Please, explain and write about what type of evidence, biochemically, led to the cyclic nature of the glyoxylate pathway?
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Chemistry
Please, explain and write about what type of evidence, biochemically, led to the cyclic nature of the glyoxylate pathway?
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- Inquiry and Analysis Do Enzymes Physically Attach to Their Substrates? When scientists first began to examine the chemical activities of organisms, no one knew that biochemical reactions were catalyzed by enzymes. The first enzyme was discovered in 1833 by French chemist Anselme Payen. He was studying how beer is made from barley: First, barley is pressed and gently heated so its starches break down into simple two-sugar units; then yeasts convert these units into ethanol. Payen found that the initial breakdown requires a chemical factor that is not alive and that does not seem to be used up during the process-a catalyst. He called this first enzyme diastase (we call it amylase today). Did this catalyst operate at a distance, increasing the reaction rate all around it, much as raising the temperature of nearby molecules might do? Or did it use physical contact, actually attaching to the molecules whose reaction it catalyzed (its "substrate")? The answer was discovered in 1903 by French…. Explain what is meant by the term, “high energy compound”. Name a thioester molecule that is commonly found in biochemical reactions. Explain why thioesters are “high energy” compounds. Describe the molecular structure of cellulose. How does this structure explain why cellulose forms strong fibers? Explain why digestion of cellulose takes a long time even when catalyzed by an enzyme. The enzyme phosphofructokinase transfers a phosphate from ATP to the hydroxyl group a C1 of fructose. Similar to fructose, water also has a hydroxyl group and the concentration of water is much higher than that of fructose. Explain why the phosphate is transferred to fructose and not to water.Using the Acronym LILHOT, give the 6 major families of enzymes found in biological systems
- Integration of Metabolism Complete the interrelated pathways by providing the necessary metabolite, enzyme, and reaction or metabolic pathway. Abbreviations and acronyms for pathways, metabolites, products and enzymes will not be accepted (For coenzymes, you may use abbreviations/acronyms). Fill the blank in numbers 1-20Search for a structure of one common drug that is available locally. Draw the structure of the drug and label the functional group/s found on the structure. You can use different color of pen if you wish to. Place it on a clean paper. Search for the metabolic of that particular drug, identify which Phase 1 or phase 2 metabolism it will undergo by illustrating the metabolite after metabolism. Make a brief discussion about it - handwritten - please write legibly,pluginfile.php/7382296/mod_resource/content/0/Purine%20Practice%20Pathway.pdf 1 / 1 67% Purine * Know regulatory steps Synthesis *Know how GTP and ATP control production O D-O O-0 R-5 P 5-phosphoribas ylamine EZ 9 oteps IMP ロロ AMP GMP E3 ES E7 LADP E4 Eb ATP JATP GTP typ
- Explore the difference etween amylopectin and glycogen. Be sure to highlight what structural modifications in the molecules as it relates to their localization in different organisms (structure-function relationship).BIOCHEMISTRY QUESTION The initial rate (VO) data as a function of substrate concentration [S] for an enzyme (Enzyme1) that obeys Michaelis-Menten kinetics are shown in the table below. The total enzyme concentration is 2.5 nM. [S](μm) 16.0 8.0 4.0 2.0 1.0 v (μMsec ¹) 48.5 32.7 19.8 11.1 5.88 (a) Calculate KM for the enzyme, using the estimated slope (slope = (y2-y1)/(x2-x1)) from a Lineweaver-Burk plot. Show your work and don't forget the units! (b) When the enzyme concentration is 2.5 nM, a Lineweaver-Burk plot of this data gives a line with a y- intercept of 0.0106 μ M-1 sec. Calculate kcat for the enzyme. (Show your work and don't forget to include units). (c) A second enzyme (Enzyme2) also obeys Michaelis-Menten kinetics. Its kcat and KM are 800 sec-1 and 5 µM, respectively. Which is the more efficient enzyme? Briefly explain d) Is Enzyme 1 diffusion limited? Explain.Identification of the active site of an enzyme - which methods do scientists use today to identify the active site?
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