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Module 3- Bioenergetics - Bangen Athletic Development
Module 3- Bioenergetics - Bangen Athletic Development

... acids. There are nine essential amino acids (histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine) and eleven nonessential amino acids (alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glycine, glutamine, proline, serine and tyros ...
Chem*3560 Lecture 11: Regulation by proteolytic cleavage
Chem*3560 Lecture 11: Regulation by proteolytic cleavage

... is structurally equivalent to Lys6 and Ile7 in trypsinogen. The newly exposed N-terminal Ile is similarly positioned to make an ion pair with Asp 194, and the mechanism of activation is the same as for trypsin. The immediate product is called π -chymotrypsin and is fully active as a protease. Self-e ...
AP BIOLOGY – CHAPTER 7 Cellular Respiration Outline
AP BIOLOGY – CHAPTER 7 Cellular Respiration Outline

... 4. NADH gives up its electrons and becomes NAD+; next carrier gains electrons and is reduced. 5. At each sequential oxidation-reduction reaction, energy is released to form ATP molecules. 6. Oxygen serves as terminal electron acceptor and combines with hydrogen ions to form water. 7. Because O2 must ...
chapt05_lecture
chapt05_lecture

... excreted as urea in the urine. b. Oxidative deamination sometimes forms pyruvic acid or another citric acid cycle intermediates. 1) These can be used to make energy or converted to glucose or fat. 2) The formation of glucose from amino acids is called gluconeogenesis and occurs in the Cori cycle. 3) ...
Partial Purification and Characterization of the Maize Mitochondrial
Partial Purification and Characterization of the Maize Mitochondrial

pyruvate dehydrogenase complex
pyruvate dehydrogenase complex

... fluoroacetyl CoA, which condenses with OAA to form fluorocitrate, a potent inhibitor of aconitase, resulting in citrate accumulation D. Oxidation and decarboxylation of isocitrate - Isocitrate dehydrogenase catalyzes the irreversible oxidative decarboxylation of isocitrate, yielding the 1st of three ...
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... The tRNA molecule • tRNA molecules do the final translating • At one end the have a specific amino acid attached by a tRNA activating enzyme These enzymes do the first part of translating • At the other end they have an anticodon which is complementary to the mRNA codons © 2007 Paul Billiet ODWS ...
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... formation of a stable organic matter fraction, humus. Humus turns over slowly, at a rate of 3 to 5% per year. In addition to mineralization to CO2, a number of small carbon molecules are formed largely as a result of anaerobic activities and in some instances as a result of anthropogenic activity. T ...
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... (activate) for binding to the AMPK allosteric sites determines the activity of AMPK 1. When [ATP] is high, AMPK is inactive 2. When [AMP] is high, AMPK is allosterically activated and phosphorylates many targets controlling cellular energy production and consumption ...
The 92-kDa chitinase from Streptomyces olivaceoviridis contains a
The 92-kDa chitinase from Streptomyces olivaceoviridis contains a

... 92-kDa chitinase against casein are very similar when the different molecular masses are considered (Table 2) but were much lower than with trypsin (6600 mU nmol-t). The same is true for the four S. olivaceoviridis enzymes when the chromogenic substrates Tosyl-Gly-Pro-Lys-4-nitranilide-acetate (Chro ...
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... • Proteins must be digested to amino acids; amino groups can feed glycolysis or the citric acid cycle ...
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... Protein inhibitors regulate the activity of proteases involved in biochemical processes such as blood clotting, complement system, digestion, inflammation, apoptosis and others. In the case of protease inhibitor deficiency, some diseases may appear. Currently some attempts have been made in the ther ...
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... al., 1995; Boatright and Salvesen, 2003). The method has been proposed as a way to rapidly profile enzyme active sites ex vivo (Liu et al., 1999) and analyze the activity status of a proteasome (Bogyo et al., 1997). Presumably, the activity of paracaspase, which seems to be cryptic in the sense that ...
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... 244]. Molecular regulation of penicillin biosynthesis has been studied extensively in A. nidulans. Like P. chrysogenum, A. nidulans belongs to the class of Plectomycetes and is able to produce hydrophobic penicillins. However, while P. chrysogenum lacks a sexual cycle and is not amendable to classic ...
Bonds and Structural Supports - MSOE Center for BioMolecular
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... When a model is built on a 3D printer, additional support struts are added within the model to provide stability and durability. Struts can be automatically added using the calculate struts command. This command will only add struts to the currently selected area of a molecular structure. If you hav ...
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Uptake of organic nitrogen by plants

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... - High Km higher concentration of glucose to reach half-saturation function only when the conc- of glucose in hepatocyte increased - has high Vmax  allow to phosphorylate large amount of glucose effectively and this prevent large amount of glucose from entering the system circulation following CH ...
1. Introduction to Natural Products Chemistry
1. Introduction to Natural Products Chemistry

... via more than one biosynthetic path. That is, there may be more than one path available, such as in a modified linear process or metabolic grid. 5. Even if the same compound is present in two different organisms, it is possible that they are formed via different pathways. This, however, is more like ...
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S08 Glycolysis

... - High Km higher concentration of glucose to reach half-saturation function only when the conc- of glucose in hepatocyte increased - has high Vmax  allow to phosphorylate large amount of glucose effectively and this prevent large amount of glucose from entering the system circulation following CH ...
Biochemistry 7/e
Biochemistry 7/e

Dihydrofolate Reductase Assay Kit (CS0340) - Bulletin - Sigma
Dihydrofolate Reductase Assay Kit (CS0340) - Bulletin - Sigma

... present in all eukaryotic and prokaryotic cells, playing a key role in thymidine synthesis. It catalyzes the reduction of 7,8-dihydrofolate (DHF) to 5,6,7,8tetrahydrofolate (THF), utilizing NADPH as cofactor. This reaction is an essential step in the biosynthesis of ...
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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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