1. Shown below is the intermediate in the aldolase mechanism, after dissociation of the firstproduct (GA-3P). Draw resonance structure of this intermediate showing the carbanion speciesAND the arrow movement that associated with formation of this resonance structure.CH₂OPO²-H 1Lys-N-C||-B-H:A-H-BCovalent enzyme-enamine intermediate

When drawing chemical reaction mechanisms, we use a curved arrow to show the flow of electrons. The…

Answered: 1. Shown below is the intermediate in…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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NH3 H-SCO A LES NH CH₂ NH CH₂ CH₂ 3 H-SCO A H3C SCO A 5. Describe the role of His in the catalytic mechanism shown.
Interestingly, the most common treatment for methanol poisoning is to use ethanol as an antidote. Why would adding large amounts of ethanol help slow down the rate of formic acid production by aldehyde dehydrogenase?
Order 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
Suggest a name for an enzymes that catalyzes each of the following reactions.1. Hydrolysis of Lactose 2. Oxidation of Nitrate3. Decarboxylation of Citrate4. Reduction of Exalate
In many biochemical reactions which involves the formation of an enolate intermediate, the carbonyl oxygen of the substrate is coordinated to a divalent metal ion (usually zinc or magnesium) in the active site. Explain with structural drawings, how this ion-dipole interactions affect the acidity of the a-protons?
Refer to Table to explain why FAD rather than NAD+ is used in the succinate dehydrogenase reaction.
1. In a catabolic pathway, metabolite X gets converted into metabolite Y, metabolite X 0 J mol-¹ and AG' is <0 J mol-¹ for this reaction. a) At standard states, is this reaction favorable? b) Is the reaction favorable or unfavorable at cellular condition? c) Is this an endergonic or exergonic reaction in the cell? d) Would you describe this as a thermodynamically downhill or uphill reaction in the cell?
What if C-1 of the oxaloacetate were labeled instead, when would the label be released as CO2?
Match the following catalytic strategies with their example. Place a Letter on the picture. There are only two examples given. CH2OH CH2OH CH2OH CH2OH он он OH OH + H20 OH OH OH но H. но но OH OH OH OH OH OH A. Oxidoreducatase B. Transferase C. Hydrolase D. Lyase NH3 E. Isomerase F. Ligase R-CH-COO "ooc-CH2-CH2-C-COO Amino acid a-Ketoglutarate
The enzyme enolase has a permanently bound Mg2+ ion in its active site. To the below is a schematic of the enzyme active site bound to an intermediate of the reaction. Which of the following are true? (Pick two.) PO32- Н Mg2 C C H HO Favorable electrostatic interactions (dashed blue lines) between Mg2+ and the intermediate increase (make it more positive) the AG of the reaction. Favorable electrostatic interactions (dashed blue lines) between Mg2+ and the intermediate decrease (make it more negative) the AG of the reaction. Favorable electrostatic interactions between Mg2+ and the intermediate decrease the rate constant, k, of the reaction, decreasing the rate of the reaction. Favorable electrostatic interactions between Mg2+ and the intermediate increase the rate constant, k, of the reaction, increasing the rate of the reaction.
The enzyme which catalyzes the reaction below belongs to which enzyme classification? Н.С— ОН HC=0 C=0 Н-С—ОН H,C-0-P-o- || H,C –0-P-0- O Transfera Hydrolase Isomerase Oxidoreductase
What 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

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