
  • 9
    • 73349137655 scopus 로고    scopus 로고
    • Enhancing thermostability of a Rhizomucor miehei lipase by engineering a disulfide bond and displaying on the yeast cell surface
    • Han Z, Han S, Zheng S, Lin Y. 2009. Enhancing thermostability of a Rhizomucor miehei lipase by engineering a disulfide bond and displaying on the yeast cell surface. Appl Microbiol Biotechnol 85: 117-126.
    • (2009) Appl Microbiol Biotechnol , vol.85 , pp. 117-126
    • Han, Z.1    Han, S.2    Zheng, S.3    Lin, Y.4
  • 10
    • 65549090562 scopus 로고    scopus 로고
    • Ring-opening polymerization of DD-lactide catalyzed by novozyme 435
    • Hans M, Keul H, Moeller M. 2009. Ring-opening polymerization of DD-lactide catalyzed by novozyme 435. Macromol Biosci 9: 239-247.
    • (2009) Macromol Biosci , vol.9 , pp. 239-247
    • Hans, M.1    Keul, H.2    Moeller, M.3
  • 13
    • 77249085574 scopus 로고    scopus 로고
    • Thermostabilization of Bacillus circulans xylanase via computational design of a flexible surface cavity
    • Joo JC, Pohkrel S, Pack SP, Yoo YJ. 2010. Thermostabilization of Bacillus circulans xylanase via computational design of a flexible surface cavity. J Biotechnol 146: 31-39.
    • (2010) J Biotechnol , vol.146 , pp. 31-39
    • Joo, J.C.1    Pohkrel, S.2    Pack, S.P.3    Yoo, Y.J.4
  • 14
    • 78650678219 scopus 로고    scopus 로고
    • Thermostabilization of Bacillus circulans xylanase: Computational optimization of unstable residues based on thermal fluctuation analysis
    • Joo JC, Pack SP, Kim YH, Yoo YJ. 2011. Thermostabilization of Bacillus circulans xylanase: Computational optimization of unstable residues based on thermal fluctuation analysis. J Biotechnol 151: 56-65.
    • (2011) J Biotechnol , vol.151 , pp. 56-65
    • Joo, J.C.1    Pack, S.P.2    Kim, Y.H.3    Yoo, Y.J.4
  • 15
    • 33846219593 scopus 로고    scopus 로고
    • Engineering a de novo internal disulfide bridge to improve the thermal stability of xylanase from Bacillus stearothermophilus No. 236
    • Jeong M, Kim S, Yun C, Choi Y, Cho S. 2007. Engineering a de novo internal disulfide bridge to improve the thermal stability of xylanase from Bacillus stearothermophilus No. 236. J Biotechnol 127: 300-309.
    • (2007) J Biotechnol , vol.127 , pp. 300-309
    • Jeong, M.1    Kim, S.2    Yun, C.3    Choi, Y.4    Cho, S.5
  • 16
    • 43149089848 scopus 로고    scopus 로고
    • Improving the expression yield of Candida antarctica lipase B in Escherichia coli by mutagenesis
    • Jung S, Park S. 2008. Improving the expression yield of Candida antarctica lipase B in Escherichia coli by mutagenesis. Biotechnol Lett 30: 717-722.
    • (2008) Biotechnol Lett , vol.30 , pp. 717-722
    • Jung, S.1    Park, S.2
  • 18
    • 77953621626 scopus 로고    scopus 로고
    • Development of thermostable lipase B from Candida antarctica (CalB) through in silico design employing B-factor and RosettaDesign
    • Kim HS, Le QAT, Kim YH. 2010. Development of thermostable lipase B from Candida antarctica (CalB) through in silico design employing B-factor and RosettaDesign. Enzyme Microb Technol 47: 1-5.
    • (2010) Enzyme Microb Technol , vol.47 , pp. 1-5
    • Kim, H.S.1    Le, Q.A.T.2    Kim, Y.H.3
  • 19
    • 35448955322 scopus 로고    scopus 로고
    • Lipase-catalyzed synthesis of glycerol carbonate from renewable glycerol and dimethyl carbonate through transesterification
    • Kim SC, Kim YH, Lee H, Yoon DY, Song BK. 2007. Lipase-catalyzed synthesis of glycerol carbonate from renewable glycerol and dimethyl carbonate through transesterification. J Mol Catal B: Enzym 49: 75-78.
