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design of energy metabolism
design of energy metabolism

... Evolutionary trend is toward higher levels of activity in advanced invertebrates. This trend continues throughout vertebrate evolution. Associated with this trend is a tendency for lesser reliance on sustained anaerobic pathways and greater used of arginine phosphate (cephalopods), creatine phosphat ...
You should be able to identify each of the following functional
You should be able to identify each of the following functional

... You should be able to identify each of the following functional groups within organic molecules: amino group within an amine molecule (both the form found at low pH and high pH) carbonyl group within an aldehyde molecule (you need to know it is within an aldehyde vs a ketone) carbonyl group within a ...
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... • The cell’s boundary is made of phospholipids. The structure of cell membranes depends on how this molecule interacts with water. • Waxes, found on the surfaces of plants and aquatic bird feathers, help prevent evaporation of water from the cells of the organism. ...
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... together the remaining exons. Alternative splicing makes it possible to produce different mRNAs from the same primary transcript. Translation is the stage of gene expression when the cell synthesizes proteins according to instructions in the mRNA. a. tRNAs carry amino acids to the translation machin ...
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... What is an Organic Compound? • Anything that contains the following two elements: Carbon & Hydrogen ...
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... this mechanism. LPI is therefore treated by strict avoidance of protein-rich food and supplementation of citrulline. Citrulline is absorbed by neutral amino acid transporters and can subsequently replenish the urea cycle (9). The reduced capacity of the urea cycle probably also causes a compensatory ...
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... a good understanding of the units that make up the protein chain is important. Unlike polysaccharides, which are composed of the same type of unit linked in different ways, protein chains can contain any or all of the naturally-occurring amino acids  Table 20.1: each amino acid makes up somewhere b ...
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Chemistry in Living Things - Mercer Island School District
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... When sugars, proteins or lipids are broken down into their subunits, the opposite process occurs. Water is used in this process to break apart the polymer, so it is called a hydrolysis reaction. ...
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Lecture 4

... amino acids or to the group of uncharged ones, depending on the local pH. Lysine is classified as a charged residue because its terminal amino group is ionized under most physiological conditions, but its sidechain also contains a hydrophobic segment of four methylene groups. Likewise, the arginine ...
University of Groningen Stereoselective synthesis of glycerol
University of Groningen Stereoselective synthesis of glycerol

... cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record ...
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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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