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... 7. Effect of pH on Enzymes Enzymes work best within a range of pH depending on the type of enzyme. The pH that the enzymes works best at is called it’s Optimum pH If the pH is too high, the enzymes active site changes shape (denatured) What is the optimum pH of this enzyme ? ...
Vitamin B12 deficiency, methylmalonic acidemia
Vitamin B12 deficiency, methylmalonic acidemia

... THF methyltransferase reaction is the major and perhaps the only, metabolic reaction that can use 5-methyl THF. If this reaction is blocked or slowed down as a result of a deficiency of vitamin B12, 5-methyl THF accumulates and the THF needed for other folate-requiring reactions is not formed. Event ...
Pseudo-Replication of [GADV]-Proteins and Origin of Life
Pseudo-Replication of [GADV]-Proteins and Origin of Life

... larger than those (in parentheses) of four amino acids, Gly (10), Ala (13), Asp (16) or Val (19). This means that the nucleotides are far more complex than the four amino acids. The nucleotides would never be synthesized under pre-biotic conditions through a random combinatory process [4]. Moreover, ...
Nuclear Magnetic Resonance (NMR) Spectroscopy
Nuclear Magnetic Resonance (NMR) Spectroscopy

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What is Ketosis

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Differences in the amino acid composition of muscles from pheasant
Differences in the amino acid composition of muscles from pheasant

... broiler chickens of similar bodyweight. Changes in chemical composition of meat from pheasant and broiler chickens in the course of feeding was studied by VEČEREK et al. (2005). It follows from their results that chemical composition of pheasant meat significantly changes during growth. From a diete ...
Lipid Metabolism - Creighton Chemistry Webserver
Lipid Metabolism - Creighton Chemistry Webserver

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Pyruvate Oxidation and the Krebs Cycle
Pyruvate Oxidation and the Krebs Cycle

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Amino Acids [PDF:247KB]
Amino Acids [PDF:247KB]

... portion (Amino Acid Table 1) and per 1 g of reference nitrogen (Amino Acid Table 2), consistent with the Food Composition Tables 2015. Additionally, the weights per 1 g of protein, calculated as the sum of amino acid residues (Amino Acid Table 3) and per 1 g of protein, calculated from reference nit ...
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A report on TAK-875 analysis using the Heptox Virtual Liver Platform

Lecture 7: Metabolic Regulation - University of California, Berkeley
Lecture 7: Metabolic Regulation - University of California, Berkeley

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Hexokinase
Hexokinase

... Figure 18.19 The conversion of phosphoenolpyruvate (PEP) to pyruvate may be viewed as involving two steps: phosphoryl transfer, followed by an enol-keto tautomerization. The tautomerization is spontaneous and accounts for much of the free energy change for PEP hydrolysis. ...
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Coenzymes and Cofactors (PDF Available)

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CHAP NUM="9" ID="CH
CHAP NUM="9" ID="CH

...  Figure 9.20 The catabolism of various molecules from food. Carbohydrates, fats, and proteins can all be used as fuel for cellular respiration. Monomers of these molecules enter glycolysis or the citric acid cycle at various points. Glycolysis and the citric acid cycle are catabolic funnels through ...
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end of semester main examination - UR-CST

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... the fatty acids from which they are derived but they make up for this deficiency by serving as “water-soluble lipids” that can be more readily transported in the blood plasma. During starvation, ketone bodies are produced in large amounts becoming substitutes for glucose as the principal fuel for br ...
Poster - University of Waterloo
Poster - University of Waterloo

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... This topic begins with detail of protein biochemistry with focus also being on enzyme activity with reference to the blood clotting process. Students will have the opportunity to make molecular representations of key biochemicals to demonstrate their understanding of the basic structure of amino aci ...
Nucleic acid engineering
Nucleic acid engineering

Journal of Molecular Microbiology and Biotechnology
Journal of Molecular Microbiology and Biotechnology

... teins of the peptide synthetases involved in non-ribosomal peptide biosynthesis is reflected in its genetic organization following the colinearity rule [Guenzi et al., 1998]. Cyclic lipopeptides as surfactin, fengycin, and iturin-like antibiotics are widely spread in B. subtilis and related strains ...
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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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