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Showing 1 to 20 of 29 for “"catalytic triad"”.

  1. Structural Analysis of Cycle Inhibiting Factor from Pathogenic Escherichia Coli

    … of enzymes sharing a common Cys-His-Asp/Asn catalytic triad, which includes cysteine proteases and acetyltransferases. Mutation of these conserved active site residues abolishes the ability of Cif to block cell cycle progression in different models. We demonstrate that Cif possesses …

    rockefeller Repository record for Structural Analysis of Cycle Inhibiting Factor from Pathogenic Escherichia Coli (opens in a new tab)

  2. Elucidating the Roles of Conserved Active Site Amino Acids in the Escherichia coli Cytochrome c Nitrite Reductase

    … an active site cavity dominated by a conserved catalytic triad of histidine, tyrosine and arginine residues. The role of the catalytic triad of Escherichia coli NrfA has been explored by generating NrfA variants. Three NrfA variants were studied in which a single active site residue was …

    east-anglia Repository record for Elucidating the Roles of Conserved Active Site Amino Acids in the Escherichia coli Cytochrome c Nitrite Reductase (opens in a new tab)

  3. Elucidation of the reaction mechanisms involved in the catalysis mediated by glutamine synthetase in Escherichia coli

    … between two putative serine protease-like catalytic triads. Site-directed mutagenesis of a number of residues identiï¬ ed as playing a role in these catalytic triads, led to the following observations. Both Ser52 and Ser53 were important for the catalytic activity of the enzyme. It was …

    cape-town Repository record for Elucidation of the reaction mechanisms involved in the catalysis mediated by glutamine synthetase in Escherichia coli (opens in a new tab)

  4. Quaternary structures of the cyanide dihydratases of Bacillus pumilus C1 and Pseudomonas stutzeri AK61

    … believed to have in common a unique cys-glu-Iys catalytic triad. Many nitrilases exiat as a large molecular weight oligomers of more than 300kDa. In the current study the structures of two cyanide dihydratases, from Pseudomonas stutzeri AK61 and Bacillus pumilus Cl, have solved at a resolution …

    cape-town Repository record for Quaternary structures of the cyanide dihydratases of Bacillus pumilus C1 and Pseudomonas stutzeri AK61 (opens in a new tab)

  5. The Structural and Biochemical Characterization of Salmonella Host Specificity Determinant Gifsy-2 Gene E

    … and in vitro activity assays, we established the catalytic triad of GtgE, Cys45-His151-Asp169. We also examined a panel of cysteine protease inhibitors and found that N-ethylmaleimide, chymostatin, and antipain were capable of inhibiting GtgE activity in vitro. Furthermore, through work with the …

    rockefeller Repository record for The Structural and Biochemical Characterization of Salmonella Host Specificity Determinant Gifsy-2 Gene E (opens in a new tab)

  6. DJ-1 AND ATP13A2: TWO PROTEINS INVOLVED IN PARKINSON’S DISEASE

    … including a conserved cysteine residue, a catalytic triad, and the ability to form oligomers. Whereas PH1704, a bacterial protease and a member of the DJ-1/ThiJ/PfpI superfamily, adopts a hexameric structure that is necessary for the formation of a catalytic triad, DJ-1 exists as a …

    purdue-thes Repository record for DJ-1 AND ATP13A2: TWO PROTEINS INVOLVED IN PARKINSON’S DISEASE (opens in a new tab)

  7. Isolation, expression, purification and characterisation of a novel acetyl xylan esterase from streptomyces species ORS10

    … conserved domain and a typical AXEase catalytic triad. The axe10 gene was sub-cloned into an expression vector [pET21a(+)] and a 28.7 kDa protein with demonstrated AXE activity was purified from E. coli Rosetta (DE3) pLysS. Axe10 displayed optimum activity at 37oC and pH 7.0. Despite …

    western-cape Repository record for Isolation, expression, purification and characterisation of a novel acetyl xylan esterase from streptomyces species ORS10 (opens in a new tab)

  8. Exploring the emergence of pesticide degradation in the α/β hydrolase superfamily

    … Charting new mechanistic solutions for biocatalytic challenges is a core obstacle in the constant evolutionary adaptation of living organisms. If understood and harnessed, these processes hold the potential to revolutionise industrial processes in the chemical and pharmaceutical industry. …

    cambridge Repository record for Exploring the emergence of pesticide degradation in the α/β hydrolase superfamily (opens in a new tab)

  9. Structural studies of the YedU stress protein

    … the second smaller domain, there is a putative catalytic triad composed of Cys184, His185, and Asp213. A metal-binding site was identified, where a zinc(II) ion is coordinated by a 2-His-1-carboxylate motif composed of His85, Glu90, and His122. The possible functions of the metal-binding site …

    utmb Repository record for Structural studies of the YedU stress protein (opens in a new tab)

  10. Novel imprinted polymers as artificial enzymes

    … models for the Asp-His couple found in the catalytic triad of serine proteases. A combination of molecular dynamics and IH NMR spectroscopy suggested that the most populous conformations of N-acetyl-L-histidine and the N-acetyl-L-histidine anion were predominated by those in which the …

    aston Repository record for Novel imprinted polymers as artificial enzymes (opens in a new tab)

