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Journal Abstract Search

134 related items for PubMed ID: 1480614

  • 1.
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  • 3. Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102.
    Stec B, Hehir MJ, Brennan C, Nolte M, Kantrowitz ER.
    J Mol Biol; 1998 Apr 03; 277(3):647-62. PubMed ID: 9533886
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  • 4. Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase.
    Le Du MH, Lamoure C, Muller BH, Bulgakov OV, Lajeunesse E, Ménez A, Boulain JC.
    J Mol Biol; 2002 Mar 01; 316(4):941-53. PubMed ID: 11884134
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  • 5. 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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  • 6. Structure and mechanism of alkaline phosphatase.
    Coleman JE.
    Annu Rev Biophys Biomol Struct; 1992 Nov 01; 21():441-83. PubMed ID: 1525473
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  • 8. 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
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  • 9. 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
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  • 10. 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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  • 11. Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sites.
    Ma L, Kantrowitz ER.
    Biochemistry; 1996 Feb 20; 35(7):2394-402. PubMed ID: 8652582
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  • 12. A revised mechanism for the alkaline phosphatase reaction involving three metal ions.
    Stec B, Holtz KM, Kantrowitz ER.
    J Mol Biol; 2000 Jun 23; 299(5):1303-11. PubMed ID: 10873454
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  • 13. Mutagenesis of conserved residues within the active site of Escherichia coli alkaline phosphatase yields enzymes with increased kcat.
    Mandecki W, Shallcross MA, Sowadski J, Tomazic-Allen S.
    Protein Eng; 1991 Oct 23; 4(7):801-4. PubMed ID: 1798702
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  • 14. 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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  • 15. Improving Escherichia coli alkaline phosphatase efficacy by additional mutations inside and outside the catalytic pocket.
    Muller BH, Lamoure C, Le Du MH, Cattolico L, Lajeunesse E, Lemaître F, Pearson A, Ducancel F, Ménez A, Boulain JC.
    Chembiochem; 2001 Aug 03; 2(7-8):517-23. PubMed ID: 11828484
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  • 16. Functional interrelationships in the alkaline phosphatase superfamily: phosphodiesterase activity of Escherichia coli alkaline phosphatase.
    O'Brien PJ, Herschlag D.
    Biochemistry; 2001 May 15; 40(19):5691-9. PubMed ID: 11341834
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  • 17. Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase.
    Tibbitts TT, Murphy JE, Kantrowitz ER.
    J Mol Biol; 1996 Apr 05; 257(3):700-15. PubMed ID: 8648634
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  • 18. 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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  • 19. Function of arginine-166 in the active site of Escherichia coli alkaline phosphatase.
    Chaidaroglou A, Brezinski DJ, Middleton SA, Kantrowitz ER.
    Biochemistry; 1988 Nov 01; 27(22):8338-43. PubMed ID: 3072019
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  • 20. 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
    [Abstract] [Full Text] [Related]

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