نتایج جستجو برای: glutamine synthetase activity
تعداد نتایج: 1155348 فیلتر نتایج به سال:
The activity of micrococcal nuclease was studied on a novel substrate, denatured adenylylated glutamine synthetase [L-glutamate:ammonia ligase (ADP-forming), EC 6.3.1.2], which contains a unique tyrosyl residue linked through a phosphodiester bond to 5'-AMP. The products of the digestion were adenosine and O-phosphotyrosylglutamine synthetase. The Km of the macromolecular substrate with the nuc...
Mixed-function oxidation of glutamine synthetase from Escherichia coli causes loss of catalytic activity. The inactivation correlates with the loss of 1 of 16 histidine residues/subunit (Levine, R.L. (1983) J. Biol. Chem. 258, 11823-11827). A cyanogen bromide peptide containing the oxidizable histidine has been isolated. Within the protein, the sequence is Met-His-Cys-His-Met. This hydrophilic ...
We studied the effects of oral administration of RU38486, a potent and selective glucocorticoid antagonist, on muscle weight, non-collagen protein content, and selected enzyme activities (choline acetyltransferase, glucose-6-phosphate dehydrogenase, and glutamine synthetase) following denervation of rat skeletal muscle. Neither decreases in muscle weight, protein content, and choline acetyltran...
Rhodopseudomonas palustris, Glutamine Synthetase Regulation, Adenylylation Glutamine synthetase from Rhodopseudomonas palustris is regulated via an adenylylation/ deadenylylation mechanism. The enzyme purified from ammonia-grown cells, released AMP upon treatment with phosphodiesterase, along with drastic changes in its pH and metal dependency. Kinetic parameters for enzyme-substrate interactio...
New antibiotics to combat the emerging pandemic of drug-resistant strains of Mycobacterium tuberculosis are urgently needed. We have investigated the effects on M. tuberculosis of phosphorothioatemodified antisense oligodeoxyribonucleotides (PS-ODNs) against the mRNA of glutamine synthetase, an enzyme whose export is associated with pathogenicity and with the formation of a poly-L-glutamateyglu...
Characterization of a novel dUTP-dependent activity of CTP synthetase from Saccharomyces cerevisiae.
CTP synthetase [EC 6.3.4.2, UTP:ammonia ligase (ADP-forming)] from the yeast Saccharomyces cerevisiae catalyzes the ATP-dependent transfer of the amide nitrogen from glutamine to the C-4 position of UTP to form CTP. In this work, we demonstrated that CTP synthetase utilized dUTP as a substrate to synthesize dCTP. The dUTP-dependent activity was linear with time and with enzyme concentration. Ma...
Helicobacter pylori urease, produced in abundance, is indispensable for the survival of H. pylori in animal hosts. Urea is hydrolyzed by the enzyme, resulting in the liberation of excess ammonia, some of which neutralizes gastric acid. The remaining ammonia is assimilated into protein by glutamine synthetase (EC 6.3.1.2), which catalyzes the reaction: NH3 + glutamate + ATP-->glutamine + ADP + P...
Glutamine is an essential amino acid for the enterocytes with respect to maintaining the gut mucosal integrity and function. This study was conducted to explore a molecular basis for the beneficial effects of glutamine on intestinal cells by searching for glutamine-dependent changes in the proteome. Caco-2 cells were exposed to different concentrations of L-glutamine with or without L-methionin...
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