    • (2007) J Mol Catal B: Enzym , vol.49 , pp. 75-78
    • Kim, S.C.1    Kim, Y.H.2    Lee, H.3    Yoon, D.Y.4    Song, B.K.5
  • 20
    • 0036327837 scopus 로고    scopus 로고
    • Lipases from Candida antarctica: Unique biocatalysts from a unique origin
    • Kirk O, Christensen WM. 2002. Lipases from Candida antarctica: Unique biocatalysts from a unique origin. Org Process Res Dev 6: 446-451.
    • (2002) Org Process Res Dev , vol.6 , pp. 446-451
    • Kirk, O.1    Christensen, W.M.2
  • 21
    • 0036178806 scopus 로고    scopus 로고
    • Immobilized Candida antarctica lipase-catalyzed alcoholysis of cotton seed oil in a solvent-free medium
    • Köse Ö, Tüter M, Aksoy HA. 2002. Immobilized Candida antarctica lipase-catalyzed alcoholysis of cotton seed oil in a solvent-free medium. Bioresour Technol 83: 125-129.
    • (2002) Bioresour Technol , vol.83 , pp. 125-129
    • Köse, O.1    Tüter, M.2    Aksoy, H.A.3
  • 22
    • 0024564552 scopus 로고
    • Control of enzyme activity by an engineering disulfide bond
    • Matsumara M, Mathews BW. 1989. Control of enzyme activity by an engineering disulfide bond. Science 243(4892): 792-794.
    • (1989) Science , vol.243 , Issue.4892 , pp. 792-794
    • Matsumara, M.1    Mathews, B.W.2
  • 24
    • 0032472401 scopus 로고    scopus 로고
    • Enantioselectivity of Candida antarctica lipase for some synthetic substrates including aliphatic secondary alcohols
    • Ohtani T, Nakatsukasa H, Kamezawa M, Tachibana H, Naoshima Y. 1998. Enantioselectivity of Candida antarctica lipase for some synthetic substrates including aliphatic secondary alcohols. J Mol Catal B: Enzym 4: 53-60.
    • (1998) J Mol Catal B: Enzym , vol.4 , pp. 53-60
    • Ohtani, T.1    Nakatsukasa, H.2    Kamezawa, M.3    Tachibana, H.4    Naoshima, Y.5
  • 25
    • 0033955909 scopus 로고    scopus 로고
    • Protein thermal stability: Insights from atomic displacement parameters (B values)
    • Parthasarathy S, Murthy MR. 2000. Protein thermal stability: Insights from atomic displacement parameters (B values). Protein Eng 13(1): 9-13.
    • (2000) Protein Eng , vol.13 , Issue.1 , pp. 9-13
    • Parthasarathy, S.1    Murthy, M.R.2
  • 26
    • 33847757782 scopus 로고    scopus 로고
    • The dependence of enzyme activity on temperature: Determination and validation of parameters
    • Peterson ME, Daniel RM, Danson MJ, Eisenthal R. 2007. The dependence of enzyme activity on temperature: Determination and validation of parameters. Biochem J 402: 331-337.
    • (2007) Biochem J , vol.402 , pp. 331-337
    • Peterson, M.E.1    Daniel, R.M.2    Danson, M.J.3    Eisenthal, R.4
  • 28
    • 0034237295 scopus 로고    scopus 로고
    • Lower kinetic limit to protein thermal stability: A proposal regarding protein stability in vivo and its relation with misfolding diseases
    • Plaza del Pino IM, Ibarra-Molero B, Sanchez-Ruiz JM. 2000. Lower kinetic limit to protein thermal stability: A proposal regarding protein stability in vivo and its relation with misfolding diseases. Proteins 40: 58-70.
    • (2000) Proteins , vol.40 , pp. 58-70
    • Plaza del Pino, I.M.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3
  • 30
    • 33845288649 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis on the basis of B-factors as a strategy for increasing protein thermostability
    • Reetz MT, Carballeira JD, Vogel A. 2006. Iterative saturation mutagenesis on the basis of B-factors as a strategy for increasing protein thermostability. Angew Chem Int Ed 45: 7745-7751.
