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Volumn 276, Issue 6, 2009, Pages 1750-1761

Engineering thermal stability of l-asparaginase by in vitro directed evolution

Author keywords

Directed evolution; Enzyme engineering; Leukaemia; Saturation mutagenesis; Thermal stability

Indexed keywords

AMMONIA; ASPARAGINASE; ASPARAGINE; LEUCINE;

EID: 61349130050     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.06910.x     Document Type: Article
Times cited : (86)

References (55)
  • 1
    • 0027536607 scopus 로고
    • L-Asparaginase and PEG asparaginase - Past, present, and future
    • Keating MJ, Holmes R, Lerner S Ho DH (1993) l-Asparaginase and PEG asparaginase - past, present, and future. Leuk Lymphoma 10, 153 157.
    • (1993) Leuk Lymphoma , vol.10 , pp. 153-157
    • Keating, M.J.1    Holmes, R.2    Lerner, S.3    Ho, D.H.4
  • 2
    • 0032145202 scopus 로고    scopus 로고
    • Use of l-asparaginase in childhood ALL
    • Muller HJ Boos J (1998) Use of l-asparaginase in childhood ALL. Crit Rev Oncol Hematol 28, 97 113.
    • (1998) Crit Rev Oncol Hematol , vol.28 , pp. 97-113
    • Muller, H.J.1    Boos, J.2
  • 3
    • 0026566378 scopus 로고
    • Enzymes as agents for the treatment of disease
    • Goldberg DM (1992) Enzymes as agents for the treatment of disease. Clin Chim Acta 206, 45 76.
    • (1992) Clin Chim Acta , vol.206 , pp. 45-76
    • Goldberg, D.M.1
  • 4
    • 0036973847 scopus 로고    scopus 로고
    • In vivo half life of nanoencapsulated l-asparaginase
    • Baran ET, Ozer N Hasirci V (2002) In vivo half life of nanoencapsulated l-asparaginase. J Mater Sci Mater Med 13, 1113 1121.
    • (2002) J Mater Sci Mater Med , vol.13 , pp. 1113-1121
    • Baran, E.T.1    Ozer, N.2    Hasirci, V.3
  • 5
    • 0014424759 scopus 로고
    • Asparagine synthetase in normal and malignant tissues: Correlation with tumor sensitivity to asparaginase
    • Prager MD Bachynsky N (1968) Asparagine synthetase in normal and malignant tissues: correlation with tumor sensitivity to asparaginase. Arch Biochem Biophys 127, 645 654.
    • (1968) Arch Biochem Biophys , vol.127 , pp. 645-654
    • Prager, M.D.1    Bachynsky, N.2
  • 6
    • 28844458850 scopus 로고    scopus 로고
    • Serum asparaginase activities and asparagine concentrations in the cerebrospinal fluid after a single infusion of 2,500 IU/m(2) PEG asparaginase in children with ALL treated according to protocol COALL-06-97
    • Vieira Pinheiro JP, Wenner K, Escherich G, Lanvers-Kaminsky C, Wurthwein G, Janka-Schaub G Boos J (2006) Serum asparaginase activities and asparagine concentrations in the cerebrospinal fluid after a single infusion of 2,500 IU/m(2) PEG asparaginase in children with ALL treated according to protocol COALL-06-97. Pediatr Blood Cancer 46, 18 25.
    • (2006) Pediatr Blood Cancer , vol.46 , pp. 18-25
    • Vieira Pinheiro, J.P.1    Wenner, K.2    Escherich, G.3    Lanvers-Kaminsky, C.4    Wurthwein, G.5    Janka-Schaub, G.6    Boos, J.7
  • 8
    • 0028069252 scopus 로고
    • Increased endogenous thrombin generation in children with acute lymphoblastic leukemia: Risk of thrombotic complications in l-asparaginase- induced antithrombin III deficiency
    • Mitchell L, Hoogendoorn H, Giles AR, Vegh P Andrew M (1994) Increased endogenous thrombin generation in children with acute lymphoblastic leukemia: risk of thrombotic complications in l-asparaginase-induced antithrombin III deficiency. Blood 83, 386 391.
