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Volumn 23, Issue 5, 2006, Pages 247-251

Protein engineering of class-A non-specific acid phosphatase (PhoN) of Salmonella typhimurium: Modulation of the pH-activity profile

Author keywords

Bioremediation; Class A bacterial non specific acid phosphatase; pH optimum; PhoN protein of Salmonella typhimurium; Protein engineering; Site directed mutagenesis

Indexed keywords

BIOREMEDIATION; CATALYSIS; ENZYME KINETICS; ESCHERICHIA COLI; GENES; HEAVY METALS; HYDROLYSIS; MUTAGENESIS; NICKEL; PH EFFECTS; URANIUM;

EID: 33747879510     PISSN: 13890344     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioeng.2006.06.004     Document Type: Article
Times cited : (15)

References (30)
  • 2
    • 0032724864 scopus 로고    scopus 로고
    • Isolation, cloning, and expression of an acid phosphatase containing phosphotyrosyl phosphatase activity from Prevotella intermedia
    • Chen X., Ansai T., Awano S., Iida T., Barik S., and Takehara T. Isolation, cloning, and expression of an acid phosphatase containing phosphotyrosyl phosphatase activity from Prevotella intermedia. J. Bacteriol. 181 (1999) 7107-7114
    • (1999) J. Bacteriol. , vol.181 , pp. 7107-7114
    • Chen, X.1    Ansai, T.2    Awano, S.3    Iida, T.4    Barik, S.5    Takehara, T.6
  • 3
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative computational project, number 4, 1994. Programs for Protein, Crystallography. Acta Cryst. D 50, 760-763.
  • 4
    • 0037250672 scopus 로고    scopus 로고
    • Kinetic and site-directed mutagenesis studies of Prevotella intermedia acid phosphatase
    • Chen X., Ansai T., Barik S., and Takehara T. Kinetic and site-directed mutagenesis studies of Prevotella intermedia acid phosphatase. Protein Pept. Lett. 10 (2003) 53-59
    • (2003) Protein Pept. Lett. , vol.10 , pp. 53-59
    • Chen, X.1    Ansai, T.2    Barik, S.3    Takehara, T.4
  • 6
    • 0036783381 scopus 로고    scopus 로고
    • a of histidine side-chains correlates with burial within proteins
    • a of histidine side-chains correlates with burial within proteins. Proteins 49 (2002) 1-6
    • (2002) Proteins , vol.49 , pp. 1-6
    • Edgcomb, S.P.1    Murphy, K.P.2
  • 7
    • 0031813124 scopus 로고    scopus 로고
    • Protein engineering of Aspergillus awamori glucoamylase to increase its pH optimum
    • Fang T.Y., and Ford C. Protein engineering of Aspergillus awamori glucoamylase to increase its pH optimum. Protein Eng. 11 (1998) 383-388
    • (1998) Protein Eng. , vol.11 , pp. 383-388
    • Fang, T.Y.1    Ford, C.2
  • 9
    • 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
  • 10
  • 11
    • 0034213094 scopus 로고    scopus 로고
    • X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate
    • Ishikawa K., Mihara Y., Gondoh K., Suzuki E., and Asano Y. X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate. EMBO J. 19 (2000) 2412-2423
    • (2000) EMBO J. , vol.19 , pp. 2412-2423
    • Ishikawa, K.1    Mihara, Y.2    Gondoh, K.3    Suzuki, E.4    Asano, Y.5
  • 12
    • 0017614303 scopus 로고
    • Resolution and purification of three periplasmic phosphatases of Salmonella typhimurium
    • Kier L.D., Weppelman R., and Ames B.N. Resolution and purification of three periplasmic phosphatases of Salmonella typhimurium. J. Bacteriol 130 (1977) 399-410
    • (1977) J. Bacteriol , vol.130 , pp. 399-410
    • Kier, L.D.1    Weppelman, R.2    Ames, B.N.3
  • 14
    • 0028169546 scopus 로고
    • Enzymically accelerated biomineralization of heavy metals: application to the removal of americium and plutonium from aqueous flows
