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211 related items for PubMed ID: 11718552

  • 1. The conserved methionine residue of the metzincins: a site-directed mutagenesis study.
    Hege T, Baumann U.
    J Mol Biol; 2001 Nov 23; 314(2):181-6. PubMed ID: 11718552
    [Abstract] [Full Text] [Related]

  • 2. Protease C of Erwinia chrysanthemi: the crystal structure and role of amino acids Y228 and E189.
    Hege T, Baumann U.
    J Mol Biol; 2001 Nov 23; 314(2):187-93. PubMed ID: 11718553
    [Abstract] [Full Text] [Related]

  • 3. Type II protein secretion in gram-negative pathogenic bacteria: the study of the structure/secretion relationships of the cellulase Cel5 (formerly EGZ) from Erwinia chrysanthemi.
    Chapon V, Czjzek M, El Hassouni M, Py B, Juy M, Barras F.
    J Mol Biol; 2001 Jul 27; 310(5):1055-66. PubMed ID: 11501995
    [Abstract] [Full Text] [Related]

  • 4. Metzincin's canonical methionine is responsible for the structural integrity of the zinc-binding site.
    Oberholzer AE, Bumann M, Hege T, Russo S, Baumann U.
    Biol Chem; 2009 Sep 27; 390(9):875-81. PubMed ID: 19558324
    [Abstract] [Full Text] [Related]

  • 5. Refined 2.0 A X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin.
    Gomis-Rüth FX, Kress LF, Kellermann J, Mayr I, Lee X, Huber R, Bode W.
    J Mol Biol; 1994 Jun 17; 239(4):513-44. PubMed ID: 8006965
    [Abstract] [Full Text] [Related]

  • 6. Site-directed mutagenesis of the active site glutamate in human matrilysin: investigation of its role in catalysis.
    Cha J, Auld DS.
    Biochemistry; 1997 Dec 16; 36(50):16019-24. PubMed ID: 9398337
    [Abstract] [Full Text] [Related]

  • 7. Structural analysis of Sindbis virus capsid mutants involving assembly and catalysis.
    Choi HK, Lee S, Zhang YP, McKinney BR, Wengler G, Rossmann MG, Kuhn RJ.
    J Mol Biol; 1996 Sep 20; 262(2):151-67. PubMed ID: 8831786
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  • 9. Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft.
    Wang WC, Hsu WH, Chien FT, Chen CY.
    J Mol Biol; 2001 Feb 16; 306(2):251-61. PubMed ID: 11237598
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  • 12. The conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroni.
    Nam GH, Cha SS, Yun YS, Oh YH, Hong BH, Lee HS, Choi KY.
    Biochem J; 2003 Oct 15; 375(Pt 2):297-305. PubMed ID: 12852789
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  • 14. 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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  • 15. Effect of the Met344His mutation on the conformational dynamics of bovine beta-1,4-galactosyltransferase: crystal structure of the Met344His mutant in complex with chitobiose.
    Ramakrishnan B, Boeggeman E, Qasba PK.
    Biochemistry; 2004 Oct 05; 43(39):12513-22. PubMed ID: 15449940
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  • 16. Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540.
    Prag G, Papanikolau Y, Tavlas G, Vorgias CE, Petratos K, Oppenheim AB.
    J Mol Biol; 2000 Jul 14; 300(3):611-7. PubMed ID: 10884356
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  • 17. Site-directed mutagenesis of residues in a conserved region of bovine aspartyl (asparaginyl) beta-hydroxylase: evidence that histidine 675 has a role in binding Fe2+.
    McGinnis K, Ku GM, VanDusen WJ, Fu J, Garsky V, Stern AM, Friedman PA.
    Biochemistry; 1996 Apr 02; 35(13):3957-62. PubMed ID: 8672427
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  • 18. Site-directed mutagenesis of active site residues of phosphite dehydrogenase.
    Woodyer R, Wheatley JL, Relyea HA, Rimkus S, van der Donk WA.
    Biochemistry; 2005 Mar 29; 44(12):4765-74. PubMed ID: 15779903
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  • 20. 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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