    • (1994) Blood , vol.83 , pp. 386-391
    • Mitchell, L.1    Hoogendoorn, H.2    Giles, A.R.3    Vegh, P.4    Andrew, M.5
  • 9
    • 0028136892 scopus 로고
    • Erwinia chrysanthemil-asparaginase: Epitope mapping and production of antigenically modified enzymes
    • Moola ZB, Scawen MD, Atkinson T Nicholls DJ (1994) Erwinia chrysanthemil-asparaginase: epitope mapping and production of antigenically modified enzymes. Biochem J 302, 921 927.
    • (1994) Biochem J , vol.302 , pp. 921-927
    • Moola, Z.B.1    Scawen, M.D.2    Atkinson, T.3    Nicholls, D.J.4
  • 11
    • 5344224839 scopus 로고    scopus 로고
    • Extracellular expression and single step purification of recombinant Escherichia colil-asparaginase II
    • Khushoo A, Pal Y, Singh BN Mukherjee KJ (2004) Extracellular expression and single step purification of recombinant Escherichia colil-asparaginase II. Protein Expr Purif 38, 29 36.
    • (2004) Protein Expr Purif , vol.38 , pp. 29-36
    • Khushoo, A.1    Pal, Y.2    Singh, B.N.3    Mukherjee, K.J.4
  • 12
    • 50549191387 scopus 로고
    • Tumor inhibitory effect of l-asparaginase from Escherichia coli
    • Mashburn LT Wriston JC Jr. (1964) Tumor inhibitory effect of l-asparaginase from Escherichia coli. Arch Biochem Biophys 105, 450 452.
    • (1964) Arch Biochem Biophys , vol.105 , pp. 450-452
    • Mashburn, L.T.1    Wriston Jr., J.C.2
  • 13
    • 0016794183 scopus 로고
    • Comparative study on conformational stability and subunit interactions of two bacterial asparaginases
    • Marlborough DI, Miller DS Cammack KA (1975) Comparative study on conformational stability and subunit interactions of two bacterial asparaginases. Biochim Biophys Acta 386, 576 589.
    • (1975) Biochim Biophys Acta , vol.386 , pp. 576-589
    • Marlborough, D.I.1    Miller, D.S.2    Cammack, K.A.3
  • 14
    • 0037177490 scopus 로고    scopus 로고
    • Effects of polyethylene glycol attachment on physicochemical and biological stability of E. colil-asparaginase
    • Soares AL, Guimaraes GM, Polakiewicz B, de Moraes Pitombo RN Abrahao-Neto J (2002) Effects of polyethylene glycol attachment on physicochemical and biological stability of E. colil-asparaginase. Int J Pharm 237, 163 170.
    • (2002) Int J Pharm , vol.237 , pp. 163-170
    • Soares, A.L.1    Guimaraes, G.M.2    Polakiewicz, B.3    De Moraes Pitombo, R.N.4    Abrahao-Neto, J.5
  • 15
    • 24944555774 scopus 로고    scopus 로고
    • Cloning, expression and characterization of Erwinia carotovoral- asparaginase
    • Kotzia GA Labrou NE (2005) Cloning, expression and characterization of Erwinia carotovoral-asparaginase. J Biotechnol 119, 309 323.
    • (2005) J Biotechnol , vol.119 , pp. 309-323
    • Kotzia, G.A.1    Labrou, N.E.2
  • 16
    • 33845649780 scopus 로고    scopus 로고
    • L-Asparaginase from Erwinia chrysanthemi 3937: Cloning, expression and characterization
    • Kotzia GA Labrou NE (2007) l-Asparaginase from Erwinia chrysanthemi 3937: cloning, expression and characterization. J Biotechnol 127, 657 669.