    • Macaskie L.E., Jeong B.C., and Tolley M.R. Enzymically accelerated biomineralization of heavy metals: application to the removal of americium and plutonium from aqueous flows. FEMS Microbiol. Rev. 14 (1994) 351-367
    • (1994) FEMS Microbiol. Rev. , vol.14 , pp. 351-367
    • Macaskie, L.E.1    Jeong, B.C.2    Tolley, M.R.3
  • 15
    • 0030217708 scopus 로고    scopus 로고
    • The use of micro-organism for the remediation of solutions contaminated with actinide elements, other radionuclides, and organic contaminants generated by nuclear fuel cycle activities
    • Macaskie L.E., Lloyd J.R., Thomas A.P., and Tolley M.R. The use of micro-organism for the remediation of solutions contaminated with actinide elements, other radionuclides, and organic contaminants generated by nuclear fuel cycle activities. Nucl. energy 5 (1996) 257-271
    • (1996) Nucl. energy , vol.5 , pp. 257-271
    • Macaskie, L.E.1    Lloyd, J.R.2    Thomas, A.P.3    Tolley, M.R.4
  • 16
    • 0031553509 scopus 로고    scopus 로고
    • Bioremediation of uranium-bearing wastewater: biochemical and chemical factors influencing bioprocess application
    • Macaskie L.E., Yong P., Doyle T.C., Roig M.G., Diaz M., and Manzano T. Bioremediation of uranium-bearing wastewater: biochemical and chemical factors influencing bioprocess application. Biotechnol. Bioeng. 53 (1997) 100-109
    • (1997) Biotechnol. Bioeng. , vol.53 , pp. 100-109
    • Macaskie, L.E.1    Yong, P.2    Doyle, T.C.3    Roig, M.G.4    Diaz, M.5    Manzano, T.6
  • 17
    • 0037348493 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction studies of recombinant class-A non-specific acid phosphatase of Salmonella typhimurium
    • Makde R.D., Kumar V., Rao A.S., Yadava V.S., and Mahajan S.K. Purification, crystallization and preliminary X-ray diffraction studies of recombinant class-A non-specific acid phosphatase of Salmonella typhimurium. Acta Cryst. D 59 (2003) 515-518
    • (2003) Acta Cryst. D , vol.59 , pp. 515-518
    • Makde, R.D.1    Kumar, V.2    Rao, A.S.3    Yadava, V.S.4    Mahajan, S.K.5
  • 18
    • 0025298012 scopus 로고
    • Protein engineering of chymosin; modification of the optimum pH of enzyme catalysis
    • Mantafounis D., and Pitts J. Protein engineering of chymosin; modification of the optimum pH of enzyme catalysis. Protein Eng. 3 (1990) 605-609
    • (1990) Protein Eng. , vol.3 , pp. 605-609
    • Mantafounis, D.1    Pitts, J.2
  • 19
    • 9844256470 scopus 로고
    • Protein determination for large numbers of samples
    • Miller G.L. Protein determination for large numbers of samples. Anal. Chem. 31 (1959) 964
    • (1959) Anal. Chem. , vol.31 , pp. 964
    • Miller, G.L.1
  • 20
    • 0030753213 scopus 로고    scopus 로고
    • An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases
    • Neuwald A.F. An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases. Protein Sci. 6 (1997) 1764-1767
    • (1997) Protein Sci. , vol.6 , pp. 1764-1767
    • Neuwald, A.F.1
  • 21
    • 0034855331 scopus 로고    scopus 로고
    • The determinant of α-amylase pH-activity profiles
    • Nielsen J.E., Borchert T.V., and Vriend G. The determinant of α-amylase pH-activity profiles. Protein Eng. 14 (2001) 505-512
    • (2001) Protein Eng. , vol.14 , pp. 505-512
    • Nielsen, J.E.1    Borchert, T.V.2    Vriend, G.3
  • 22
    • 0031689411 scopus 로고    scopus 로고
    • Bacterial non-specific acid phosphohydrolases: physiology, evolution and use as tools in microbial biotechnology
