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 & 4-hydroxytryptamine ATP Psik ADP HO HO norbaeocystin The standard free energy changes for each reaction is shown in the Table below. AG 27.7 kJ/mol -32.2 kJ/mol (b) What is the equilibrium constant at 37 °C? reaction 4-hydroxytryptamine + P→ norbaeocystin ATP → ADP+ Pi (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?
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- Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?Which cytochrome P450-catalyzed reaction is shown below? R-CH2NH2 [R-CH=NH] Oxidation of aromatic amines Oxidative deamination Oxidative O-dealkylation Oxidative N-dealkylation para-hydroxylation R-CHO + NH3ATCase catalyzes the conversion of carbamoyl phosphate and aspartate into N-carbamoylaspartate, a precursor in pyrimidine biosynthesis. What roles do ATP and CTP play in this reaction? uncompetitive inhibitors heterotropic modulators homotropic modulators mixed inhibitors
- Match each of the enzymes involved in de novo pyrimidine synthesis with the correct description: _______ Dihydroorotate dehydrogenase _______ UMP synthase_______ Carbamoyl phosphate synthetase II _______ TMP synthase _______ CTP synthetase_______ Aspartate transcarbamoylase _______ PRPP synthetase (A) attaches an aspartate to an activated carbamoyl molecule(B) bifunctional enzyme that combines a nitrogenase pyrimidine ring to an activated ribose(C) catalyzes the formation of the activated ribose sugar(D) uses glutamine to add an amine to a preformed nucleotide(E) produces the first cyclic nitrogenase ring during de novo pyrimidine synthesis(F) combines bicarbonate and nitrogen from glutamine in the first step of pyrimidine ring synthesis (G) uses a folate derivative to add a methyl group to a preformed nucleotideBelow is an image of the Krebs cycle: acetyl-CoA oxaloacetate COASH H20 NADH NAD* H20 malate citrate fumarate isocitrate FADH2 NAD* CO2 FAD АТР NADH + ADP succinate GTP NAD+ a-ketoglutarate H20 GDP NADH + CO2 COASH succinyl CoA COASH Consider the conversion of succinate to fumarate, which is coupled with the production the electron carrier FADH2. If this reaction was NOT coupled with the production of FADH2 (and only catalyzed the conversion of succinate to fumarate), how would this impact ATP production through cell respiration? OATP production would stop because no high energy electron carriers would be produced ATP production would still occur, but there would be a much lower ATP yield because a large number of electron carriers are no longer being made ATP production would stop because without FADH2 we will no longer have electrons moving through the electron transport chain ATP production would still occur, but there would be a slightly lower ATP yield because a small number of…A schematic representation of the enzyme IspD complexed to inhibitor 3, and a series of inhibitors 3-5 are shown below. Ala202 lle240 mwww NH NH Val263 ОН www HN N- lle177 HN 'N' CI 3 X = N 4 X = C-CN 5 X = C-COO IC50 274 µM IC50 140 nM IC50 35 nM NH2 HN Val266 N -N O-H---- N HN %3D Arg157 HN wwww lle265 Explain why structure 4 is a more potent inhibitor (lower IC50 value) than inhibitor 3 and why structure 5 is a much weaker inhibitor (higher IC50 value) than 3 and 4.
- Describe the biochemical role of coenzyme Q10 and how supplementation may impact metabolism. Be sure to address the key terms listed below as part of your discussion; you may address additional etiologies as well. coenzyme Q Complex I Complex II Complex III ubiquinone ubiquinol Electron transport chain Oxidative phosphorylation Reactive oxygen species1) Tabulate the differences and/ or similarities of the different kinds of coenzymes and cofactors. Structure Source ATP SAM COA Retinal THF- tetrahydrofolate Vitamin K NAD, NADP FMN, FAD TPP PLP Adenosylcobalamin methylcobalamin and Function/ Role/ ImportanceIn this step of purine biosynthesis, which functional group gets activated by ATP Pribose NH, ATP Carboxyaminolmidazole ribonedeotide Asp AD Fumarate Pribose NH, S-Aminolmidazole- 4(N-succinylcarboxamide) ribonucleotide O Carboxyaminoimidazole ribonucleotide COOH O Carboxyaminoimidazole ribonucleotide NH2 O Asp side chain COOH O Asp main chain NH2 O Asp main chain COOH
- Transamination reactions typically involve which of the following (select all that apply)? O almidine linkage/Schiff base O biotin O alpha-keto acid O pyridoxal phosphate zymogens O glutamate dehydrogenaseRefer to the figure below: -Adenosine COAS The thiolate anion of CoA acts as a/an nucleophile attacking the carbonyl carbon of the enzyme bound intermediate, displacing AMP and forming a fatty acyl CoA. Which of the following glycolytic intermediates could be regarded as a high-energy molecule? Dihydroxyacetone phosphate Phosphoenolpyruvate Fructose 6-phosphate 3-PhosphoglycerateWhat is X in the following biochemical pathway? RH NH₂+ A. R CH a-ketoglutarate CH3 coenzyme PLP coenzyme TPP aminotransferase decarboxylase D. glutamate R B. NH X R E. 0 R C. CH CO₂ I OH R. H H