    • (2007) J Biotechnol , vol.127 , pp. 657-669
    • Kotzia, G.A.1    Labrou, N.E.2
  • 17
    • 0014048162 scopus 로고
    • Suppression of murine leukemias by l-asparaginase. Incidence of sensitivity among leukemias of various types: Comparative inhibitory activities of guinea pig serum l-asparaginase and Escherichia colil-asparaginase
    • Boyse EA, Old LJ, Campbell HA Mashburn LT (1967) Suppression of murine leukemias by l-asparaginase. Incidence of sensitivity among leukemias of various types: comparative inhibitory activities of guinea pig serum l-asparaginase and Escherichia colil-asparaginase. J Exp Med 125, 17 31.
    • (1967) J Exp Med , vol.125 , pp. 17-31
    • Boyse, E.A.1    Old, L.J.2    Campbell, H.A.3    Mashburn, L.T.4
  • 18
    • 0030835335 scopus 로고    scopus 로고
    • Polysialylated asparaginase: Preparation, activity and pharmacokinetics
    • Fernandes AI Gregoriadis G (1997) Polysialylated asparaginase: preparation, activity and pharmacokinetics. Biochim Biophys Acta 1341, 26 34.
    • (1997) Biochim Biophys Acta , vol.1341 , pp. 26-34
    • Fernandes, A.I.1    Gregoriadis, G.2
  • 19
    • 0027982957 scopus 로고
    • Polymers for delivering peptides and proteins
    • Burnham NL (1994) Polymers for delivering peptides and proteins. Am J Hosp Pharm 51, 210 218.
    • (1994) Am J Hosp Pharm , vol.51 , pp. 210-218
    • Burnham, N.L.1
  • 20
    • 26944452043 scopus 로고    scopus 로고
    • PEGylation, successful approach to drug delivery
    • Veronese FM Pasut G (2005) PEGylation, successful approach to drug delivery. Drug Discov Today 10, 1451 1458.
    • (2005) Drug Discov Today , vol.10 , pp. 1451-1458
    • Veronese, F.M.1    Pasut, G.2
  • 21
    • 34249812940 scopus 로고    scopus 로고
    • Tailoring structure-function properties of l-asparaginase: Engineering resistance to trypsin cleavage
    • Kotzia GA, Lappa K Labrou NE (2007) Tailoring structure-function properties of l-asparaginase: engineering resistance to trypsin cleavage. Biochem J 404, 337 343.
    • (2007) Biochem J , vol.404 , pp. 337-343
    • Kotzia, G.A.1    Lappa, K.2    Labrou, N.E.3
  • 22
    • 4143143467 scopus 로고    scopus 로고
    • Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface
    • Bjork A, Dalhus B, Mantzilas D, Sirevag R Eijsink VGH (2004) Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface. J Mol Biol 341, 1215 1226.
    • (2004) J Mol Biol , vol.341 , pp. 1215-1226
    • Bjork, A.1    Dalhus, B.2    Mantzilas, D.3    Sirevag, R.4    Eijsink, V.G.H.5
  • 25
    • 0036699655 scopus 로고    scopus 로고
    • Improvement of oxidative and thermostability of N-carbamyl-d-amino acid amidohydrolase by directed evolution
    • Oh KH, Nam SH Kim HS (2002) Improvement of oxidative and thermostability of N-carbamyl-d-amino acid amidohydrolase by directed evolution. Protein Eng 15, 689 695.
    • (2002) Protein Eng , vol.15 , pp. 689-695
    • Oh, K.H.1    Nam, S.H.2    Kim, H.S.3
  • 26
    • 18044366809 scopus 로고    scopus 로고
    • A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents
    • Hao J Berry A (2004) A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents. Protein Eng Des Sel 17, 689 697.
    • (2004) Protein Eng des Sel , vol.17 , pp. 689-697
    • Hao, J.1    Berry, A.2
  • 30
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov PL Gill SJ (1988) Stability of protein structure and hydrophobic interaction. Adv Protein Chem 39, 191 234.
