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Microbiology 146:
Microbiology 146:

... strain utilized less succinate and glutamate and grew less with this and other amino acids as nitrogen source. R. etli assimilates ammonium by the glutamine synthetase (GS)-GOGAT pathway and a GOGAT mutant prevents the cycling of glutamine by this pathway, something that impairs nitrogen and carbon ...
Homology Claims
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... An isolated and purified nucleic acid comprising a nucleotide sequence that is 90% identical to SEQ ID NO: 1. An isolated and purified nucleic acid comprising a nucleotide sequence that is 90% identical to SEQ ID NO: 1, wherein said nucleic acid encodes a protein having activity X. ...
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... Once inside the mitochondrial matrix, pyruvate is decarboxylated in an oxidation reaction by the enzyme pyruvate dehydrogenase (PDH). The products are NADH (from NAD+), CO2, and acetic acid in the form of acetyl-CoA, in which a thioester bond links the acetic acid to a sulfur-containing cofactor, co ...
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Gluconeogenesis - Assignment Point
Gluconeogenesis - Assignment Point

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Chemistry -- Acids and Bases
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Chapter 3: The Chemical Basis for Life Lesson 3.2: Organic
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... usually occur within organic compounds in smaller groups of elements called functional groups. When organic compounds react with other compounds, generally just the functional groups are involved. Therefore, functional groups generally determine the nature and functions of organic compounds. You can ...
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Chemical Biology - Chem 370 (3 credits)
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... graduate and professional programs requirements, more advanced coursework, and research needs. The first half of the course will focus on structure and function of the chemistry of biological systems while the second half of the course will concentrate on metabolic cycles and energy production. This ...
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... the strongest inter-strand stability because it allows the inter-strand hydrogen bonds between carbonyls and amines to be planar, which is their preferred orientation. ...
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... found in energy levels outside the nucleus. They are likely to be found in certain levels, but may change levels when energy is absorbed or given off. The number of electrons can change in atoms. ( P=E) Go to ...
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The final publication is available at Copyright - RiuNet

... the results given by Atuoi et al. [10] and Gorjanovic et al. [11] for tea and herbal teas [12,13], and by ...
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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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