1) Sketch out the schematic diagram for the enzymatic mechanism of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) Please provide the structure of the functional groups of the substrate and enzyme involved in the reaction at each step (rest of the structure can be indicated as R) Indicate clearly the flow of the electrons at each step Indicate in short form the cofactor involved and the acid or basic groups of the enzyme involved
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1) Sketch out the schematic diagram for the enzymatic mechanism of glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
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- Please provide the structure of the functional groups of the substrate and enzyme involved in the reaction at each step (rest of the structure can be indicated as R)
- Indicate clearly the flow of the electrons at each step
- Indicate in short form the cofactor involved and the acid or basic groups of the enzyme involved
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- Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.Extending the Mechanism of Methylmalonyl-CoA Mutase to Similar Reactions Based on the mechanism for the methylmalonyl-CoA mutase (see problem 14), write reasonable mechanisms for the following reactions shown.The Reactions and Meehanisms of the Leloir Pathway Write the reactions that permit galactose to be utilized in glycolysis. Write a suitable mechanism, tor one of these reactions.
- Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described. _____________________1. Name: alkaline phosphataseReaction: a phosphate monoester + H2O = an alcohol + phosphate_____________________2. Reaction: L-threonine = D-threonine.Other information: Inverts both chiral centers, a racemase. _____________________3. Name: glycine-N-acylaseReaction: acyl-COA + glycine = CoA + N-acylglycine_____________________ 4. Name: lysine decarboxylaseReaction: L-lysine = cadaverine + CO2 _____________________5. Name: methanol dehydrogenaseReaction: methanol + NAD+ = formaldehyde + NADH + H+ _____________________6. Name: citryl-CoA synthetaseReaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA_____________________7. Name: D-xylulose reductaseReaction: xylitol + NAD+ = D-xylulose + NADH + H+ _____________________8. Name: cellobiose phosphorylaseReaction: cellobiose phosphate =…In Bacillus subtilis, threonine is metabolized by the following sequence of reactions: (a) oxidation; (b) decarboxylation;(c) transamination; and (d) oxidation to produce pyruvate. Outline this sequence of steps, show the structures of thesubstances, use abbreviations for the cofactors, and show any enzyme-bound coenzymes. What type of enzyme bound intermediate is likely for reaction (d)?
- Sketch out the schematic diagram for the enzymatic mechanism of pyruvate dehydrogenase complex Please provide the structure of the functional groups of the substrate and enzyme involved in the reaction at each step (rest of the structure can be indicated as R) Indicate clearly the flow of electrons in the E-1 and E-2 reaction Indicate in short form the cofactor involvedDraw the Fischer projection of galactcose and show its catabolism until it releases carbon dioxide via complete oxidation. Use inter-related reactions or pathways, correct names and number of moles of intermediates involved, and the enzymes catalyzing the reactions. Account for all the 6 carbons of thr monosaccharide as they become carbon dioxide by encircling them all throughout the pathway you have writteOrder the cofactors based on their use in the mechanism of the a-etogluterate dehydrogenase complex. 1. Stabilizes a carbanion due to decarboxylation 2. Allows for the splitting of the carbon skeleton from the electron pair generated in a redox reaction 3. Enzyme bond electron carrier that is part of dihydrolipoyl dehydrogenase 4. Final electron acceptor in the overall reaction catalyzed by this complex 1 2 3 4 answer choices: lipoamide, biotin, 2 Fe - 2S cluster, TPP, NAD+, FAD
- With regard to the glyceraldehyde-3-phosphate dehydrogenase enzyme reaction:a) Write the mechanism of the reaction.b) What two enzyme intermediates are involved? One undergoes an oxidation-reduction step.What is oxidized and what is reduced? How are the electrons transferred? The secondintermediate has some different chemistry than usual esters. Comment.c) What factors are operating here to bring about the catalysis that this enzyme carries out?d) The product of this reaction is “rather special”. CommentIn order to function as an oxidative phosphorylation uncoupler, 2,4-dinitrophenol must act catalytically, not stoichiometrically. What does this mean? Identify and discuss an important implication of this conclusion.Aminolevulinate (ALA) synthase is a pyridoxal phosphate containing enzyme displaying a non-sequential (ping-pong) enzyme mechanism. It catalyses the reaction: glycine + succinyl-CoA ⇌ aminolevulinate + CO2 Draw a Cleland diagram (diagram illustrating when the substrates and products form an enzyme substrate complex) for this reaction if glycine is the first substrate to bind.