The enzyme Glucose-6-phosphate dehydrogenase catalyzes the nicotinamide adenine dinucleotide oxidation of cyclic glucose-6-phosphate to form the lactone product shown below. Propose a mechanism for this reaction showing all electron flow (using the arrow convention). You must draw the substrate glucose-6-phosphate (the configuration of the anomeric carbon does not matter) and the “business end” of the cofactor.
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The enzyme Glucose-6-phosphate dehydrogenase catalyzes the nicotinamide adenine dinucleotide oxidation of cyclic glucose-6-phosphate to form the lactone product shown below. Propose a mechanism for this reaction showing all electron flow (using the arrow convention). You must draw the substrate glucose-6-phosphate (the configuration of the anomeric carbon does not matter) and the “business end” of the
cofactor.
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- In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly. Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.There is another class of aldolase enzymes known as Class II. These enzymes are found in fungi, algae, and some bacteria. This class differs for Class I in that these enzymes do not have a Lys residue associated with their active sites, but contain a divalent cation (usually Zn2+ or Fe2+) in the active site. Outline a possible mechanism for a Class II aldolase and explain the function of the metal ion in the reaction.
- The reaction catalyzed by phosphorylase is readily reversible in vitro. At pH 6.8, the equilibrium ratio of orthophosphate to glucose 1-phosphate is 3.6. The value of ΔG°’ for this reaction is small because a glycosidic bond is replaced by a phosphoryl ester bond that has a nearly equal transfer potential. However, phosphorolysis proceeds far in the direction of glycogen breakdown in vivo. Suggest one means by which the reaction can be made irreversible in vivo.The purinosome contains enzymes that convert the serine hydroxymethyl group to the formyl group of 10-formyltetrahydrofolate. Write a balanced equation for each reaction in this conversion.Explain the basis for the following statement. For efficient conver- sion of galactose to glucose-1-phosphate, UDP-glucose need be present in catalytic amounts only.
- In the pyrimidine degradative pathway, all pyrimidines undergo conversion to uracil, which undergoes an NADPH-dependent reduction. Show plausible reactions leading from cytidine, cytosine, and uridine to uracil, and write a plausible structure for the product of uracil reduction (dihydrouracil).In the hydrolysis of ATP to ADP and Pi, the equilibrium concentration of ATP is too small to be measured accurately. A better way of determining K’eq, and hence ΔG◦’ of this reaction, is to break it up into two steps whose values of ΔG◦’ can be accurately determined. This has been done using the following pair of reactions (the first being catalyzed by glutamine synthetase): (1) ATP + glutamate + NH3 ⇌ ADP + Pi + glutamine + H+ ΔG1◦’= -16.3 kJ/mol (2) glutamate + NH3 ⇌ glutamine + H2O + H+ ΔG2◦’= 14.2 kJ/mol What is the ΔG◦’ of ATP hydrolysis according to these data and is the overall reaction spontaneous? What is the value of the equilibrium constant for the overall reaction at 25.0 °C. If the concentration of ATP at equilibrium is 20.0 mM and the concentration of ADP at equilibrium is 50 nM. What is the concentration the phosphate group (in mM) at equilibrium?Using the principles described in the text regarding pyridoxal phosphate mechanisms, propose a mechanism for the reaction catalyzed by serine hydroxymethyltransferase.
- In humans, the biosynthesis of L-glutamine is catalyzed by the L-glutamine synthetase. The global reaction can be written as follows: ATP + glutamate + NH3 ADP + phosphate + glutamine The A,Gº' value for this reaction is -16.3 kJ.mol-1 (from left to right). 1- Explain the significance this information. 2- This reaction can be considered as the sum of two component reactions which are exergonic and endergonic, respectively, under standard conditions. Write these two component reactions and evaluate A,Gº of the endergonic reaction. Data: A,Gº of ATP hydrolysis = -30.4 kJ mol-¹Consider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). I. For one mole of the fatty acid residue, determine the following: b. What is the number of ATP yield obtained from NADH coming from the complete β-oxidation of the fatty acid residueThe high phosphoryl transfer potential of 1,3-bisphosphoglycerate is explained by the resonance stability of the product, 3-phosphoglycerate. The same explanation applies to the reaction that generates resonance stabilized pyruvate from phosphoenolpyruvate. Show the resonance structures for both products, 3-phosphoglycerate and pyruvate, and state why the reactant in both reactions is not resonance stabilized.