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FIGURE 21–6 Part 1
FIGURE 21–6 Part 1

... stages: (1) synthesis of the 18-carbon amine sphinganine from palmitoyl-CoA and serine; (2) attachment of a fatty acid in amide linkage to yield N-acylsphinganine; (3) desaturation of the sphinganine moiety to form Nacylsphingosine (ceramide); and (4) attachment of a head group to produce a sphingol ...
Chemistry of Carbohydrates
Chemistry of Carbohydrates

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Role of Carnitine in Lipid Metabolism
Role of Carnitine in Lipid Metabolism

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Chapter 4 PPT-VIEW
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Biologically active octapeptides

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heterogeneous chiral catalyst derived from hydrolyzed

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Enzymes - Ústav lékařské chemie a biochemie

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Amines and Amides

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Glucose metabolic flux distribution of Lactobacillus amylophilus

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Method of Analysis for Feed Enzymes: Methodological Problems?
Method of Analysis for Feed Enzymes: Methodological Problems?

... xylanase on arabinoxylan, an amylase on starch, a proteinase on protein) even in the presence of other reactants. Furthermore, the substrate needs to be of a defined quality. For example, similar results are obtained from xylanase with xylan substrates extracted from birchwood or from wheat (Table 1 ...
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Review Questions for Respiration
Review Questions for Respiration

... Circle the correct answer. 1. NAD+ is a (reactant/product) of glycolysis. 2. NAD+ is a (reactant/product) of the link reaction (or the oxidation of pyruvate). 3. NAD+ is a (reactant/product) of the ETC. 4. NAD+ is a (reactant/product) of the Krebs cycle. 5. Water is a (reactant/product) of the ETC. ...
Metabolism of Lipids
Metabolism of Lipids

... a hungry state. In contrast, administration of food after a fast, or of insulin to the diabetic subject, reduces plasma free fatty acid concentrations and increases liver concentration of malonyl-CoA, this will inhibit carnitine acyltransferase I and thus reverses the ketogenic process. ...
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Rubisco

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Bioactivation of Selenocysteine Se-Conjugates by a Highly Purified

... its ability to convert leukotriene E4 and 5⬘-S-cysteinyldopamine and by its lower specific activity toward cysteine conjugates of halogenated alkenes (Abraham et al., 1995). Recently, we demonstrated that replacing the sulfur of cysteine S-conjugates by a selenium atom resulted in a dramatic increas ...
medical chemistry and biochemistry
medical chemistry and biochemistry

... 4. Compare the results of determining formaldehyde, glucose and sucrose by Fehling's reagent. 5. Compare the most important precipitation and colored chemical reactions for detecting proteins. 6. Compare the results of determining glycine and proteins using the ninhindrin reaction. 7. Analyse variou ...
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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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