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Journal Abstract Search

282 related items for PubMed ID: 8648634

  • 1. 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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  • 2. 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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  • 3. 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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  • 4. 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 JE, Tibbitts TT, Kantrowitz ER.
    J Mol Biol; 1995 Nov 03; 253(4):604-17. PubMed ID: 7473737
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  • 5. Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase.
    Wang J, Stieglitz KA, Kantrowitz ER.
    Biochemistry; 2005 Jun 14; 44(23):8378-86. PubMed ID: 15938627
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  • 8. Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli.
    Martí-Arbona R, Fresquet V, Thoden JB, Davis ML, Holden HM, Raushel FM.
    Biochemistry; 2005 May 17; 44(19):7115-24. PubMed ID: 15882050
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  • 10. Structural principles for the inhibition of the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I by phosphorothioates.
    Brautigam CA, Steitz TA.
    J Mol Biol; 1998 Mar 27; 277(2):363-77. PubMed ID: 9514742
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  • 11. Structure and mechanism of alkaline phosphatase.
    Coleman JE.
    Annu Rev Biophys Biomol Struct; 1992 Mar 27; 21():441-83. PubMed ID: 1525473
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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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  • 14. 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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  • 15. 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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  • 16. Structures of normal single-stranded DNA and deoxyribo-3'-S-phosphorothiolates bound to the 3'-5' exonucleolytic active site of DNA polymerase I from Escherichia coli.
    Brautigam CA, Sun S, Piccirilli JA, Steitz TA.
    Biochemistry; 1999 Jan 12; 38(2):696-704. PubMed ID: 9888810
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  • 19. Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase.
    Joshi MD, Sidhu G, Pot I, Brayer GD, Withers SG, McIntosh LP.
    J Mol Biol; 2000 May 26; 299(1):255-79. PubMed ID: 10860737
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