Global ETD Search
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Showing 1 to 5 of 5 for “"adenylylation"”.
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DNA enzymes for tyrosine PEGylation and azido-adenylylation of peptide and protein substrates
… onto the tyrosine hydroxyl group (azido-adenylylation). Second, a particular modification of interest is attached to the azido group by copper-catalyzed azide-alkyne cycloaddition (CuAAC) using an alkyne-functionalized reagent. Eleven deoxyribozymes with azido-adenylylation activity are …
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Studies of protein complexes involved in the adenylation cascade of the nitrogen signalling pathway in Escherichia coli.
… bifunctional enzyme that catalyses the opposing adenylylation and deadenylylation of glutamine synthetase (GS). The overall aim of this thesis was elucidation of the molecular mechanisms of the adenylylation cascade. A new central domain has been identified using ATase truncation constructs in …
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In vitro selection of deoxyribozymes for O-glycoside cleavage and for 3-nitrotyrosine modification
… of deoxyribozymes for 3-nitrotyrosine azido-adenylylation described in Chapter 4. Previous research had identified deoxyribozymes for tyrosine azido-adenylylation. The hydroxyl group of 3-nitrotyrosine is many orders of magnitude less reactive than that of tyrosine. In addition to potential …
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Elucidation of the reaction mechanisms involved in the catalysis mediated by glutamine synthetase in Escherichia coli
… indicates that a possible mechanism by which the adenylylation/deadenylylation of the enzyme affects the enzyme specificity for either MgATP or Mn2ATP and NH4+ or NH3, is by switching between two putative serine protease-like catalytic triads. Site-directed mutagenesis of a number of residues …
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Post-translational regulation of BiP by FICD-mediated AMPylation and deAMPylation
Regulation of the amount and activity of Binding Immunoglobulin Protein (BiP) contributes to protein-folding homeostasis. BiP’s abundance is modulated transcriptionally by the canonical unfolded protein response (UPR). Conversely, a metazoan-specific, endoplasmic reticulum (ER)-resident, Fic domain …