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499 Med Chem Chap 3 problems
499 Med Chem Chap 3 problems

... 07) Which of the following descriptions best describes a coenzyme? a. A non-protein substance that is required by an enzyme if it is to catalyse a reaction. b. A non-protein organic molecule that is required by some enzymes in order to catalyse a reaction on a substrate. c. A non-protein organic mol ...
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... acholeplasmas from animal mycoplasmas is their codon usage; animal mycoplasmas use the UGA stop codon, in addition to UGG, as a tryptophan codon, whereas acholeplasmas use only UGG [6-9]. No protein gene sequence information has been available from any plant-pathogenic MLO, and thus their codon usag ...
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What`s so great about Protein

... Proteins are compounds that are made by linking together amino acids into chains-like structures called peptides. One amino acid is joined to a second; a third is then added to the first two and so on. The bonds between amino acids are called peptide bonds. Peptides are then linked together into lon ...
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chapter 20 lecture (ppt file)

... Regulation, cont. With feedback inhibition, a product in a series of enzyme-catalyzed reactions serves as an inhibitor for a previous allosteric enzyme in the series. A zymogen is a preenzyme. It is coinverted to its active form, usually by hydrolysis, at the active site in the cell. E. g. Pepsinog ...


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عرض تقديمي من PowerPoint

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Chapter 17 - FIU Faculty Websites

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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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