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Volumn 79, Issue 5, 2008, Pages 751-758

Assembly of mutations for improving thermostability of Escherichia coli AppA2 phytase

Author keywords

Enzyme; Phytase; Protein engineering; Structure; Thermostability

Indexed keywords

COULOMB INTERACTIONS; ENZYME ACTIVITY; PROTEINS; THERMODYNAMIC STABILITY;

EID: 46549087211     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-008-1478-2     Document Type: Article
Times cited : (25)

References (30)
  • 1
    • 0037528980 scopus 로고    scopus 로고
    • Efficacy of an E. coli phytase expressed in yeast for releasing phytate-bound phosphorus in young chicks and pigs
    • Augspurger NR, Webel DM, Lei XG, Baker DH (2003) Efficacy of an E. coli phytase expressed in yeast for releasing phytate-bound phosphorus in young chicks and pigs. J Anim Sci 81:474-483
    • (2003) J Anim Sci , vol.81 , pp. 474-483
    • Augspurger, N.R.1    Webel, D.M.2    Lei, X.G.3    Baker, D.H.4
  • 2
    • 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 KQ, Robinson AC, Van Dam ME, Martinez P, Economou C, Arnold FH (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.Q.1    Robinson, A.C.2    Van Dam, M.E.3    Martinez, P.4    Economou, C.5    Arnold, F.H.6
  • 3
    • 0031022887 scopus 로고    scopus 로고
    • Additivity principles in biochemistry
    • Dill KA (1997) Additivity principles in biochemistry. J Biol Chem 272:701-704
    • (1997) J Biol Chem , vol.272 , pp. 701-704
    • Dill, K.A.1
  • 4
    • 0027383834 scopus 로고
    • Patterns of nonadditivity between pairs of stability mutations in Staphylococcal nuclease
    • Green SM, Shortle D (1993) Patterns of nonadditivity between pairs of stability mutations in Staphylococcal nuclease. Biochemistry 32:10131-10139
    • (1993) Biochemistry , vol.32 , pp. 10131-10139
    • Green, S.M.1    Shortle, D.2
  • 5
    • 0344289519 scopus 로고    scopus 로고
    • Role of glycosylation in the functional expression of an Aspergillus niger phytase (phyA) in Pichia pastoris
    • Han Y, Lei XG (1999) Role of glycosylation in the functional expression of an Aspergillus niger phytase (phyA) in Pichia pastoris. Arch Biochem Biophys 364:83-90
    • (1999) Arch Biochem Biophys , vol.364 , pp. 83-90
    • Han, Y.1    Lei, X.G.2
  • 6
    • 0032923801 scopus 로고    scopus 로고
    • Expression of an Aspergillus niger phytase gene (phyA) in Saccharomyces cerevisiae
    • Han YM, Wilson DB, Lei XG (1999) Expression of an Aspergillus niger phytase gene (phyA) in Saccharomyces cerevisiae. Appl Environ Microbiol 65:1915-1918
    • (1999) Appl Environ Microbiol , vol.65 , pp. 1915-1918
    • Han, Y.M.1    Wilson, D.B.2    Lei, X.G.3
  • 8
    • 0035936616 scopus 로고    scopus 로고
    • Structure-based chimeric enzymes as an alternative to directed enzyme evolution: Phytase as a test case
    • Jermutus L, Tessier M, Pasamontes L, van Loon A, Lehmann M (2001) Structure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case. J Biotechnol 85:15-24
    • (2001) J Biotechnol , vol.85 , pp. 15-24
    • Jermutus, L.1    Tessier, M.2    Pasamontes, L.3    Van Loon, A.4    Lehmann, M.5
  • 9
    • 42149088826 scopus 로고    scopus 로고
    • Enhancing thermostability of Escherichia coli phytase AppA2 by error-prone PCR
    • 1
    • Kim M-S, Lei XG (2008) Enhancing thermostability of Escherichia coli phytase AppA2 by error-prone PCR. Appl Microbiol Biotechnol 79(1):69-75
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 69-75