  11. Structural and Functional Characterization of B. Anthracis Udp-Glcnac 2-Epimerase and Salmonella Secreted Effector I

    … of direct contact between an allosteric and catalytic substrate molecule. Arg210 was identified as a critical residue for both binding sites. Furthermore, the structure was used to design an inhibitor that would bind to the conserved bacterial allosteric site and inhibit epimerase activity. …

    rockefeller Repository record for Structural and Functional Characterization of B. Anthracis Udp-Glcnac 2-Epimerase and Salmonella Secreted Effector I (opens in a new tab)

  12. A Characterization of Aspartyl Peptidases in Salmonella Typhimurium

    … that in this family of enzymes both the catalytic and the substrate specificity have been conserved. An alignment of the amino acid sequences of the Peptidase E family allowed for potentially important residues to be identified. Through site-directed mutagenesis of the S. typhimurium …

    uiuc Repository record for A Characterization of Aspartyl Peptidases in Salmonella Typhimurium (opens in a new tab)

  13. Characterization of Novel Urethanases and a Commercial Cutinase for the Degradation of Polyurethane

    … candidates possess a conserved Ser- cisSer-Lys catalytic triad characteristic of the Amidase Signature family, preliminary efforts to assay partially purified WprA demonstrated significant activity on substrates of interest. Specifically, opaque Impranil dispersions were cleared by treatment …

    queens Repository record for Characterization of Novel Urethanases and a Commercial Cutinase for the Degradation of Polyurethane (opens in a new tab)

  14. Novel Sulfated 4-Hydroxycinnamic Acid Oligomers as Potent Anticoagulants

    … CDs interacts with exosite II and disrupts the catalytic triad of thrombin. These results indicate that the preferred mechanism of CDs action is exosite II mediated allosteric disruption of thrombin. CDs appears to be the first exosite II mediated DTI and this represents a novel mechanism of …

    vcu Repository record for Novel Sulfated 4-Hydroxycinnamic Acid Oligomers as Potent Anticoagulants (opens in a new tab)

  15. Structural and Biochemical Characterization of N-Terminal Protease of Classical Swine Fever Virus

    … core protein for viral assembly. The predicted catalytic triad of Npro is Glu22, His49 and Cys69, which differs from the known catalytic triads in either serine or cysteine proteases. Due to its unique sequence and catalytic site, Npro forms its own cysteine protease family C53. After the …

    utmb Repository record for Structural and Biochemical Characterization of N-Terminal Protease of Classical Swine Fever Virus (opens in a new tab)

  16. Characterization of BphD, a C-C bond hydrolase involved in the degradation of polychlorinated biphenyls

    … benzoate. Although MCP hydrolases contain the catalytic triad (Ser112-His265-Asp237) and structural fold of the α/β-hydrolase superfamily, previous studies suggest they deviate from the classical hydrolytic mechanism in two respects: (1) enol-keto tautomerization precedes hydrolysis and (2) …

    ubc Repository record for Characterization of BphD, a C-C bond hydrolase involved in the degradation of polychlorinated biphenyls (opens in a new tab)

  17. Deciphering the role of Hsp31 as a multitasking chaperone

    … in solution. It possesses the Cys-His-Glu catalytic triad common to ThiJ/DJ-1/PfpI superfamily proteins. Previously, we have shown that Hsp31 possesses chaperone properties with protective effects against α-syn toxicity in yeast. Recently, it is shown that Hsp31 has a methylglyoxalase …

    purdue-thes Repository record for Deciphering the role of Hsp31 as a multitasking chaperone (opens in a new tab)

  18. Studies on cathepsin B of Eimeria tenella and pyroglutamyl peptidase of Leishmania major

    … with those of mammalian PPIs. The active site catalytic triad E101, C210, and H234 (L. major PPI numbering) was confirmed by mutagenesis. The PPI activity was detected in L. major promastigotes, and the enzyme localised to the parasite cytoplasm. PPI knockout mutants were generated, and …

    glasgow Repository record for Studies on cathepsin B of Eimeria tenella and pyroglutamyl peptidase of Leishmania major (opens in a new tab)

  19. Identification and characterisation of proteases in Mycobacterium tuberculosis

    … serine proteases and contained the classic catalytic triad and oxyanion hole. Mycosin-1 also contained a typical signal peptide, a likely propeptide, and a Cterminal hydrophobic sequence with a high transmembrane potential. Topology analyses predicted mycosin-1 to be a type I ectoprotein. …

    cape-town Repository record for Identification and characterisation of proteases in Mycobacterium tuberculosis (opens in a new tab)

  20. A COMPARATIVE ANALYSIS OF INTRACELLULAR CHOLESTEROL ESTERIFYING ENZYMES IN MAMMALS

    … the active site of ACAT enzymes may comprise a catalytic triad of serine, histidine and aspartic acid residues. Results showed that in ACAT1, S456, H460 and D400 are essential for activity of the enzyme. In contrast, in ACAT2, only the analogous H438 was identified to be necessary for enzymatic …

    wfu Repository record for A COMPARATIVE ANALYSIS OF INTRACELLULAR CHOLESTEROL ESTERIFYING ENZYMES IN MAMMALS (opens in a new tab)

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