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While specific steps in protein synthesis affected may vary somewhat between specific aminoglycoside agents, as can their affinity and degree of binding, [8] aminoglycoside presence in the cytosol generally disturbs peptide elongation at the 30S ribosomal subunit, giving rise to inaccurate mRNA translation and therefore biosynthesis of proteins ...
A protein synthesis inhibitor is a compound that stops or slows the growth or proliferation of cells by disrupting the processes that lead directly to the generation of new proteins. [1] A ribosome is a biological machine that utilizes protein dynamics on nanoscales to translate RNA into proteins
A classic example of this effect is the interaction between β-lactams, which damage the bacteria cell membrane, and aminoglycosides, which inhibit protein synthesis. [1] The damage dealt to the cell wall by β-lactams allows more aminoglycoside molecules to be taken up into the cell than would otherwise be possible, enhancing cell damage. [1]
Aminoglycoside-3'-phosphotransferase (APH(3')), also known as aminoglycoside kinase, is an enzyme that primarily catalyzes the addition of phosphate from ATP to the 3'-hydroxyl group of a 4,6-disubstituted aminoglycoside, such as kanamycin. [2]
In enzymology, an aminoglycoside N6'-acetyltransferase (EC 2.3.1.82) is an enzyme that catalyzes the chemical reaction. acetyl-CoA + kanamycin-B CoA + N 6 '-acetylkanamycin-B. Thus, the two substrates of this enzyme are acetyl-CoA and kanamycin B, whereas its two products are CoA and N6'-acetylkanamycin-B.
AMPylator setting up target protein with ATP for AMPylation reaction. Adenylylation, [1] [2] more commonly known as AMPylation, is a process in which an adenosine monophosphate (AMP) molecule is covalently attached to the amino acid side chain of a protein. [3]
I thought: ‘Maybe I will be able to step into that frame’.” The Oscar-winning star caused quite a frenzy at the festival on Saturday, with ticket holders fighting to secure a good spot in ...
Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...