    • (1988) Adv Protein Chem , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 32
    • 0015877037 scopus 로고
    • L-Asparaginase from Erwinia carotovora. Physicochemical properties of the native and succinylated enzyme
    • Shifrin S, Solis BG Chaiken IM (1973) l-Asparaginase from Erwinia carotovora. Physicochemical properties of the native and succinylated enzyme. J Biol Chem 248, 3464 3469.
    • (1973) J Biol Chem , vol.248 , pp. 3464-3469
    • Shifrin, S.1    Solis, B.G.2    Chaiken, I.M.3
  • 35
    • 0026315680 scopus 로고
    • Measurement of serum l-asparagine in the presence of l-asparaginase requires the presence of an l-asparaginase inhibitor
    • Asselin BL, Lorenson MY, Whitin JC, Coppola DJ, Kende AS, Blakley RL Cohen HJ (1991) Measurement of serum l-asparagine in the presence of l-asparaginase requires the presence of an l-asparaginase inhibitor. Cancer Res 51, 6568 6573.
    • (1991) Cancer Res , vol.51 , pp. 6568-6573
    • Asselin, B.L.1    Lorenson, M.Y.2    Whitin, J.C.3    Coppola, D.J.4    Kende, A.S.5    Blakley, R.L.6    Cohen, H.J.7
  • 36
    • 0035873421 scopus 로고    scopus 로고
    • Structural basis for the activity and substrate specificity of Erwinia chrysanthemil-asparaginase
    • Aghaiypour K, Wlodawer A Lubkowski J (2001b) Structural basis for the activity and substrate specificity of Erwinia chrysanthemil-asparaginase. Biochemistry 40, 5655 5664.
    • (2001) Biochemistry , vol.40 , pp. 5655-5664
    • Aghaiypour, K.1    Wlodawer, A.2    Lubkowski, J.3
  • 37
    • 0027717326 scopus 로고
    • Contribution of long-range electrostatic interactions to the stabilization of the catalytic transition state of the serine protease subtilisin BPN'
    • Jackson SE Fersht AR (1993) Contribution of long-range electrostatic interactions to the stabilization of the catalytic transition state of the serine protease subtilisin BPN'. Biochemistry 32, 13909 13916.
    • (1993) Biochemistry , vol.32 , pp. 13909-13916
    • Jackson, S.E.1    Fersht, A.R.2
  • 38
    • 32344451863 scopus 로고    scopus 로고
    • Free-energy simulations and experiments reveal long-range electrostatic interactions and substrate-assisted specificity in an aminoacyl-tRNA synthetase
    • Thompson D, Plateau P Simonson T (2006) Free-energy simulations and experiments reveal long-range electrostatic interactions and substrate-assisted specificity in an aminoacyl-tRNA synthetase. ChemBioChem 7, 337 344.
    • (2006) ChemBioChem , vol.7 , pp. 337-344
    • Thompson, D.1    Plateau, P.2    Simonson, T.3
  • 39
    • 30144432502 scopus 로고    scopus 로고
    • Contributions of long-range electrostatic interactions to 4-chlorobenzoyl-CoA dehalogenase catalysis: A combined theoretical and experimental study
    • Wu J, Xu D, Lu X, Wang C, Guo H Dunaway-Mariano D (2006) Contributions of long-range electrostatic interactions to 4-chlorobenzoyl-CoA dehalogenase catalysis: a combined theoretical and experimental study. Biochemistry 45, 102 112.
    • (2006) Biochemistry , vol.45 , pp. 102-112
    • Wu, J.1    Xu, D.2    Lu, X.3    Wang, C.4    Guo, H.5    Dunaway-Mariano, D.6
  • 40
    • 0033280672 scopus 로고    scopus 로고
    • Exploring nonnatural evolutionary pathways by saturation mutagenesis: Rapid improvement of protein function
    • Miyazaki K Arnold FH (1999) Exploring nonnatural evolutionary pathways by saturation mutagenesis: rapid improvement of protein function. J Mol Evol 49, 716 720.
