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Module 1. General principles of metabolism. Metabolism of
Module 1. General principles of metabolism. Metabolism of

... 80. Conserved serine, histidine and aspartate residues are present in the catalytic center of all serine proteases. Which of the following describes the role of the histidine residue in the mechanism of this reaction? A. * Covalent binding of acyl groups B. Hydrophobic stabilization of the substrate ...
CBS (EC 4.2.1.22). The rate equation for the CBS reaction
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... Concentrations of ATP, adenosine, betaine, dimethylglycine, glycine, NADPH, and serine, as well as a total concentration of all intracellular folates (F0) are assumed to be constant. In this way, either there is no dependence of reaction rates on these metabolites, or they are included in the releva ...
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L-Carnitine in human metabolism

... swollen mitochondria seen with electron microscopy (C, D; arrows). Immunohistochemistry with antibodies directed against aldehyde 4-hydroxy-2-nonenal 4HNE (E , F) and sarcoendoplasmic reticulum calcium ATPase SERCA-SO 3 shows increased staining (F, H) compared to normal controls ( E, G) ...
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Universal Functional and Model Consistency Testing
Universal Functional and Model Consistency Testing

... Validation of the myocyte network included simulating the ATP production from one mole of octadecenoate (C18:1), palmitate (C16:0) and pentadecanoate (C15:0) (Table 2). To demonstrate how each of these fatty acids could be catabolized to produce energy, the influx of all other carbon sources includ ...
Hydrogen Bonds
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The exam is worth 200 points, divided into 7 questions. You must do
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Immobilized Enzyme Technology: Potentiality and Prospects
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... 1g). It is different from other techniques in the sense that it does not require a support for the immobilization. There are two methods of cross linking in use, (i) Cross Linking Enzyme Aggregate (CLEA), and (ii) Cross Linking Enzyme Crystals (CLEC). Both CLEA and CLEC are modifications of a primit ...
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...  Fatty acids esterified to CoA are substrates for the ER elongation machinery, which uses malonyl-CoA as donor of 2-carbon units. The reaction sequence is similar to Fatty Acid Synthase but individual steps are catalyzed by separate proteins. A family of enzymes designated Fatty Acid Elongases cata ...
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... [14, 15] and transport through Golgi to the acrosome in male germ cells [15]. The exact reason for the static retention or recycling of cytochromes P450 is not fully understood. ER resident proteins must possess specific motifs, which enable them to be excluded from transport through Golgi to other ...
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... The second step in β-lactam synthesis is the oxidative cyclization of LLDACV into isopenicillin N (IPN). In this step, the bicyclic penam nucleus, consisting of the β-lactam and thiazolidine rings is generated (34, 102). This step is mediated by IPN synthase (IPNS) a protein of 38 kDa that is encode ...
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A generalized stoichiometric model of C3, C2, C2
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... and oxygenation (VO, VC), and PEP carboxylation rate (VP). The ATP and NADPH requirements are SMA outputs and they are not related to light reactions at this stage. Reactions are typically grouped by the biochemical function of the pathways, of which only the entry point is calculated. The SMA is ba ...
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Oxidative phosphorylation



Oxidative phosphorylation (or OXPHOS in short) is the metabolic pathway in which the mitochondria in cells use their structure, enzymes, and energy released by the oxidation of nutrients to reform ATP. Although the many forms of life on earth use a range of different nutrients, ATP is the molecule that supplies energy to metabolism. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is probably so pervasive because it is a highly efficient way of releasing energy, compared to alternative fermentation processes such as anaerobic glycolysis.During oxidative phosphorylation, electrons are transferred from electron donors to electron acceptors such as oxygen, in redox reactions. These redox reactions release energy, which is used to form ATP. In eukaryotes, these redox reactions are carried out by a series of protein complexes within the inner membrane of the cell's mitochondria, whereas, in prokaryotes, these proteins are located in the cells' intermembrane space. These linked sets of proteins are called electron transport chains. In eukaryotes, five main protein complexes are involved, whereas in prokaryotes many different enzymes are present, using a variety of electron donors and acceptors.The energy released by electrons flowing through this electron transport chain is used to transport protons across the inner mitochondrial membrane, in a process called electron transport. This generates potential energy in the form of a pH gradient and an electrical potential across this membrane. This store of energy is tapped by allowing protons to flow back across the membrane and down this gradient, through a large enzyme called ATP synthase; this process is known as chemiosmosis. This enzyme uses this energy to generate ATP from adenosine diphosphate (ADP), in a phosphorylation reaction. This reaction is driven by the proton flow, which forces the rotation of a part of the enzyme; the ATP synthase is a rotary mechanical motor.Although oxidative phosphorylation is a vital part of metabolism, it produces reactive oxygen species such as superoxide and hydrogen peroxide, which lead to propagation of free radicals, damaging cells and contributing to disease and, possibly, aging (senescence). The enzymes carrying out this metabolic pathway are also the target of many drugs and poisons that inhibit their activities.
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