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192 related items for PubMed ID: 8104481

  • 1. Binding of magnesium in a mutant Escherichia coli alkaline phosphatase changes the rate-determining step in the reaction mechanism.
    Xu X, Kantrowitz ER.
    Biochemistry; 1993 Oct 12; 32(40):10683-91. PubMed ID: 8104481
    [Abstract] [Full Text] [Related]

  • 2. Magnesium in the active site of Escherichia coli alkaline phosphatase is important for both structural stabilization and catalysis.
    Janeway CM, Xu X, Murphy JE, Chaidaroglou A, Kantrowitz ER.
    Biochemistry; 1993 Feb 16; 32(6):1601-9. PubMed ID: 8431439
    [Abstract] [Full Text] [Related]

  • 3. Enhanced catalysis by active-site mutagenesis at aspartic acid 153 in Escherichia coli alkaline phosphatase.
    Matlin AR, Kendall DA, Carano KS, Banzon JA, Klecka SB, Solomon NM.
    Biochemistry; 1992 Sep 08; 31(35):8196-200. PubMed ID: 1525159
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  • 4. The importance of aspartate 327 for catalysis and zinc binding in Escherichia coli alkaline phosphatase.
    Xu X, Kantrowitz ER.
    J Biol Chem; 1992 Aug 15; 267(23):16244-51. PubMed ID: 1644810
    [Abstract] [Full Text] [Related]

  • 5. Bovine kidney alkaline phosphatase. Catalytic properties, subunit interactions in the catalytic process, and mechanism of Mg2+ stimulation.
    Cathala G, Brunel C.
    J Biol Chem; 1975 Aug 10; 250(15):6046-53. PubMed ID: 238994
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  • 8. Rate-determining step of Escherichia coli alkaline phosphatase altered by the removal of a positive charge at the active center.
    Sun L, Martin DC, Kantrowitz ER.
    Biochemistry; 1999 Mar 02; 38(9):2842-8. PubMed ID: 10052956
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  • 9. Glutamic acid residues as metal ligands in the active site of Escherichia coli alkaline phosphatase.
    Wojciechowski CL, Kantrowitz ER.
    Biochim Biophys Acta; 2003 Jun 26; 1649(1):68-73. PubMed ID: 12818192
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  • 10. A water-mediated salt link in the catalytic site of Escherichia coli alkaline phosphatase may influence activity.
    Xu X, Kantrowitz ER.
    Biochemistry; 1991 Aug 06; 30(31):7789-96. PubMed ID: 1907846
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  • 11. Probing the role of histidine-372 in zinc binding and the catalytic mechanism of Escherichia coli alkaline phosphatase by site-specific mutagenesis.
    Xu X, Qin XQ, Kantrowitz ER.
    Biochemistry; 1994 Mar 01; 33(8):2279-84. PubMed ID: 8117685
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  • 12. Alteration of aspartate 101 in the active site of Escherichia coli alkaline phosphatase enhances the catalytic activity.
    Chaidaroglou A, Kantrowitz ER.
    Protein Eng; 1989 Nov 01; 3(2):127-32. PubMed ID: 2687845
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  • 14. 3-D structure of the D153G mutant of Escherichia coli alkaline phosphatase: an enzyme with weaker magnesium binding and increased catalytic activity.
    Dealwis CG, Chen L, Brennan C, Mandecki W, Abad-Zapatero C.
    Protein Eng; 1995 Sep 01; 8(9):865-71. PubMed ID: 8746724
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  • 16. Conversion of a magnesium binding site into a zinc binding site by a single amino acid substitution in Escherichia coli alkaline phosphatase.
    Murphy JE, Xu X, Kantrowitz ER.
    J Biol Chem; 1993 Oct 15; 268(29):21497-500. PubMed ID: 8407998
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  • 17. Investigation of a catalytic zinc binding site in Escherichia coli L-threonine dehydrogenase by site-directed mutagenesis of cysteine-38.
    Johnson AR, Chen YW, Dekker EE.
    Arch Biochem Biophys; 1998 Oct 15; 358(2):211-21. PubMed ID: 9784233
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  • 18. Kinetics and crystal structure of a mutant Escherichia coli alkaline phosphatase (Asp-369-->Asn): a mechanism involving one zinc per active site.
    Tibbitts TT, Xu X, Kantrowitz ER.
    Protein Sci; 1994 Nov 15; 3(11):2005-14. PubMed ID: 7703848
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  • 19. Glu-416 of beta-galactosidase (Escherichia coli) is a Mg2+ ligand and beta-galactosidases with substitutions for Glu-416 are inactivated, rather than activated, by MG2+.
    Roth NJ, Huber RE.
    Biochem Biophys Res Commun; 1996 Feb 06; 219(1):111-5. PubMed ID: 8619791
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  • 20. Site directed substitutions suggest that His-418 of beta-galactosidase (E. coli) is a ligand to Mg2+.
    Roth NJ, Huber RE.
    Biochem Biophys Res Commun; 1994 Jun 15; 201(2):866-70. PubMed ID: 8003024
    [Abstract] [Full Text] [Related]

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