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2.3 Carbon-Based Molecules
2.3 Carbon-Based Molecules

... • Lipids are nonpolar molecules that include fats, oils, and cholesterol. – Many contain carbon chains called fatty acids. – Fats and oils contain fatty acids bonded to glycerol. Triglyceride ...
Chapter 12 Pathways to biomolecules
Chapter 12 Pathways to biomolecules

... lactase – which breaks down the sugar lactose in the small intestine salivary amylase – which breaks down polysaccharides in the mouth. Almost all the chemical reactions occurring in living creatures are controlled by enzymes. Enzymes speed up the reactions that are essential for life processes by a ...
ppt - UGA CAES - University of Georgia
ppt - UGA CAES - University of Georgia

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... superscript negative sign, as in Cl– or O2b. An ionic bond is formed when positive and negative ions attract each other; the number of ions used is what is needed to maintain electrical neutrality c. ...
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Biotechnology and the manufacturing industry
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No Slide Title

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Kreb`s Cycle - Montgomery College

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Relative Reactivity of Amino Acids with Chlorine

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...  Fumarate produced in the argininosuccinase reaction is also an intermediate of the citric acid cycle, the cycles are interconnected in process dubbed the “Krebs bicycle”.  Each cycle can operate independently and connection between them depends on the transport of the intermediates between the mi ...
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49. enzyme review - Khan Usman Ghani

... accelerates the rate of reaction. Enzymes act on substrate as a result substrate is converted to product. Substrate binds on active site of enzymes that is specific for substrate (Hansen et al., 1990). Enzymes increases or decreases rate of reaction by increasing or decreasing the energy of activati ...
Enzyme basic concepts, Enzyme Regulation IIII
Enzyme basic concepts, Enzyme Regulation IIII

... Generally involves allosteric enzymes and occurs when the end­product of a pathway  inhibits its own synthesis.  Usually the inhibitor inhibits the earlier steps in the pathway  or reactions at a branching point. A very important way of saving cellular energy in  biosynthetic pathways. Example: Nega ...
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enzymes - MrsGorukhomework

... Controls metabolic pathways. It is a type of non-competitive inhibition that regulates enzymes. Many enzymes have Allosteric sites – not active sites- molecules fit into these sites and either activate or inhibit the enzyme by slightly changing the shape. Eg. As the product builds up, the product wi ...
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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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