메뉴 건너뛰기




Volumn 44, Issue 23, 2005, Pages 8378-8386

Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CATALYSIS; ESCHERICHIA COLI; MAGNESIUM PRINTING PLATES; PH EFFECTS; ZINC;

EID: 20444390656     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050155p     Document Type: Article
Times cited : (47)

References (24)
  • 1
    • 0014231123 scopus 로고
    • The kinetics of the reaction of nitrophenyl phosphate with alkaline phosphatase from Escherichia coli
    • Trentham, D. R., and Gutfreund, H. (1968) The kinetics of the reaction of nitrophenyl phosphate with alkaline phosphatase from Escherichia coli, Biochem. J. 106, 455-460.
    • (1968) Biochem. J. , vol.106 , pp. 455-460
    • Trentham, D.R.1    Gutfreund, H.2
  • 2
    • 0025977645 scopus 로고
    • Bacillus subtilis alkaline phosphatase III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure
    • Hulett, F. M., Kim, E. E., Bookstein, C., Kapp, N. V., Edward, C. W., and Wyckoff, H. W. (1991) Bacillus subtilis alkaline phosphatase III and IV. Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure, J. Biol. Chem. 266, 1077-1084.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1077-1084
    • Hulett, F.M.1    Kim, E.E.2    Bookstein, C.3    Kapp, N.V.4    Edward, C.W.5    Wyckoff, H.W.6
  • 3
    • 0036130777 scopus 로고    scopus 로고
    • Alkaline phosphtase from the hyperthermophilic bacterium Thermotoga maritima requires cobalt for activity
    • Wojciechowski, C. L., Cardia, J. P., and Kantrowitz, E. R. (2002) Alkaline phosphtase from the hyperthermophilic bacterium Thermotoga maritima requires cobalt for activity, Protein Sci. 11, 903-911.
    • (2002) Protein Sci. , vol.11 , pp. 903-911
    • Wojciechowski, C.L.1    Cardia, J.P.2    Kantrowitz, E.R.3
  • 4
    • 0037184908 scopus 로고    scopus 로고
    • Altering of the metal specificity of Escherichia coli alkaline phosphatase
    • Wojciechowski, C. L., and Kantrowitz, E. R. (2002) Altering of the metal specificity of Escherichia coli alkaline phosphatase, J. Biol. Chem. 277, 50476-50481.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50476-50481
    • Wojciechowski, C.L.1    Kantrowitz, E.R.2
  • 5
    • 0024116932 scopus 로고
    • Function of arginine in the active site of Escherichia coli alkaline phosphatase
    • Chaidaroglou, A., Brezinski, J. D., Middleton, S. A., and Kantrowitz, E. R. (1988) Function of arginine in the active site of Escherichia coli alkaline phosphatase, Biochemistry 27, 8338-8343.
    • (1988) Biochemistry , vol.27 , pp. 8338-8343
    • Chaidaroglou, A.1    Brezinski, J.D.2    Middleton, S.A.3    Kantrowitz, E.R.4
  • 6
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (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
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (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.M.1
  • 8
    • 0035908887 scopus 로고    scopus 로고
    • 2+ binding to alkaline phosphatase correlates with slow changes in protein lability
    • 2+ binding to alkaline phosphatase correlates with slow changes in protein lability, Biochemistry 40, 11219-11226.
    • (2001) Biochemistry , vol.40 , pp. 11219-11226
    • Dirnbach, E.1    Steel, D.G.2    Gafni, A.3
  • 9
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 10
    • 0034705337 scopus 로고    scopus 로고
    • A revised mechanism of the alkaline phosphatase reaction involving three metal ions
    • Stec, B., Holtz, K. M., and Kantrowitz, E. R. (2000) A revised mechanism of the alkaline phosphatase reaction involving three metal ions, J. Mol. Biol. 299, 1303-1311.
    • (2000) J. Mol. Biol. , vol.299 , pp. 1303-1311
    • Stec, B.1    Holtz, K.M.2    Kantrowitz, E.R.3
  • 12
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. (1999) XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density, J. Struct. Biol. 125, 156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 14
    • 0028845411 scopus 로고
    • Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases
    • Murphy, J. E., Tibbitts, T. T., and Kantrowitz, E. R. (1995) Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases, J. Mol. Biol. 253, 604-617.
    • (1995) J. Mol. Biol. , vol.253 , pp. 604-617
    • Murphy, J.E.1    Tibbitts, T.T.2    Kantrowitz, E.R.3
  • 16
    • 20444401773 scopus 로고    scopus 로고
    • E. coli alkaline phosphatase
    • (Messerschmidt, A., Bode, W., and Cygler, M., Eds.), John Wiley & Sons. Ltd., Chichester, U.K.
    • Kantrowitz, E. R. (2004) E. coli Alkaline Phosphatase, in Handbook of Metalloproteins (Messerschmidt, A., Bode, W., and Cygler, M., Eds.) pp 71-82, John Wiley & Sons. Ltd., Chichester, U.K.
    • (2004) Handbook of Metalloproteins , pp. 71-82
    • Kantrowitz, E.R.1
  • 17
    • 0033564306 scopus 로고    scopus 로고
    • Escherichia coli Methionine Aminopeptidase: Implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis
    • Lowther, W. T., Orville, A. M., Madden, D. T., Lim, S., Rich, D. H., and Matthews, B. W. (1999) Escherichia coli Methionine Aminopeptidase: Implications of Crystallographic Analyses of the Native, Mutant, and Inhibited Enzymes for the Mechanism of Catalysis. Biochemistry 38, 7678-7688.
    • (1999) Biochemistry , vol.38 , pp. 7678-7688
    • Lowther, W.T.1    Orville, A.M.2    Madden, D.T.3    Lim, S.4    Rich, D.H.5    Matthews, B.W.6
  • 20
    • 0019176756 scopus 로고
    • Catalytic mechanism of Escherichia coli alkaline phosphatase: Resolution of three variants of the acyl-enzyme mechanism
    • Bloch, W., and Gorby, M. S. (1980) Catalytic mechanism of Escherichia coli alkaline phosphatase: Resolution of three variants of the acyl-enzyme mechanism, Biochemistry 19, 5008-5018.
    • (1980) Biochemistry , vol.19 , pp. 5008-5018
    • Bloch, W.1    Gorby, M.S.2
  • 21
    • 0020650842 scopus 로고
    • Alkaline phosphatase, solution structure, and mechanism
    • Coleman, J. E., and Getting, P. (1983) Alkaline Phosphatase, Solution Structure, and Mechanism, Adv. Enzymol. 55, 351-452.
    • (1983) Adv. Enzymol. , vol.55 , pp. 351-452
    • Coleman, J.E.1    Getting, P.2
  • 22
  • 23
    • 0027493015 scopus 로고
    • Conversion of a magnesium binding site into a zinc binding site by a single amino acid substitution Escherichia coli alkaline phosphatase
    • Murphy, J. E., Xu, X., and Kantrowitz, E. R. (1993) Conversion of a magnesium binding site into a zinc binding site by a single amino acid substitution Escherichia coli alkaline phosphatase, J. Biol. Chem. 268, 21497-21500.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21497-21500
    • Murphy, J.E.1    Xu, X.2    Kantrowitz, E.R.3
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: A Program to Produce Both Detailed and Schematic Plots of Protein Structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.