    • (1999) J Mol Evol , vol.49 , pp. 716-720
    • Miyazaki, K.1    Arnold, F.H.2
  • 41
    • 3843146246 scopus 로고    scopus 로고
    • An efficient one-step site-directed and site-saturation mutagenesis protocol
    • Zheng L, Baumann U Reymond JL (2004) An efficient one-step site-directed and site-saturation mutagenesis protocol. Nucleic Acids Res 32, e115.
    • (2004) Nucleic Acids Res , vol.32
    • Zheng, L.1    Baumann, U.2    Reymond, J.L.3
  • 42
    • 0036902235 scopus 로고    scopus 로고
    • Close-range electrostatic interactions in proteins
    • Kumar S Nussinov R (2002) Close-range electrostatic interactions in proteins. ChemBioChem 3, 604 617.
    • (2002) ChemBioChem , vol.3 , pp. 604-617
    • Kumar, S.1    Nussinov, R.2
  • 44
    • 0033554840 scopus 로고    scopus 로고
    • Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface
    • Loladze VV, Ibarra-Molero B, Sanchez-Ruiz JM Makhatadze GI (1999) Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. Biochemistry 38, 16419 16423.
    • (1999) Biochemistry , vol.38 , pp. 16419-16423
    • Loladze, V.V.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3    Makhatadze, G.I.4
  • 45
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao H, Giver L, Shao Z, Affholter JA Arnold FH (1998) Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat Biotechnol 16, 258 261.
    • (1998) Nat Biotechnol , vol.16 , pp. 258-261
    • Zhao, H.1    Giver, L.2    Shao, Z.3    Affholter, J.A.4    Arnold, F.H.5
  • 46
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK Pease LR (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51 59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 47
    • 0034965123 scopus 로고    scopus 로고
    • Structural and functional stabilization of l-asparaginase via multisubunit immobilization onto highly activated supports
    • Balcao VM, Mateo C, Fernandez-Lafuente R, Malcata FX Guisan JM (2001) Structural and functional stabilization of l-asparaginase via multisubunit immobilization onto highly activated supports. Biotechnol Prog 17, 537 542.
    • (2001) Biotechnol Prog , vol.17 , pp. 537-542
    • Balcao, V.M.1    Mateo, C.2    Fernandez-Lafuente, R.3    Malcata, F.X.4    Guisan, J.M.5
  • 49
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MA (1976) A rapid and sensitive method for the 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.A.1
  • 50
    • 0037174163 scopus 로고    scopus 로고
    • Beta-aspartylpeptides as substrates of l-asparaginases from Escherichia coli and Erwinia chrysanthemi
    • Kelo E, Noronkoski T, Stoineva IB, Petkov DD Mononen I (2002) Beta-aspartylpeptides as substrates of l-asparaginases from Escherichia coli and Erwinia chrysanthemi. FEBS Lett 528, 130 132.
    • (2002) FEBS Lett , vol.528 , pp. 130-132
    • Kelo, E.1    Noronkoski, T.2    Stoineva, I.B.3    Petkov, D.D.4    Mononen, I.5
  • 51
    • 0025398721 scopus 로고
    • What if: A molecular modeling and drug design program
    • Vriend G (1990) what if: a molecular modeling and drug design program. J Mol Graph 8, 52 56.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 52
    • 0028863047 scopus 로고
    • The use of position specific rotamers in model building by homology
    • Chinea G, Padron G, Hooft RWW, Sander C Vriend G (1995) The use of position specific rotamers in model building by homology. Proteins 23, 415 421.
    • (1995) Proteins , vol.23 , pp. 415-421
    • Chinea, G.1    Padron, G.2    Hooft, R.W.W.3    Sander, C.4    Vriend, G.5
  • 53
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18, 2714 2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 55
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


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