    • (2006) Angew Chem Int Ed , vol.45 , pp. 7745-7751
    • Reetz, M.T.1    Carballeira, J.D.2    Vogel, A.3
  • 33
    • 33745328074 scopus 로고    scopus 로고
    • The effect of engineered disulfide bonds on the stability of Drosophila melanogaster acetylcholinesterase
    • Siadat OR, Lougarre A, Lamouroux L, Ladurantie C, Fournier D. 2006. The effect of engineered disulfide bonds on the stability of Drosophila melanogaster acetylcholinesterase. BMC Biochem 7: 12.
    • (2006) BMC Biochem , vol.7 , pp. 12
    • Siadat, O.R.1    Lougarre, A.2    Lamouroux, L.3    Ladurantie, C.4    Fournier, D.5
  • 34
    • 0024818499 scopus 로고
    • Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis
    • Sowdhamini R, Srinivasan N, Schoichet B, Santi DV, Ramakrishman C, Balaram P. 1989. Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis. Protein Eng 3: 95-103.
    • (1989) Protein Eng , vol.3 , pp. 95-103
    • Sowdhamini, R.1    Srinivasan, N.2    Schoichet, B.3    Santi, D.V.4    Ramakrishman, C.5    Balaram, P.6
  • 35
    • 0035370202 scopus 로고    scopus 로고
    • A combination of weakly stabilizing mutations with a disulfide bridge in the α-helix region of Trichoderma reesei endo-1,4-β-xylanase II increase the thermal stability through synergism
    • Turunen O, Ethuaho K, Fenel F, Vehmaanperä J, Wu X, Rouvinen J, Leisola M. 2001. A combination of weakly stabilizing mutations with a disulfide bridge in the α-helix region of Trichoderma reesei endo-1, 4-β-xylanase II increase the thermal stability through synergism. J Biotechnol 88: 37-46.
    • (2001) J Biotechnol , vol.88 , pp. 37-46
    • Turunen, O.1    Ethuaho, K.2    Fenel, F.3    Vehmaanperä, J.4    Wu, X.5    Rouvinen, J.6    Leisola, M.7
  • 36
    • 0028773288 scopus 로고
    • The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
    • Uppenberg J, Hansen TM, Patkar S, Jones AT. 1994. The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica Structure 2: 293-308.
    • (1994) Structure , vol.2 , pp. 293-308
    • Uppenberg, J.1    Hansen, T.M.2    Patkar, S.3    Jones, A.T.4
  • 38
    • 0022998684 scopus 로고
    • In Vivo formation and stability of engineered disulfide bonds in Subtilisin
    • Wells JA, Powers DB. 1986. In Vivo formation and stability of engineered disulfide bonds in Subtilisin. J Biol Chem 261(14): 6564-6570.
    • (1986) J Biol Chem , vol.261 , Issue.14 , pp. 6564-6570
    • Wells, J.A.1    Powers, D.B.2
  • 40
    • 0347915684 scopus 로고    scopus 로고
    • High efficiency transformation by electroporation of Pichia pastoris pretreated with lithium acetate and dithiothreitol
    • Wu S, Letchworth GJ. 2004. High efficiency transformation by electroporation of Pichia pastoris pretreated with lithium acetate and dithiothreitol. Biotechniques 36(1): 152-154.
    • (2004) Biotechniques , vol.36 , Issue.1 , pp. 152-154
    • Wu, S.1    Letchworth, G.J.2
  • 41
    • 0141817121 scopus 로고    scopus 로고
    • Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution
    • Zhang N, Suen W, Windsor W, Xiao L, Madison V, Zaks A. 2003. Improving tolerance of Candida antarctica lipase B towards irreversible thermal inactivation through directed evolution. Protein Eng 16(8): 599-605.
    • (2003) Protein Eng , vol.16 , Issue.8 , pp. 599-605
    • Zhang, N.1    Suen, W.2    Windsor, W.3    Xiao, L.4    Madison, V.5    Zaks, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.