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Volumn 139, Issue 2, 2009, Pages 186-193

Structure-based fragment shuffling of two fungal phytases for combination of desirable properties

Author keywords

Aspergillus fumigatus; Aspergillus niger; Heat resistance; Phytase; Protein engineering

Indexed keywords

3D STRUCTURES; ASPERGILLUS FUMIGATUS; ASPERGILLUS NIGER; DESIRABLE PROPERTIES; PHYTASE; PHYTASES; PICHIA PASTORIS; PROTEIN ENGINEERING; SEQUENCE ALIGNMENTS; SPECIFIC ACTIVITIES; SYSTEMATIC EVALUATIONS;

EID: 57949091755     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2008.08.011     Document Type: Article
Times cited : (18)

References (34)
  • 2
    • 0035349519 scopus 로고    scopus 로고
    • Overexpression of artificial synthetic gene of Aspergillus niger NRRL3135 phytase in Pichia pastoris
    • Bei J.L., Chen Z., Yang L., Liao L., Wang X.Z., and Jiang Z.Y. Overexpression of artificial synthetic gene of Aspergillus niger NRRL3135 phytase in Pichia pastoris. Sheng Wu Gong Cheng Xue Bao 17 (2001) 254-258
    • (2001) Sheng Wu Gong Cheng Xue Bao , vol.17 , pp. 254-258
    • Bei, J.L.1    Chen, Z.2    Yang, L.3    Liao, L.4    Wang, X.Z.5    Jiang, Z.Y.6
  • 3
    • 0030747157 scopus 로고    scopus 로고
    • RNA virus mutations and fitness for survival
    • Domingo E., and Holland J.J. RNA virus mutations and fitness for survival. Annu. Rev. Microbiol. 51 (1997) 151-178
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 151-178
    • Domingo, E.1    Holland, J.J.2
  • 6
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 7
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 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.P., and Lehmann M. Structure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case. J. Biotechnol. 85 (2001) 15-24
    • (2001) J. Biotechnol. , vol.85 , pp. 15-24
    • Jermutus, L.1    Tessier, M.2    Pasamontes, L.3    van Loon, A.P.4    Lehmann, M.5
  • 11
    • 0033591464 scopus 로고    scopus 로고
    • Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2.4 A resolution
    • Kostrewa D., Wyss M., D'Arcy A., and van Loon A.P. Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2.4 A resolution. J. Mol. Biol. 288 (1999) 965-974
    • (1999) J. Mol. Biol. , vol.288 , pp. 965-974
    • Kostrewa, D.1    Wyss, M.2    D'Arcy, A.3    van Loon, A.P.4
  • 12
    • 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., and van Loon A.P. From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase. Protein Eng. 13 (2000) 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.P.7
  • 13
    • 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., and van Loon A.P. Exchanging the active site between phytases for altering the functional properties of the enzyme. Protein Sci. 9 (2000) 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
  • 15
    • 4444336413 scopus 로고    scopus 로고
    • Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics
    • Liu Q., Huang Q., Lei X.G., and Hao Q. Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics. Structure 12 (2004) 1575-1583
    • (2004) Structure , vol.12 , pp. 1575-1583
    • Liu, Q.1    Huang, Q.2    Lei, X.G.3    Hao, Q.4
  • 18
    • 1642578253 scopus 로고    scopus 로고
    • Biochemical properties and substrate specificities of alkaline and histidine acid phytases
    • Oh B.C., Choi W.C., Park S., Kim Y.O., and Oh T.K. Biochemical properties and substrate specificities of alkaline and histidine acid phytases. Appl. Microbiol. Biotechnol. 63 (2004) 362-372
    • (2004) Appl. Microbiol. Biotechnol. , vol.63 , pp. 362-372
    • Oh, B.C.1    Choi, W.C.2    Park, S.3    Kim, Y.O.4    Oh, T.K.5
  • 19
    • 0030898612 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus
    • Pasamontes L., Haiker M., Wyss M., Tessier M., and van Loon A.P. Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus. Appl. Environ. Microbiol. 63 (1997) 1696-1700
