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Ch. 2-4 Review
Ch. 2-4 Review

... d. It causes the enzyme to break up. e. It decreases the chance that the enzyme will meet a substrate molecule. 7. An enzyme is specific. This means a. it has a certain amino acid sequence. b. it is found only in a certain place. c. it functions only under certain environmental conditions. d. it spe ...
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... The resultant particle consists of a cluster of two or more atoms strongly bound together known as a molecule. When there is more than one type of atom present, the compound produced is termed a molecular compound. The net electrostatic force of attraction between the atoms in the molecule is termed ...
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... Quarternary structure of proteins Allosteric interactions Multiple Choice 1) The role of an enzyme in an enzyme-catalyzed reaction is to A) bind a transition state intermediate, such that it can be converted back to a substrate B) ensure that all substrate is converted to product C) ensure that prod ...
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... Important coenzymes: Pyridoxal phosphate (derived from vitamin B6) is the quintessential coenzyme of amino acid metabolism. In degradation, it is involved in the removal of amino groups, principally through transamination reactions and in donation of amino groups for various amino acid biosynthetic ...
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... 1. Use Figure 22.3 to determine which template strand DNA sequence (written in  the 5' → 3' direc on) specifies the tripeptide with the sequence gly‐ala‐leu. A) GGGGCTCTC  B) CTCTCGGGG  C) CCCCGAGAG  D) GAGAGCCCC  2. Which is not true about the genetic code?  A) Some amino acids share the same codon ...
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Final Exam - UC Davis Plant Sciences
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... This exam consists of 8 questions. A maximum of 100 points can be earned. Partial credit will be given. There are a total of 12 pages, including the cover page and one blank sheet at the end for notes. However, do not use the blank sheet for your final answers. If you need more space, use the back o ...
Catabolism
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... Carbohydrates and other nutrients serve two functions in the metabolism of heterotrophic microorganisms: 1. They are oxidized to release energy 2. They supply carbon or building blocks for the synthesis of new cell constituents. • Amphibolic pathways: function both catabolically and anabolically ...
Introduction to Protein Structure
Introduction to Protein Structure

... After binding the two substrates, the enzyme may need to change its shape in order to position them closer together. In addition, the chemistry may need to be protected from the aqueous environment -for example, a charged molecule may be more attracted to water than to the second molecule involved i ...
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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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