MATCH a structure or term from the following list with each description below. Place the letter of the structure or term in the blank to the left of the description. The reactive electrophile in Friedel-Crafts acylation reactions. [Choose ] R3C+ The electrophile in aromatic +NO2 nitration. electron-withdrawing +NO Groups which activate aromatic rings towards electrophilic substitution. Groups which activate aromatic rings towards nucleophilic substitution. electron-donating benzyne Meisenheimer complex [Choose ] Intermediate in the elimination- addition mechanism of nucleophilic aromatic substitution. [Choose ]
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- In the biosynthesis of heme, ring cyclization, isomerization, and decarboxylation reactions take place. Identify the potential intermediates and show the electron flow in the following diagram. HO,C R1 HO2C- -R2 NH HN- но- NH HN- HO2C R R2 unstable intermediate Uro'gen II HO2C Me Me NH HN- -CO2H HN NH Me Me HO2C CO2H Coproporphyrinogen IIConsider the following structure. CO₂CH2CH3 CO₂CH2CH3 This substance could be produced by the reaction of the following diene and dienophile. diene + dienophile H CO,CH,CH3 སངས་ CH3CH₂O₂C True Falseguanosine and a water bind in the active site, does not matter in which order. The scissile N-1 glycosidic bond between the anomeric carbon and N9 of the base is broken resulting in an oxocarbenium transition state. The leaving group electrons are not protonated, but instead swing up to form a double bond between N9 and C8. The double bond that is already present on the purine swings out on N7 and is protonated by an active site histidine acting as a general acid. An active site aspartate acts as a general base, and deprotonates the water substrate molecule. The deprotonated water is then free to attack the transition state in a manner that will generate an αribose. Draw the active site and show how the mechanism works. You will need to draw 3 or 4 different active site “snap-shots” to show the entire process. Be sure to clearly show the transition state and how it might be stabilized
- One of the steps in psilocybin biosynthesis is the phosphorylation of 4-hydroxytryptamine By the enzyme Psik as shown below, that involves the hydrolysis of ATP. NH₂ OH HO Psik HO of A& ADP 4-hydroxytryptamine ATP norbaeocystin The standard free energy changes for each reaction is shown in the Table below. J reaction 4-hydroxytryptamine + P₁ → norbaeocystin ATP → ADP+ Pi (b) What is the equilibrium constant at 37 °C? AG 27.7 kJ/mol -32.2 kJ/mol (a) Write the net reaction. What is the standard free energy change for the net reaction? (c) In the cell, the concentration of ATP is 3.1 mM, the concentration of P; Is 5.90 mM, and the Concentration of ADP is 220 μM. What will AG Be if the concentration of norbaeocystin Is always kept at 1/100 of the concentration of 4-hydroxytryptamine?Give an electrophilic addition reaction involving a coenzymeWhich of the following statement is CORRECT? O Hydrolysis of starch into glucose in an elimination reaction Group transfer reaction is a nucleophilic substitution reaction Conversion of 3-phosphoglycerate to 2-phosphoglycerate is a group transfer reaction Most biochemical reaction occurs via homolytic cleavage Electrophiles are electron-rich, while nucleophiles are electron-deficient
- t In the enolase reaction, the Lys 345 and Glu 211 residues participate in the reaction to convert 2-phosphoglycerate (2-PGA) to phosphoenolpyruvate (PEP). Based on the reaction scheme shown in the figure below, which statement below best describes the roles of Lys 345 and Glu 211 in the enolase reaction? Lys345 Mg² Mg O=P-OH -H O-H Glu211 Enolate intermediate NH3 Mg Mg 01P-O -H H₂O NH3 Mg Mg FCH₂ 0=Write the correct order of the following structures: To select the correct order start from the first steps of the primary metabolite. A В 1 Shikmic acid corismic acid 3 tyrosine 4 para-hydroxyphenylpyruvic acid 5 3-deyhydroqunic acid prephenic acid 7 erthrose-4-phosphate 8 photosynthesis 9. CO2 10 cynogenic glycosideGiven the active site diagram below, which best described the mechanism(s) of Active Site `NH2. SH OH - catalysis? NH -Mg²+ O Acid-Base O Acid-Base & Metal lon Covalent Catalysis Acid-Base & Covalent Catalysis O Metal lon
- Given the active site diagram below, indicate the mechanism(s) of catalysis. 5 HO OH HN OH ΝΗ *HN ΝΗ Zn²+ Acid-base, Metal ion 3 Metal ion, By Approximation Metal ion Acid-Base, By Approximation Acid-baseGiven the active site below, which best describes the mechanism(s) of catalysis? 5 NH* 2 -N +H3N. HN Mn²+ H₂ Covalent Catalysis By Approximation Mn²+ -3 Metal ion, By Approximation Acid-Base, Metal ion Acid-Base, Metal ion, By ApproximationGiven the active site below, which best describes the mechanism(s) of catalysis? 5 NH+ 2 HN H₂ 03 NH Mn²+ -3 O Covalent Catalysis Metal ion, By Approximation O Acid-Base, Metal ion By Approximation Acid-Base, Metal ion, By Approximation