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Topic guide 1.2: Enzymes
Topic guide 1.2: Enzymes

... Applying heat energy to molecules increases their kinetic energy so there will be an increased number of collisions between enzyme and substrate molecules. This in turn will increase the rate of reaction and so the products will be formed more quickly. However, applying too much heat can cause enzym ...
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pdf-download

... corresponding back reaction. One example is the racemic resolution of amino acids like methionine to the desired enantiopure L-compounds. Another class of enzymes that can be found regularly in commercialised processes are the so-called oxidoreductases, enzymes that perform oxidation or reduction re ...
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Divergent Evolution of Function in the ROK Sugar
Divergent Evolution of Function in the ROK Sugar

... ABSTRACT: The D-allose and N-acetyl-D-mannosamine kinases of Escherichia coli K-12 are divergent members of the functionally diverse ROK (repressor, open reading frame, kinase) superfamily. Previous work in our laboratory has demonstrated that AlsK and NanK possess weak phosphoryl transfer activity ...
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Final Respiration

... Efficiency of Glycolysis • Compare the kilocalories of glucose with the kilocalories in the ATP that is made. • The 2 ATP molecules made during glycolysis account for only 2% of the energy in glucose • Where does the rest go? • It’s still in pyruvic acid • This small amount of energy is enough for ...
cellrespdiagrams
cellrespdiagrams

... Efficiency of Glycolysis • Compare the kilocalories of glucose with the kilocalories in the ATP that is made. • The 2 ATP molecules made during glycolysis account for only 2% of the energy in glucose • Where does the rest go? • It’s still in pyruvic acid • This small amount of energy is enough for ...
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... carbon, nitrogen, phosphorus and sulphur. This enables them to feed the central metabolic pathways — glycolysis, the pentose-phosphate pathway, the citric acid cycle and the 2‑oxoglutarate–glutamate–glutamine cycle — from which all of the precursors that are required for the synthesis of the cell’s ...
Final Respiration
Final Respiration

... Efficiency of Glycolysis • Compare the kilocalories of glucose with the kilocalories in the ATP that is made. • The 2 ATP molecules made during glycolysis account for only 2% of the energy in glucose • Where does the rest go? • It’s still in pyruvic acid • This small amount of energy is enough for ...
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... be charged with that amino acid. The amino acid is recognized on the basis of its side chain structure and chemistry. The correct tRNA is recognized as described above. Some of the Aminoacyl-tRNA Synthetases have proof reading capabilities. After the amino acid has been attached, some of these enzym ...
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cell respiration notes ap - Wesleyan
cell respiration notes ap - Wesleyan

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PDF Full-text

... peptide analogues include: phosphonamidates (X = NH, the closest TS analogues), phosphonates (X = O, pseudodepsipeptides) and phosphinates (X = CH2). All these compounds appear particularly effective in regulating the activity of metalloproteases. Nevertheless, investigation of other proteases (e.g. ...
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Amino Acid Composition in Fillets of Mirror Crossbreds Common

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... group of electron carriers (usually to NAD+ and FAD). Then, the electrons are passed through a series of different electron carriers to molecules of O2 or other oxidized inorganic and organic molecules. This process occurs in the plasma membrane of prokaryotes and in the inner mitochondrial membrane ...
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enhanced rate of ethanol elimination from blood after intravenous

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Chapter 15 Acids and Bases
Chapter 15 Acids and Bases

...  the H+ from the acid combines with the OH- from the base to make a molecule of H2O  it is often helpful to think of H2O as H-OH  the cation from the base combines with the anion from the acid to make a salt acid + base → salt + water HCl(aq) + NaOH(aq) → NaCl(aq) + H2O(l) H+(aq)+Cl-(aq)+Na+(aq)+ ...
A novel assay method for an amino acid racemase reaction based
A novel assay method for an amino acid racemase reaction based

... The new assay method established in the present study for the measurement of the catalytic activity of ALR is based on the CD spectra of both enantiomers of Ala. The method is highly quantitative and provides visible data that reflect the exhaustive reaction of ALR. We conclude that the CD assay met ...
Amino Acids, Proteins, and Enzymes
Amino Acids, Proteins, and Enzymes

... An enzyme in a pathway that controls the rate of the reaction. 2. PR Speeds up a reaction by combining with an enzyme in the pathway. 3. Z Removal of a peptide activates the enzyme. 4. FC Some product binds to the first enzyme to limit the synthesis of product. ...
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... phosphoric acid esters (phosphates). For example, glucose phosphorylation takes place with the participation of ATP and enzyme glucokinase: ...
Cell Respiration Notes Kelly
Cell Respiration Notes Kelly

... Regulated by phosphofructokinase ALLOSTERIC enzyme near beginning of pathway AMP turns pathway on (AMP is high when ATP is needed) ATP turns pathway off (don’t waste energy making ATP when not needed) ...
Cell Respiration Notes
Cell Respiration Notes

... Regulated by phosphofructokinase ALLOSTERIC enzyme near beginning of pathway AMP turns pathway on (AMP is high when ATP is needed) ATP turns pathway off (don’t waste energy making ATP when not needed) ...
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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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