    • Kim, M.-S.1    Lei, X.G.2
  • 12
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar S, Tsai CJ, Nussinov R (2000) Factors enhancing protein thermostability. Protein Eng 13:179-191
    • (2000) Protein Eng , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 13
    • 17644384867 scopus 로고    scopus 로고
    • Expression of Escherichia coli AppA2 phytase in four yeast systems
    • Lee S, Kim T, Stahl CH, Lei XG (2005) Expression of Escherichia coli AppA2 phytase in four yeast systems. Biotechnol Lett 27:327-334
    • (2005) Biotechnol Lett , vol.27 , pp. 327-334
    • Lee, S.1    Kim, T.2    Stahl, C.H.3    Lei, X.G.4
  • 14
    • 0033963277 scopus 로고    scopus 로고
    • From DNA sequence to improved functionality: Using protein sequence comparisons to rapidly design a thermostable consensus phytase
    • Lehmann M, Kostrewa D, Wyss M, Brugger R, D'Arcy A, Pasamontes L, van Loon A (2000a) From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase. Protein Eng 13:49-57
    • (2000) Protein Eng , vol.13 , pp. 49-57
    • Lehmann, M.1    Kostrewa, D.2    Wyss, M.3    Brugger, R.4    D'Arcy, A.5    Pasamontes, L.6    Van Loon, A.7
  • 15
    • 0033769666 scopus 로고    scopus 로고
    • Exchanging the active site between phytases for altering the functional properties of the enzyme
    • Lehmann M, Lopez-Ulibarri R, Loch C, Viarouge C, Wyss M, van Loon AP (2000b) Exchanging the active site between phytases for altering the functional properties of the enzyme. Protein Sci 9:1866-1872
    • (2000) Protein Sci , vol.9 , pp. 1866-1872
    • Lehmann, M.1    Lopez-Ulibarri, R.2    Loch, C.3    Viarouge, C.4    Wyss, M.5    Van Loon, A.P.6
  • 16
    • 0028965496 scopus 로고
    • Long-range, small magnitude nonadditivity of mutational effects in proteins
    • LiCata VJ, Ackers GK (1995) Long-range, small magnitude nonadditivity of mutational effects in proteins. Biochemistry 34:3133-3139
    • (1995) Biochemistry , vol.34 , pp. 3133-3139
    • Licata, V.J.1    Ackers, G.K.2
  • 17
    • 0033952704 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli phytase and its complex with phytate
    • Lim D, Golovan S, Forsberg CW, Jia Z (2000) Crystal structures of Escherichia coli phytase and its complex with phytate. Nat Struct Biol 7:108-113
    • (2000) Nat Struct Biol , vol.7 , pp. 108-113
    • Lim, D.1    Golovan, S.2    Forsberg, C.W.3    Jia, Z.4
  • 18
    • 0034790185 scopus 로고    scopus 로고
    • New insights into the thermostability of bacterial ferredoxins: High-resolution crystal structure of the seven-iron ferredoxin from Thermus thermophilus
    • Macedo-Ribeiro S, Martins BM, Pereira PJ, Buse G, Huber R, Soulimane T (2001) New insights into the thermostability of bacterial ferredoxins: high-resolution crystal structure of the seven-iron ferredoxin from Thermus thermophilus. J Biol Inorg Chem 6:663-674
    • (2001) J Biol Inorg Chem , vol.6 , pp. 663-674
    • MacEdo-Ribeiro, S.1    Martins, B.M.2    Pereira, P.J.3    Buse, G.4    Huber, R.5    Soulimane, T.6
  • 19
    • 0033593453 scopus 로고    scopus 로고
    • Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues
    • Oue S, Okamoto A, Yano T, Kagamiyama H (1999) Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues. J Biol Chem 274:2344-2349
    • (1999) J Biol Chem , vol.274 , pp. 2344-2349
    • Oue, S.1    Okamoto, A.2    Yano, T.3    Kagamiyama, H.4
  • 20
    • 0034802215 scopus 로고    scopus 로고
    • Hydrogen-bonding classes in proteins and their contribution to the unfolding reaction