    • Rossolini G.M., Schippa S., Riccio M.L., Berlutti F., Makaskie L.E., and Thaller M.C. Bacterial non-specific acid phosphohydrolases: physiology, evolution and use as tools in microbial biotechnology. Cell Mol. Life Sci. 54 (1998) 833-850
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 833-850
    • Rossolini, G.M.1    Schippa, S.2    Riccio, M.L.3    Berlutti, F.4    Makaskie, L.E.5    Thaller, M.C.6
  • 23
    • 0026548444 scopus 로고
    • Cloning and sequencing of the gene coding for alcohol dehydrogenase of Bacillus stearothermophilus and rational shift of the optimum pH
    • Sakoda H., and Imanaka T. Cloning and sequencing of the gene coding for alcohol dehydrogenase of Bacillus stearothermophilus and rational shift of the optimum pH. J. Bacteriol. 174 (1992) 1397-1402
    • (1992) J. Bacteriol. , vol.174 , pp. 1397-1402
    • Sakoda, H.1    Imanaka, T.2
  • 25
    • 0031048876 scopus 로고    scopus 로고
    • Identification of a novel phosphatase sequence motif
    • Stukey J., and Carman G.M. Identification of a novel phosphatase sequence motif. Protein Sci. 6 (1997) 469-472
    • (1997) Protein Sci. , vol.6 , pp. 469-472
    • Stukey, J.1    Carman, G.M.2
  • 26
    • 0028225869 scopus 로고
    • Characterization and sequence of PhoC, the principal phosphate-irrepressible acid phosphatase of Morganella morganii
    • Thaller M.C., Berlutti F., Schippa S., Lombardi G., and Rossolini G.M. Characterization and sequence of PhoC, the principal phosphate-irrepressible acid phosphatase of Morganella morganii. Microbiology 140 (1994) 1341-1350
    • (1994) Microbiology , vol.140 , pp. 1341-1350
    • Thaller, M.C.1    Berlutti, F.2    Schippa, S.3    Lombardi, G.4    Rossolini, G.M.5
  • 27
    • 0029038590 scopus 로고
    • Lanthanum accumulation from acidic solutions using a Citrobacter sp. immobilised in a flow-through bioreactor
    • Tolley M.R., Strachan L.F., and Mackaskie L.E. Lanthanum accumulation from acidic solutions using a Citrobacter sp. immobilised in a flow-through bioreactor. J. Ind. Microbiol. 14 (1995) 271-280
    • (1995) J. Ind. Microbiol. , vol.14 , pp. 271-280
    • Tolley, M.R.1    Strachan, L.F.2    Mackaskie, L.E.3
  • 28
    • 0029786040 scopus 로고    scopus 로고
    • Identification and characterization of phoN-Sf, a gene on the large plasmid of Shigella flexneri 2a encoding a non-specific phosphatase
    • Uchiya K.I., Tohsuji M., Nikai T., Sugihara H., and Sasakawa C. Identification and characterization of phoN-Sf, a gene on the large plasmid of Shigella flexneri 2a encoding a non-specific phosphatase. J. Bacteriol. 178 (1996) 4548-4554
    • (1996) J. Bacteriol. , vol.178 , pp. 4548-4554
    • Uchiya, K.I.1    Tohsuji, M.2    Nikai, T.3    Sugihara, H.4    Sasakawa, C.5
  • 29
    • 0017597241 scopus 로고
    • Properties of two phosphatases and a cyclic phosphodiesterase of Salmonella typhimurium
    • Weppelman R., Kier L.D., and Ames B.N. Properties of two phosphatases and a cyclic phosphodiesterase of Salmonella typhimurium. J. Bacteriol. 130 (1977) 411-419
    • (1977) J. Bacteriol. , vol.130 , pp. 411-419
    • Weppelman, R.1    Kier, L.D.2    Ames, B.N.3
  • 30
    • 0029311098 scopus 로고
    • Enhancement of uranium bioaccumulation by a Citrobacter sp. via enzymatically-mediated growth of polycrystalline NH4UO2PO4
    • Yong P., and Mackaskie L.E. Enhancement of uranium bioaccumulation by a Citrobacter sp. via enzymatically-mediated growth of polycrystalline NH4UO2PO4. J. Chem. Technol. Biotechnol. 65 (1995) 101-108
    • (1995) J. Chem. Technol. Biotechnol. , vol.65 , pp. 101-108
    • Yong, P.1    Mackaskie, L.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.