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1696-1700
    • Pasamontes, L.1    Haiker, M.2    Wyss, M.3    Tessier, M.4    van Loon, A.P.5
  • 20
    • 0034673345 scopus 로고    scopus 로고
    • Expression of the Aspergillus fumigatus phytase gene in Pichia pastoris and characterization of the recombinant enzyme
    • Rodriguez E., Mullaney E.J., and Lei X.G. Expression of the Aspergillus fumigatus phytase gene in Pichia pastoris and characterization of the recombinant enzyme. Biochem. Biophys. Res. Commun. 268 (2000) 373-378
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 373-378
    • Rodriguez, E.1    Mullaney, E.J.2    Lei, X.G.3
  • 21
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer W.P. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370 (1994) 389-391
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.1
  • 25
    • 0024237908 scopus 로고
    • Aspergillus ficuum phytase: partial primary structure, substrate selectivity, and kinetic characterization
    • Ullah A.H. Aspergillus ficuum phytase: partial primary structure, substrate selectivity, and kinetic characterization. Prep. Biochem. 18 (1988) 459-471
    • (1988) Prep. Biochem. , vol.18 , pp. 459-471
    • Ullah, A.H.1
  • 26
    • 0023080759 scopus 로고
    • Extracellular phytase (E.C. 3.1.3.8) from Aspergillus ficuum NRRL 3135: purification and characterization
    • Ullah A.H., and Gibson D.M. Extracellular phytase (E.C. 3.1.3.8) from Aspergillus ficuum NRRL 3135: purification and characterization. Prep. Biochem. 17 (1987) 63-91
    • (1987) Prep. Biochem. , vol.17 , pp. 63-91
    • Ullah, A.H.1    Gibson, D.M.2
  • 31
    • 0031734945 scopus 로고    scopus 로고
    • Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase, A. niger phytase, and A. niger PH 2.5 acid phosphatase
    • Wyss M., Pasamontes L., Remy R., Kohler J., Kusznir E., Gadient M., Muller F., and van Loon A.P.G.M. Comparison of the thermostability properties of three acid phosphatases from molds: Aspergillus fumigatus phytase, A. niger phytase, and A. niger PH 2.5 acid phosphatase. Appl. Environ. Microbiol. 64 (1998) 4446-4451
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4446-4451
    • Wyss, M.1    Pasamontes, L.2    Remy, R.3    Kohler, J.4    Kusznir, E.5    Gadient, M.6    Muller, F.7    van Loon, A.P.G.M.8
  • 32
    • 2342501800 scopus 로고    scopus 로고
    • Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine
    • Xiang T., Liu Q., Deacon A.M., Koshy M., Kriksunov I.A., Lei X.G., Hao Q., and Thiel D.J. Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine. J. Mol. Biol. 339 (2004) 437-445
    • (2004) J. Mol. Biol. , vol.339 , pp. 437-445
    • Xiang, T.1    Liu, Q.2    Deacon, A.M.3    Koshy, M.4    Kriksunov, I.A.5    Lei, X.G.6    Hao, Q.7    Thiel, D.J.8
  • 33
    • 37249041070 scopus 로고    scopus 로고
    • Cumulative improvements of thermostability and pH-activity profile of Aspergillus niger PhyA phytase by site-directed mutagenesis
    • Zhang W.M., and Lei X.G. Cumulative improvements of thermostability and pH-activity profile of Aspergillus niger PhyA phytase by site-directed mutagenesis. Appl. Microbiol. Biotechnol. 77 (2008) 1033-1040
    • (2008) Appl. Microbiol. Biotechnol. , vol.77 , pp. 1033-1040
    • Zhang, W.M.1    Lei, X.G.2
  • 34
    • 34248192717 scopus 로고    scopus 로고
    • Adopting selected hydrogen bonding and ionic interactions from Aspergillus fumigatus phytase structure improves the thermostability of Aspergillus niger PhyA phytase
    • Zhang W.M., Mullaney E.J., and Lei X.G. Adopting selected hydrogen bonding and ionic interactions from Aspergillus fumigatus phytase structure improves the thermostability of Aspergillus niger PhyA phytase. Appl. Environ. Biotechnol. 73 (2007) 3069-3076
    • (2007) Appl. Environ. Biotechnol. , vol.73 , pp. 3069-3076
    • Zhang, W.M.1    Mullaney, E.J.2    Lei, X.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.