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Resistance to Antibiotics Mediated by Target Alterations
Resistance to Antibiotics Mediated by Target Alterations

... catalyze the final cross-linking reactions of peptidoglycan synthesis (9). Penicillin inhibits these enzymes by acting as a structural analog, forming an irreversible penicilloyl-enzyme complex that is analogous to the transient acyl-enzyme formed during the normal transpeptidation reaction. Transpe ...
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... (kD) and 18 kD when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Time, course experiments indicate that the latter is a modification derivative of the 14-kD peptide after the removal of the transit peptide. Substitution of serine 38 by alanine, eliminating the phosphopantet ...
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... S1). Our results indicate that glutamate, leucine, alanine and glutamine are much more abundant in the rod domain, and serine and glycine are most frequently found in both the head and tail domains (Fig. 1; P,0.001 for all comparisons). Lysine and arginine are also common, particularly in both rod a ...
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... Step 3. The third step is the phosphorylation of fructose-6-phosphate, catalyzed by the enzyme phosphofructokinase. A second ATP molecule donates a high-energy phosphate to fructose-6-phosphate, producing fructose-1,6-bisphosphate. In this pathway, phosphofructokinase is a rate-limiting enzyme. It i ...
Enzymatic Protein Deglycosylation Kit (EDEGLY)
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... are resistant to PNGase F. Endoglycosidase A, isolated from almond meal, must be used in this situation.5 This enzyme, however, is ineffective when sialic acid is present on the N-linked oligosaccharide. Steric hindrance slows or inhibits the action of PNGase F on certain residues of glycoproteins. ...
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Amino acid synthesis

Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids. Humans are excellent example of this, since humans can only synthesise 11 of the 20 standard amino acids (aka non-essential amino acid), and in time of accelerated growth, arginine, can be considered an essential amino acid.A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.In amino acid production, one encounters an important problem in biosynthesis, namely stereochemical control. Because all amino acids except glycine are chiral, biosynthetic pathways must generate the correct isomer with high fidelity. In each of the 19 pathways for the generation of chiral amino acids, the stereochemistry at the α-carbon atom is established by a transamination reaction that involves pyridoxal phosphate. Almost all the transaminases that catalyze these reactions descend from a common ancestor, illustrating once again that effective solutions to biochemical problems are retained throughout evolution.Biosynthetic pathways are often highly regulated such that building-blocks are synthesized only when supplies are low. Very often, a high concentration of the final product of a pathway inhibits the activity of enzymes that function early in the pathway. Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species. These enzymes are similar in functional properties to aspartate transcarbamoylase and its regulators. Feedback and allosteric mechanisms ensure that all twenty amino acids are maintained in sufficient amounts for protein synthesis and other processes.
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