    • Ragone R (2001) Hydrogen-bonding classes in proteins and their contribution to the unfolding reaction. Protein Sci 10:2075-2082
    • (2001) Protein Sci , vol.10 , pp. 2075-2082
    • Ragone, R.1
  • 21
    • 0033562103 scopus 로고    scopus 로고
    • Different sensitivity of recombinant Aspergillus niger phytase (r-PhyA) and Escherichia coli pH 2.5 acid phosphatase (r-AppA) to trypsin and pepsin in vitro
    • Rodriguez E, Porres JM, Han Y, Lei XG (1999) Different sensitivity of recombinant Aspergillus niger phytase (r-PhyA) and Escherichia coli pH 2.5 acid phosphatase (r-AppA) to trypsin and pepsin in vitro. Arch Biochem Biophys 365:262-267
    • (1999) Arch Biochem Biophys , vol.365 , pp. 262-267
    • Rodriguez, E.1    Porres, J.M.2    Han, Y.3    Lei, X.G.4
  • 22
    • 0034307020 scopus 로고    scopus 로고
    • Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris
    • Rodriguez E, Wood ZA, Karplus PA, Lei XG (2000) Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris. Arch Biochem Biophys 382:105-112
    • (2000) Arch Biochem Biophys , vol.382 , pp. 105-112
    • Rodriguez, E.1    Wood, Z.A.2    Karplus, P.A.3    Lei, X.G.4
  • 23
    • 0029056922 scopus 로고
    • Energetics of protein-protein interactions: Analysis of the barnase-barstar interface by single mutations and double mutant cycles
    • Schreiber G, Fersht AR (1995) Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles. J Mol Biol 248:478-486
    • (1995) J Mol Biol , vol.248 , pp. 478-486
    • Schreiber, G.1    Fersht, A.R.2
  • 24
    • 0028807466 scopus 로고
    • Design and structural analysis of an engineered thermostable chicken lysozyme
    • Shih P, Kirsch JF (1995) Design and structural analysis of an engineered thermostable chicken lysozyme. Protein Sci 4:2063-2072
    • (1995) Protein Sci , vol.4 , pp. 2063-2072
    • Shih, P.1    Kirsch, J.F.2
  • 25
    • 0029785464 scopus 로고    scopus 로고
    • Potential use of additivity of mutational effects in simplifying protein engineering
    • Skinner MM, Terwilliger TC (1996) Potential use of additivity of mutational effects in simplifying protein engineering. Proc Natl Acad Sci USA 93:10753-10757
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10753-10757
    • Skinner, M.M.1    Terwilliger, T.C.2
  • 27
    • 0029893110 scopus 로고    scopus 로고
    • Thermozymes: Identifying molecular determinants of protein structural and functional stability
    • Vieille C, Zeikus JG (1996) Thermozymes: identifying molecular determinants of protein structural and functional stability. Trends Biotechnol 14:183-190
    • (1996) Trends Biotechnol , vol.14 , pp. 183-190
    • Vieille, C.1    Zeikus, J.G.2
  • 28
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Vieille C, Zeikus GJ (2001) Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65:1-43
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 29
    • 0035957360 scopus 로고    scopus 로고
    • Computational method to reduce the search space for directed protein evolution
    • Voigt CA, Mayo SL, Arnold FH, Wang ZG (2001) Computational method to reduce the search space for directed protein evolution. Proc Natl Acad Sci USA 98:3778-3783
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3778-3783
    • Voigt, C.A.1    Mayo, S.L.2    Arnold, F.H.3    Wang, Z.G.4
  • 30
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells JA (1990) Additivity of mutational effects in proteins. Biochemistry 29:8509-8517
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.